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71001
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The Hepatitis E virus intraviral interactome
|
71002
|
The Hepatitis E virus intraviral interactome
|
71003
|
The Hepatitis E virus intraviral interactome
|
71004
|
The Hepatitis E virus intraviral interactome
|
71005
|
The Hepatitis E virus intraviral interactome
|
71006
|
The Hepatitis E virus intraviral interactome
|
71007
|
The Hepatitis E virus intraviral interactome
|
71008
|
The Hepatitis E virus intraviral interactome
|
71009
|
The Hepatitis E virus intraviral interactome
|
71010
|
The Hepatitis E virus intraviral interactome
|
71011
|
The octahaem MccA is a haem c-copper sulfite reductase.
|
71012
|
The octahaem MccA is a haem c-copper sulfite reductase.
|
71013
|
The octahaem MccA is a haem c-copper sulfite reductase.
|
71014
|
The octahaem MccA is a haem c-copper sulfite reductase.
|
71015
|
Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis.
|
71016
|
Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis.
|
71017
|
Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD
|
71018
|
Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD
|
71019
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71020
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71021
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71022
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71023
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71024
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71025
|
Structural and functional analyses of human tryptophan 2,3-dioxygenase
|
71026
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71027
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71028
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71029
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71030
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71031
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71032
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71033
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71034
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71035
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71036
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71037
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71038
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71039
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71040
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71041
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71042
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71043
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71044
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71045
|
Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen
|
71046
|
Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme
|
71047
|
Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme
|
71048
|
Human indolylamine 2,3-dioxygenase. Its tissue distribution, and characterization of the placental enzyme
|
71049
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71050
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71051
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71052
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71053
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71054
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71055
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71056
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71057
|
Reassessment of the reaction mechanism in the heme dioxygenases
|
71058
|
Biochemical characterization of the very long-chain fatty acid elongase ELOVL7.
|
71059
|
Biochemical characterization of the very long-chain fatty acid elongase ELOVL7.
|
71060
|
Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of ...
|
71061
|
Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of ...
|
71062
|
Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of ...
|
71063
|
Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of ...
|
71064
|
Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of ...
|
71065
|
Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of ...
|
71066
|
PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by ...
|
71067
|
PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by ...
|
71068
|
PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by ...
|
71069
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71070
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71071
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71072
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71073
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71074
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71075
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71076
|
The Escherichia coli CysZ is a pH dependent sulfate transporter that can be inhibited by sulfite.
|
71077
|
Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
|
71078
|
Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the ...
|
71079
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71080
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71081
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71082
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71083
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71084
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71085
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71086
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71087
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71088
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71089
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71090
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71091
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71092
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71093
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71094
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71095
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71096
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71097
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71098
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71099
|
Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as ...
|
71100
|
Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
|
71101
|
Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
|
71102
|
Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
|
71103
|
Biosynthesis of riboflavin. Single turnover kinetic analysis of GTP cyclohydrolase II
|
71104
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71105
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71106
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71107
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71108
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71109
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71110
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71111
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71112
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71113
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71114
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71115
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71116
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71117
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71118
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71119
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71120
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71121
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71122
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71123
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71124
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71125
|
Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
|
71126
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71127
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71128
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71129
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71130
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71131
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71132
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71133
|
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain ...
|
71134
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71135
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71136
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71137
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71138
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71139
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71140
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71141
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71142
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71143
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71144
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71145
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71146
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71147
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71148
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71149
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71150
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71151
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71152
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71153
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71154
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71155
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71156
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71157
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71158
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71159
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71160
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71161
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71162
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71163
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71164
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71165
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71166
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71167
|
Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand ...
|
71168
|
Camostat mesylate inhibits SARS-CoV-2 activation by TMPRSS2-related proteases and its metabolite GBPA exerts ...
|
71169
|
Camostat mesylate inhibits SARS-CoV-2 activation by TMPRSS2-related proteases and its metabolite GBPA exerts ...
