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51001
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51002
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51003
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51004
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51005
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51006
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51007
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51008
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51009
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Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the ...
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51010
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51011
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51012
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51013
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51014
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51015
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51016
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51017
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51018
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51019
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51020
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51021
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51022
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51023
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51024
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51025
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51026
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51027
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51028
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51029
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51030
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51031
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51032
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51033
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51034
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51035
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51036
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51037
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51038
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51039
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51040
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51041
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51042
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51043
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51044
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51045
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51046
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51047
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51048
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51049
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51050
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51051
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51052
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51053
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51054
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51055
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51056
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51057
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51058
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51059
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51060
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51061
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51062
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51063
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51064
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51065
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51066
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51067
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51068
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51069
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51070
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51071
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51072
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Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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51073
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51074
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51075
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51076
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51077
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51078
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51079
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51080
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51081
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51082
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51083
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51084
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51085
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51086
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51087
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51088
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51089
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51090
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51091
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51092
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51093
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51094
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51095
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51096
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51097
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51098
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51099
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51100
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51101
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51102
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51103
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51104
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51105
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Nitric-oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and carbon ...
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51106
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51107
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51108
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51109
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51110
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51111
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51112
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51113
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51114
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51115
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51116
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51117
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51118
|
Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51119
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51120
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51121
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51122
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51123
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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51124
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51125
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51126
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Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
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|
51127
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Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions
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51128
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Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions
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51129
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Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions
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51130
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Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions
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51131
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Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase ...
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51132
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Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase ...
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|
51133
|
Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase ...
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51134
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Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase ...
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51135
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Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during ...
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51136
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Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during ...
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51137
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Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during ...
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|
51138
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Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during ...
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51139
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Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during ...
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51140
|
Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during ...
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|
51141
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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51142
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Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51143
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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|
51144
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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|
51145
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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|
51146
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51147
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51148
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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|
51149
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51150
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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|
51151
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51152
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51153
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51154
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
|
|
51155
|
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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51156
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Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana.
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|
51157
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
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51158
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His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
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51159
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His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
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51160
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
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51161
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51162
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51163
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51164
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51165
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51166
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51167
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51168
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51169
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51170
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51171
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51172
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51173
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51174
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51175
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51176
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51177
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51178
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51179
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51180
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51181
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51182
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51183
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51184
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51185
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51186
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51187
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51188
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51189
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51190
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51191
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51192
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51193
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51194
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51195
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51196
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51197
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51198
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51199
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51200
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51201
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51202
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51203
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51204
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51205
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51206
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51207
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51208
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51209
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51210
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51211
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51212
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51213
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51214
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51215
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51216
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51217
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51218
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51219
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51220
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51221
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51222
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51223
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51224
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51225
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51226
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51227
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51228
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51229
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51230
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51231
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51232
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51233
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51234
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51235
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51236
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51237
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51238
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51239
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51240
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51241
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51242
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51243
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51244
|
His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition ...
|
|
51245
|
Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted ...
|
|
51246
|
Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted ...
|
|
51247
|
Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted ...
|
|
51248
|
Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted ...
|
|
51249
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51250
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51251
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51252
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51253
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51254
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51255
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51256
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51257
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51258
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51259
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51260
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51261
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51262
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51263
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51264
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51265
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51266
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51267
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51268
|
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, ...
|
|
51269
|
Purification and characterization of a recombinant alpha-N-acetylgalactosaminidase from Clostridium ...
|
|
51270
|
Purification and characterization of a recombinant alpha-N-acetylgalactosaminidase from Clostridium ...
|
|
51271
|
A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene ...
|
|
51272
|
A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene ...
|
|
51273
|
A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene ...
|
|
51274
|
A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene ...
|
|
51275
|
Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus ...
|
|
51276
|
Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus ...
|
|
51277
|
Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus ...
|
|
51278
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51279
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51280
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51281
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51282
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51283
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51284
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51285
|
Unexpected Divergence of Enzyme Function and Sequence: "N-Acylamino Acid Racemase" Is o-Succinylbenzoate ...
|
|
51286
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51287
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51288
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51289
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51290
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51291
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51292
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51293
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51294
|
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site ...
|
|
51295
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51296
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51297
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51298
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51299
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51300
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51301
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51302
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51303
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51304
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51305
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51306
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51307
|
Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase ...
|
|
51308
|
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
|
|
51309
|
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
|
|
51310
|
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
|
|
51311
|
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
|
|
51312
|
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
|
|
51313
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51314
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51315
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51316
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51317
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51318
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51319
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51320
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51321
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51322
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51323
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51324
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51325
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51326
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51327
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51328
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51329
|
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications ...
|
|
51330
|
GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase
|
|
51331
|
GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase
|
|
51332
|
GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase
|
|
51333
|
GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase
|
|
51334
|
GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase
|
|
51335
|
GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase
|
|
51336
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51337
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51338
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51339
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51340
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51341
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51342
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51343
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51344
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51345
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51346
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51347
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51348
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51349
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51350
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51351
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51352
|
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
|
|
51353
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51354
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51355
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51356
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51357
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51358
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51359
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51360
|
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development.