|
71170
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71171
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71172
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71173
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71174
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71175
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71176
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71177
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71178
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71179
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71180
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71181
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71182
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71183
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71184
|
Role of the ortholog and paralog amino acid invariants in the active site of the ...
|
71185
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71186
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71187
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71188
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71189
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71190
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71191
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71192
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71193
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71194
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71195
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71196
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71197
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71198
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71199
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71200
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71201
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71202
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71203
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71204
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71205
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71206
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71207
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71208
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71209
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71210
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71211
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71212
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71213
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71214
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71215
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71216
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71217
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71218
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71219
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71220
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71221
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71222
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71223
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71224
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71225
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71226
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71227
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71228
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71229
|
Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based ...
|
71230
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71231
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71232
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71233
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71234
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71235
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71236
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71237
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71238
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71239
|
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ ...
|
71240
|
Molecular cloning and expression of a cDNA encoding an olfactory-specific mouse phenol sulphotransferase
|
71241
|
Molecular cloning and expression of a cDNA encoding an olfactory-specific mouse phenol sulphotransferase
|
71242
|
Molecular cloning and expression of a cDNA encoding an olfactory-specific mouse phenol sulphotransferase
|
71243
|
Expression of pig heart mitochondrial NADP-dependent isocitrate dehydrogenase in Escherichia coli
|
71244
|
Expression of pig heart mitochondrial NADP-dependent isocitrate dehydrogenase in Escherichia coli
|
71245
|
Sequential hydrolysis of the gamma- and beta-phosphate groups of ATP by the ATP diphosphohydrolase from pig ...
|
71246
|
Sequential hydrolysis of the gamma- and beta-phosphate groups of ATP by the ATP diphosphohydrolase from pig ...
|
71247
|
Sequential hydrolysis of the gamma- and beta-phosphate groups of ATP by the ATP diphosphohydrolase from pig ...
|
71248
|
Sequential hydrolysis of the gamma- and beta-phosphate groups of ATP by the ATP diphosphohydrolase from pig ...
|
71249
|
Purification and characterization of specific 3-deoxy-D- manno-octulosonate 8-phosphate phosphatase from ...
|
71250
|
Purification and characterization of specific 3-deoxy-D- manno-octulosonate 8-phosphate phosphatase from ...
|
71251
|
Purification and characterization of specific 3-deoxy-D- manno-octulosonate 8-phosphate phosphatase from ...
|
71252
|
Purification and characterization of specific 3-deoxy-D- manno-octulosonate 8-phosphate phosphatase from ...
|
71253
|
Kinetic and thermodynamic characterization of novel alkaline lipase from halotolerant Bacillus gibsonii
|
71254
|
Kinetic and thermodynamic characterization of novel alkaline lipase from halotolerant Bacillus gibsonii
|
71255
|
Kinetic and thermodynamic characterization of novel alkaline lipase from halotolerant Bacillus gibsonii
|
71256
|
Substrate specificity of a new laccase from Trametes polyzona WRF03
|
71257
|
Substrate specificity of a new laccase from Trametes polyzona WRF03
|
71258
|
Substrate specificity of a new laccase from Trametes polyzona WRF03
|
71259
|
Substrate specificity of a new laccase from Trametes polyzona WRF03
|
71260
|
Substrate specificity of a new laccase from Trametes polyzona WRF03
|
71261
|
Substrate specificity of a new laccase from Trametes polyzona WRF03
|
71262
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71263
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71264
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71265
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71266
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71267
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71268
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71269
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71270
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71271
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71272
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71273
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71274
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71275
|
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase
|
71276
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71277
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71278
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71279
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71280
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71281
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71282
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71283
|
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure ...
|
71284
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71285
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71286
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71287
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71288
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71289
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71290
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71291
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71292
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71293
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71294
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71295
|
Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli ...
|
71296
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71297
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71298
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71299
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71300
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71301
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71302
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71303
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71304
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71305
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71306
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71307
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71308
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71309
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71310
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71311
|
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into ...
|
71312
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71313
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71314
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71315
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71316
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71317
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71318
|
Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV
|
71319
|
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
|
71320
|
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
|
71321
|
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
|
71322
|
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
|
71323
|
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
|
71324
|
Sequential O-methylation of tricetin by a single gene product in wheat
|
71325
|
Sequential O-methylation of tricetin by a single gene product in wheat
|
71326
|
Sequential O-methylation of tricetin by a single gene product in wheat
|
71327
|
Sequential O-methylation of tricetin by a single gene product in wheat
|
71328
|
Identification of isoliquiritigenin as an activator that stimulates the enzymatic production of glycyrrhetinic ...
|
71329
|
Identification of isoliquiritigenin as an activator that stimulates the enzymatic production of glycyrrhetinic ...
|
71330
|
A bacterium that degrades and assimilates poly(ethylene terephthalate).
|
71331
|
A bacterium that degrades and assimilates poly(ethylene terephthalate).
|
71332
|
Active Site Flexibility as a Hallmark for Efficient PET Degradation by I. sakaiensis PETase.
|
71333
|
Active Site Flexibility as a Hallmark for Efficient PET Degradation by I. sakaiensis PETase.
|
71334
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71335
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71336
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71337
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71338
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71339
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71340
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71341
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71342
|
Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase.
|
71343
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71344
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71345
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71346
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71347
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71348
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71349
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71350
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71351
|
Fluorinated substrates result in variable leakage of a reaction intermediate during catalysis by ...
|
71352
|
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
|
71353
|
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
|
71354
|
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
|
71355
|
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
|
71356
|
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
|
71357
|
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
|
71358
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71359
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71360
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71361
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71362
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71363
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71364
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71365
|
Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent ...
|
71366
|
Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by ...
|
71367
|
Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by ...
|
71368
|
Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by ...
|
71369
|
Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by ...
|
71370
|
Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by ...
|
71371
|
Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action
|
71372
|
Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action
|
71373
|
Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action
|
71374
|
Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action
|
71375
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71376
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71377
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71378
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71379
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71380
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71381
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71382
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71383
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71384
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71385
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71386
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71387
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71388
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71389
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71390
|
The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia ...
|
71391
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71392
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71393
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71394
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71395
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71396
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71397
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71398
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71399
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71400
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71401
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71402
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71403
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71404
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71405
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71406
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71407
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71408
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71409
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71410
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71411
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71412
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71413
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71414
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71415
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71416
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71417
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71418
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71419
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71420
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71421
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71422
|
Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate ...
|
71423
|
Alterations of bile acid and bumetanide uptake during culturing of rat hepatocytes.
|
71424
|
Alterations of bile acid and bumetanide uptake during culturing of rat hepatocytes.
|
71425
|
Alterations of bile acid and bumetanide uptake during culturing of rat hepatocytes.
|
71426
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71427
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71428
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71429
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71430
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71431
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71432
|
Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group ...
|
71433
|
A novel inhibitor that suspends the induced fit mechanism of UDP-N- acetylglucosamine enolpyruvyl transferase ...
|
71434
|
A novel inhibitor that suspends the induced fit mechanism of UDP-N- acetylglucosamine enolpyruvyl transferase ...
|
71435
|
Purification and properties of L-histidine decarboxylase from mouse stomach.
|
71436
|
Biochemical characterization of the cutinases from Thermobifida fusca
|
71437
|
Biochemical characterization of the cutinases from Thermobifida fusca
|
71438
|
Biochemical characterization of the cutinases from Thermobifida fusca
|
71439
|
Biochemical characterization of the cutinases from Thermobifida fusca
|
71440
|
Biochemical characterization of the cutinases from Thermobifida fusca
|
71441
|
Biochemical characterization of the cutinases from Thermobifida fusca
|
71442
|
Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
|
71443
|
Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
|
71444
|
Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
|
71445
|
Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
|
71446
|
Novel antifungal drug discovery based on targeting pathways regulating the fungus-conserved Upc2 transcription ...