|
|
51361
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51362
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51363
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51364
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51365
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51366
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51367
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51368
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51369
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51370
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51371
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51372
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51373
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51374
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51375
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51376
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51377
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51378
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51379
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51380
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51381
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51382
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51383
|
Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
|
|
51384
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51385
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51386
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51387
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51388
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51389
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51390
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51391
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51392
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51393
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51394
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51395
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51396
|
Kinetic and molecular properties of Bacillus subtilis IBTC-3 subtilisin
|
|
51397
|
The missing step of the L-galactose pathway of ascorbate biosynthesis in plants, an L-galactose ...
|
|
51398
|
The missing step of the L-galactose pathway of ascorbate biosynthesis in plants, an L-galactose ...
|
|
51399
|
The missing step of the L-galactose pathway of ascorbate biosynthesis in plants, an L-galactose ...
|
|
51400
|
X-ray, NMR, and mutational studies of the catalytic cycle of the GDP-mannose mannosyl hydrolase reaction
|
|
51401
|
X-ray, NMR, and mutational studies of the catalytic cycle of the GDP-mannose mannosyl hydrolase reaction
|
|
51402
|
Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila ...
|
|
51403
|
Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila ...
|
|
51404
|
Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila ...
|
|
51405
|
Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison ...
|
|
51406
|
Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison ...
|
|
51407
|
Cytokinin-deficient transgenic Arabidopsis plants show multiple developmental alterations indicating opposite ...
|
|
51408
|
Cytokinin-deficient transgenic Arabidopsis plants show multiple developmental alterations indicating opposite ...
|
|
51409
|
Cytokinin-deficient transgenic Arabidopsis plants show multiple developmental alterations indicating opposite ...
|
|
51410
|
Cytokinin-deficient transgenic Arabidopsis plants show multiple developmental alterations indicating opposite ...
|
|
51411
|
Formamide probes a role for water in the catalytic cycle of cytochrome c oxidase
|
|
51412
|
Formamide probes a role for water in the catalytic cycle of cytochrome c oxidase
|
|
51413
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51414
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51415
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51416
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51417
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51418
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51419
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51420
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51421
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51422
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51423
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51424
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51425
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51426
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51427
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51428
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51429
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51430
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51431
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51432
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51433
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51434
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51435
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51436
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51437
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51438
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51439
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51440
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51441
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51442
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51443
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51444
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51445
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51446
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51447
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51448
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51449
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51450
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51451
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51452
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51453
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51454
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51455
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51456
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51457
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51458
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51459
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51460
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51461
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51462
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51463
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51464
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51465
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51466
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51467
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51468
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51469
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51470
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51471
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51472
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51473
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51474
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51475
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51476
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51477
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51478
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51479
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51480
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51481
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51482
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51483
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51484
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51485
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51486
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51487
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51488
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51489
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51490
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51491
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51492
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51493
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51494
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51495
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51496
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51497
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51498
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51499
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51500
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51501
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51502
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51503
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51504
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51505
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51506
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51507
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51508
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51509
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51510
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51511
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51512
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51513
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51514
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51515
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51516
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51517
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51518
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51519
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51520
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51521
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51522
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51523
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51524
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51525
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51526
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51527
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51528
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51529
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51530
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51531
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51532
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51533
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51534
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51535
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51536
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51537
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51538
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51539
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51540
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51541
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51542
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51543
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51544
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51545
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51546
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51547
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51548
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51549
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51550
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51551
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51552
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51553
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51554
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51555
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51556
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51557
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51558
|
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and ...
|
|
51559
|
Inhibition of influenza A virus sialidase activity by sulfatide
|
|
51560
|
Inhibition of influenza A virus sialidase activity by sulfatide
|
|
51561
|
Inhibition of influenza A virus sialidase activity by sulfatide
|
|
51562
|
Inhibition of influenza A virus sialidase activity by sulfatide
|
|
51563
|
Inhibition of influenza A virus sialidase activity by sulfatide
|
|
51564
|
Inhibition of influenza A virus sialidase activity by sulfatide
|
|
51565
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51566
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51567
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51568
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51569
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51570
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51571
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51572
|
Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in ...
|
|
51573
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51574
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51575
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51576
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51577
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51578
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51579
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51580
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51581
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51582
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51583
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51584
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51585
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51586
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51587
|
Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and ...
|
|
51588
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51589
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51590
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51591
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51592
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51593
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51594
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51595
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51596
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51597
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51598
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51599
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51600
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51601
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51602
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51603
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51604
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51605
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51606
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51607
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51608
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51609
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51610
|
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in ...
|
|
51611
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51612
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51613
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51614
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51615
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51616
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51617
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51618
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51619
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51620
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51621
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51622
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51623
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51624
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51625
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51626
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51627
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51628
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51629
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51630
|
Development of a retinoic acid receptor-binding assay with rainbow trout tissue: characterization of retinoic ...