|
71447
|
Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1
|
71448
|
Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1
|
71449
|
Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1
|
71450
|
Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1
|
71451
|
Cutinase-Catalyzed Hydrolysis of Poly(ethylene terephthalate)
|
71452
|
Cutinase-Catalyzed Hydrolysis of Poly(ethylene terephthalate)
|
71453
|
Cutinase-Catalyzed Hydrolysis of Poly(ethylene terephthalate)
|
71454
|
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from ...
|
71455
|
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from ...
|
71456
|
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from ...
|
71457
|
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from ...
|
71458
|
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from ...
|
71459
|
Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from ...
|
71460
|
Cloning, nucleotide sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas ...
|
71461
|
Cloning, nucleotide sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas ...
|
71462
|
Cloning, nucleotide sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas ...
|
71463
|
Cloning, nucleotide sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas ...
|
71464
|
Cloning, nucleotide sequencing and characterization of a polyurethanase gene (pueB) from Pseudomonas ...
|
71465
|
Lipase from Candida antarctica (CALB) and cutinase from Humicola insolens act synergistically for PET ...
|
71466
|
Lipase from Candida antarctica (CALB) and cutinase from Humicola insolens act synergistically for PET ...
|
71467
|
A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid ...
|
71468
|
A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid ...
|
71469
|
Cloning and expression in Escherichia coli of a polyurethane-degrading enzyme from Pseudomonas fluorescens
|
71470
|
Cloning and expression in Escherichia coli of a polyurethane-degrading enzyme from Pseudomonas fluorescens
|
71471
|
Growth of Acinetobacter gerneri P7 on polyurethane and the purification and characterization of a ...
|
71472
|
Growth of Acinetobacter gerneri P7 on polyurethane and the purification and characterization of a ...
|
71473
|
Growth of Acinetobacter gerneri P7 on polyurethane and the purification and characterization of a ...
|
71474
|
Growth of Acinetobacter gerneri P7 on polyurethane and the purification and characterization of a ...
|
71475
|
Growth of Acinetobacter gerneri P7 on polyurethane and the purification and characterization of a ...
|
71476
|
Growth of Acinetobacter gerneri P7 on polyurethane and the purification and characterization of a ...
|
71477
|
Purification and characterization of l-histidine decarboxylase from mouse mastocytoma P-815 cells.
|
71478
|
Spectroscopic analysis of recombinant rat histidine decarboxylase
|
71479
|
Growth of Pseudomonas chlororaphis on a polyester-polyurethane and the purification and characterization of a ...
|
71480
|
Growth of Bacillus subtilis on polyurethane and the purification and characterization of a ...
|
71481
|
Growth of Bacillus subtilis on polyurethane and the purification and characterization of a ...
|
71482
|
Growth of Bacillus subtilis on polyurethane and the purification and characterization of a ...
|
71483
|
Growth of Bacillus subtilis on polyurethane and the purification and characterization of a ...
|
71484
|
Growth of Bacillus subtilis on polyurethane and the purification and characterization of a ...
|
71485
|
Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch ...
|
71486
|
Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch ...
|
71487
|
Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch ...
|
71488
|
Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch ...
|
71489
|
Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch ...
|
71490
|
Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch ...
|
71491
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71492
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71493
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71494
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71495
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71496
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71497
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71498
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71499
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71500
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71501
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71502
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71503
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71504
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71505
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71506
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71507
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71508
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71509
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71510
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71511
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71512
|
Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase ...
|
71513
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71514
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71515
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71516
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71517
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71518
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71519
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71520
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71521
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71522
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71523
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71524
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71525
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71526
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71527
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71528
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71529
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71530
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71531
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71532
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71533
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71534
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71535
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71536
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71537
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71538
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71539
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71540
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71541
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71542
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71543
|
An engineered PET depolymerase to break down and recycle plastic bottles
|
71544
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71545
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71546
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71547
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71548
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71549
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71550
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71551
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71552
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71553
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71554
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71555
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71556
|
Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms ...
|
71557
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71558
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71559
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71560
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71561
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71562
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71563
|
Kinetic and mechanistic analysis of the Escherichia coli ribD-encoded bifunctional deaminase-reductase ...
|
71564
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71565
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71566
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71567
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71568
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71569
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71570
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71571
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71572
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71573
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71574
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71575
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71576
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71577
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71578
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71579
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71580
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71581
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71582
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71583
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71584
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71585
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71586
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71587
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71588
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71589
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71590
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71591
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71592
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71593
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71594
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71595
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71596
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71597
|
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
|
71598
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71599
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71600
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71601
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71602
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71603
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71604
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71605
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71606
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71607
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71608
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71609
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71610
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71611
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71612
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71613
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71614
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71615
|
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis.
|
71616
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71617
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71618
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71619
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71620
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71621
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71622
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71623
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71624
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71625
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71626
|
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
|
71627
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71628
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71629
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71630
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71631
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71632
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71633
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71634
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71635
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71636
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71637
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71638
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71639
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71640
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71641
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71642
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71643
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71644
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71645
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71646
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71647
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71648
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71649
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71650
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71651
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71652
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71653
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71654
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71655
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71656
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71657
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71658
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71659
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71660
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71661
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71662
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71663
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71664
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71665
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71666
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71667
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71668
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71669
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71670
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71671
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71672
|
Thiazolopyrimidine inhibitors of 2-methylerythritol 2,4-cyclodiphosphate synthase (IspF) from Mycobacterium ...
|
71673
|
SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity
|
71674
|
SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity
|
71675
|
SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity
|
71676
|
SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity
|
71677
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71678
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71679
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71680
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71681
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71682
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71683
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71684
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71685
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71686
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71687
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71688
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71689
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71690
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71691
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71692
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71693
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71694
|
Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
|
71695
|
Alpha-keto acid dehydrogenase complexes. XX. A kinetic study of the pyruvate dehydrogenase complex from bovine ...
|
71696
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71697
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71698
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71699
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71700
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71701
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71702
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71703
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71704
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71705
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71706
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71707
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71708
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71709
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71710
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71711
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71712
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71713
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71714
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71715
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71716
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71717
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71718
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71719
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71720
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71721
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71722
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71723
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71724
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71725
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71726
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71727
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71728
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71729
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71730
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71731
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71732
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71733
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71734
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71735
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71736
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71737
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71738
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71739
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71740
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71741
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71742
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71743
|
Correlation between dissociation and catalysis of SARS-CoV main protease
|
71744
|
Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain ...
|
71745
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71746
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71747
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71748
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71749
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71750
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71751
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71752
|
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and ...
|
71753
|
Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and ...
|
71754
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71755
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71756
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71757
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71758
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71759
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71760
|
Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2
|
71761
|
A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl (acyl carrier protein) reductase
|
71762
|
A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl (acyl carrier protein) reductase
|
71763
|
A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl (acyl carrier protein) reductase
|
71764
|
Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal ?-oxidation of unsaturated fatty ...
|
71765
|
Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal ?-oxidation of unsaturated fatty ...
|
71766
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71767
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71768
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71769
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71770
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71771
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71772
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71773
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71774
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71775
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71776
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71777
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71778
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71779
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71780
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71781
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71782
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71783
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71784
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71785
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71786
|
Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new ...
|
71787
|
Purification, characterization, and molecular cloning of S-adenosyl-L-methionine: uroporphyrinogen III ...
|
71788
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71789
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71790
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71791
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71792
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71793
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71794
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71795
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71796
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71797
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71798
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71799
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71800
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71801
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71802
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71803
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71804
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71805
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71806
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71807
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71808
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71809
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71810
|
The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family
|
71811
|
Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double ...