|
|
51631
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51632
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51633
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51634
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51635
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51636
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51637
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51638
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51639
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51640
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51641
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51642
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51643
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51644
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51645
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51646
|
L-myo-lnositol 1-Phosphate Synthase from Plant Sources (Characteristics of the Chloroplastic and Cytosolic ...
|
|
51647
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51648
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51649
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51650
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51651
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51652
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51653
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51654
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51655
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51656
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51657
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51658
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51659
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51660
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51661
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51662
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51663
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51664
|
The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human ...
|
|
51665
|
A colorimetric determination of inositol monophosphates as an assay for D-glucose 6-phosphate-1L-myoinositol ...
|
|
51666
|
A colorimetric determination of inositol monophosphates as an assay for D-glucose 6-phosphate-1L-myoinositol ...
|
|
51667
|
Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana
|
|
51668
|
Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana
|
|
51669
|
Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana
|
|
51670
|
Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana
|
|
51671
|
Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana
|
|
51672
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51673
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51674
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51675
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51676
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51677
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51678
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51679
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51680
|
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin ...
|
|
51681
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51682
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51683
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51684
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51685
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51686
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51687
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51688
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51689
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51690
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51691
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51692
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51693
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51694
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51695
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51696
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51697
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51698
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51699
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51700
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51701
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51702
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51703
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51704
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51705
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51706
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51707
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51708
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51709
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51710
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51711
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51712
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51713
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51714
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51715
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51716
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51717
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51718
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51719
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51720
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51721
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51722
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51723
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51724
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51725
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51726
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51727
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51728
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51729
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51730
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51731
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51732
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51733
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51734
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51735
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51736
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51737
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51738
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51739
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51740
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51741
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51742
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51743
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51744
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51745
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51746
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51747
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51748
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51749
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51750
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51751
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51752
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51753
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51754
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51755
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51756
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51757
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51758
|
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused ...
|
|
51759
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51760
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51761
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51762
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51763
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51764
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51765
|
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random ...
|
|
51766
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51767
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51768
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51769
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51770
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51771
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51772
|
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
|
|
51773
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51774
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51775
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51776
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51777
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51778
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51779
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51780
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51781
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51782
|
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)
|
|
51783
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51784
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51785
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51786
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51787
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51788
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51789
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51790
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51791
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51792
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51793
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51794
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51795
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51796
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51797
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51798
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51799
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51800
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51801
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51802
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51803
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51804
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51805
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51806
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51807
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51808
|
Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl ...
|
|
51809
|
Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I)
|
|
51810
|
Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I)
|
|
51811
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51812
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51813
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51814
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51815
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51816
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51817
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51818
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51819
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51820
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51821
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51822
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51823
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51824
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51825
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51826
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51827
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51828
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51829
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51830
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51831
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51832
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51833
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51834
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51835
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51836
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51837
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51838
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51839
|
Mutational, Kinetic, and NMR Studies of the Mechanism of E. coli GDP-Mannose Mannosyl Hydrolase, an Unusual ...
|
|
51840
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51841
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51842
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51843
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51844
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51845
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51846
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51847
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51848
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51849
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51850
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51851
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51852
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51853
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51854
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51855
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51856
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51857
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51858
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51859
|
Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. ...
|
|
51860
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51861
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51862
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51863
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51864
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51865
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51866
|
Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. ...
|
|
51867
|
Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import ...
|
|
51868
|
Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import ...
|
|
51869
|
Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import ...
|
|
51870
|
Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import ...
|
|
51871
|
Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import ...
|
|
51872
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51873
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51874
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51875
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51876
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51877
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51878
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51879
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51880
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51881
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51882
|
Construction of chimeric cytosolic fructose-1,6-bisphosphatases by insertion of a chloroplastic redox ...
|
|
51883
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51884
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51885
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51886
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51887
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51888
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51889
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51890
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51891
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51892
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51893
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51894
|
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
|
|
51895
|
Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum ...
|
|
51896
|
Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum ...
|
|
51897
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51898
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51899
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51900
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51901
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51902
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51903
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51904
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51905
|
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal ...
|
|
51906
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51907
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51908
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51909
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51910
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51911
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51912
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51913
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51914
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51915
|
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from ...
|
|
51916
|
The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase
|
|
51917
|
Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied ...
|
|
51918
|
Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied ...
|
|
51919
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51920
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51921
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51922
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51923
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51924
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51925
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51926
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51927
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51928
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51929
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51930
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51931
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51932
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51933
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51934
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51935
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51936
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51937
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51938
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51939
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51940
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51941
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51942
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51943
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51944
|
Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
|
|
51945
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51946
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51947
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51948
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51949
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51950
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51951
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51952
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51953
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51954
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51955
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51956
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51957
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51958
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51959
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51960
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51961
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51962
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51963
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51964
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51965
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51966
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51967
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51968
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51969
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51970
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51971
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51972
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51973
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51974
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51975
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51976
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51977
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51978
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51979
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51980
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51981
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51982
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51983
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51984
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51985
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51986
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51987
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51988
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51989
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51990
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51991
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51992
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51993
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51994
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51995
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51996
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51997
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51998
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
51999
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
|
52000
|
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
|
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