|
71812
|
Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double ...
|
71813
|
Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double ...
|
71814
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71815
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71816
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71817
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71818
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71819
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71820
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71821
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71822
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71823
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71824
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71825
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71826
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71827
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71828
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71829
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71830
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71831
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71832
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71833
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71834
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71835
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71836
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71837
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71838
|
Development of potent dipeptide-type SARS-CoV 3CL protease inhibitors with novel P3 scaffolds: design, ...
|
71839
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71840
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71841
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71842
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71843
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71844
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71845
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71846
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71847
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71848
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71849
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71850
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71851
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71852
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71853
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71854
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71855
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71856
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71857
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71858
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71859
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71860
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71861
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71862
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71863
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71864
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71865
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71866
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71867
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71868
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71869
|
Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: ...
|
71870
|
A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein ...
|
71871
|
A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein ...
|
71872
|
A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein ...
|
71873
|
A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein ...
|
71874
|
The gamma-aminobutyrate permease GabP serves as the third proline transporter of Bacillus subtilis.
|
71875
|
The gamma-aminobutyrate permease GabP serves as the third proline transporter of Bacillus subtilis.
|
71876
|
The gamma-aminobutyrate permease GabP serves as the third proline transporter of Bacillus subtilis.
|
71877
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71878
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71879
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71880
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71881
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71882
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71883
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71884
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71885
|
Identification and Functional Assessment of a New CYP2C9 Allelic Variant CYP2C9*59.
|
71886
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71887
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71888
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71889
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71890
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71891
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71892
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71893
|
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in ...
|
71894
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71895
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71896
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71897
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71898
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71899
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71900
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71901
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71902
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71903
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71904
|
Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory syndrome 3CL ...
|
71905
|
Engineering a novel endopeptidase based on SARS 3CL(pro).
|
71906
|
Engineering a novel endopeptidase based on SARS 3CL(pro).
|
71907
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71908
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71909
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71910
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71911
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71912
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71913
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71914
|
Phosphatidic acid binds and stimulates Arabidopsis sphingosine kinases.
|
71915
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71916
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71917
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71918
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71919
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71920
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71921
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71922
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71923
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71924
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71925
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71926
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71927
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71928
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71929
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71930
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71931
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71932
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71933
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71934
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71935
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71936
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71937
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71938
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71939
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71940
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71941
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71942
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71943
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71944
|
Molecular basis of perhydrolase activity in serine hydrolases
|
71945
|
Enzymatic activity of the SARS coronavirus main proteinase dimer
|
71946
|
pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics ...
|
71947
|
The cysteine protease CEP1, a key executor involved in tapetal programmed cell death, regulates pollen ...
|
71948
|
The cysteine protease CEP1, a key executor involved in tapetal programmed cell death, regulates pollen ...
|
71949
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71950
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71951
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71952
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71953
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71954
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71955
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71956
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71957
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71958
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71959
|
Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase ...
|
71960
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71961
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71962
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71963
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71964
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71965
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71966
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71967
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71968
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71969
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71970
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71971
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71972
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71973
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71974
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
|
71975
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
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71976
|
Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in ...
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71977
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71978
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71979
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71980
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71981
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71982
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71983
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71984
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71985
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71986
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71987
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71988
|
Biochemical characterization of the phosphatase domain of the tumor suppressor PH domain leucine-rich repeat ...
|
71989
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71990
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71991
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71992
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71993
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71994
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71995
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71996
|
The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon.
|
71997
|
Characterization of human fructose-1,6-bisphosphatase in control and deficient tissues.
|
71998
|
Characterization of human fructose-1,6-bisphosphatase in control and deficient tissues.
|
71999
|
Characterization of human fructose-1,6-bisphosphatase in control and deficient tissues.
|
72000
|
Characterization of human fructose-1,6-bisphosphatase in control and deficient tissues.
|