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7001
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7002
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7003
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7004
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7005
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7006
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7007
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7008
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7009
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7010
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7011
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7012
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7013
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7014
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7015
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7016
|
Detection of kinetically abnormal argininosuccinate synthase in neonatal citrullinemia by conversion of ...
|
7017
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7018
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7019
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7020
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7021
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7022
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7023
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7024
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7025
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7026
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7027
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7028
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7029
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7030
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7031
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7032
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7033
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7034
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7035
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7036
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7037
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7038
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7039
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7040
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7041
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7042
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7043
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7044
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7045
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7046
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7047
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7048
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7049
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7050
|
Effects of Self-Association of Ornithine Aminotransferase on its Physicochemical Characteristics
|
7051
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7052
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7053
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7054
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7055
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7056
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7057
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7058
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7059
|
Kinetic and Crystallographic Studies on the Active Site Arg289Lys Mutant of Flavocytochrome b2 (Yeast ...
|
7060
|
Effect of 6-phosphogluconate on phosphoglucose isomerase in rat brain in vitro and in vivo
|
7061
|
Effect of 6-phosphogluconate on phosphoglucose isomerase in rat brain in vitro and in vivo
|
7062
|
Effect of 6-phosphogluconate on phosphoglucose isomerase in rat brain in vitro and in vivo
|
7063
|
Effect of 6-phosphogluconate on phosphoglucose isomerase in rat brain in vitro and in vivo
|
7064
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7065
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7066
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7067
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7068
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7069
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7070
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7071
|
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase
|
7072
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7073
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7074
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7075
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7076
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7077
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7078
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7079
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7080
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7081
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7082
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7083
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7084
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7085
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7086
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7087
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7088
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7089
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7090
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7091
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7092
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7093
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7094
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7095
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7096
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7097
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7098
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7099
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7100
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7101
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7102
|
Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus ...
|
7103
|
Enolase from spores and cells of Bacillus megaterium: two-step purification of the enzyme and some of its ...
|
7104
|
Substrate-induced inactivation of argininosuccinate lyase by monofluorofumarate and difluorofumarate
|
7105
|
Substrate-induced inactivation of argininosuccinate lyase by monofluorofumarate and difluorofumarate
|
7106
|
Substrate-induced inactivation of argininosuccinate lyase by monofluorofumarate and difluorofumarate
|
7107
|
13C and 15N nuclear magnetic resonance evidence of the ionization state of substrates bound to bovine ...
|
7108
|
13C and 15N nuclear magnetic resonance evidence of the ionization state of substrates bound to bovine ...
|
7109
|
13C and 15N nuclear magnetic resonance evidence of the ionization state of substrates bound to bovine ...
|
7110
|
13C and 15N nuclear magnetic resonance evidence of the ionization state of substrates bound to bovine ...
|
7111
|
Characterization and enzyme activity of argininosuccinate lyase/delta-crystallin of the embryonic duck lens
|
7112
|
Characterization and enzyme activity of argininosuccinate lyase/delta-crystallin of the embryonic duck lens
|
7113
|
Characterization and enzyme activity of argininosuccinate lyase/delta-crystallin of the embryonic duck lens
|
7114
|
Characterization and enzyme activity of argininosuccinate lyase/delta-crystallin of the embryonic duck lens
|
7115
|
The kinetic effects of in vitro phosphorylation of rabbit muscle enolase by protein kinase C. A possible new ...
|
7116
|
The kinetic effects of in vitro phosphorylation of rabbit muscle enolase by protein kinase C. A possible new ...
|
7117
|
The kinetic effects of in vitro phosphorylation of rabbit muscle enolase by protein kinase C. A possible new ...
|
7118
|
The kinetic effects of in vitro phosphorylation of rabbit muscle enolase by protein kinase C. A possible new ...
|
7119
|
Identification and characterization of differentially active pools of type IIalpha phosphatidylinositol ...
|
7120
|
Identification and characterization of differentially active pools of type IIalpha phosphatidylinositol ...
|
7121
|
Modulation of the Activity of Rat Liver Acetylglutamate Synthase by pH and Arginine Concentration
|
7122
|
Modulation of the Activity of Rat Liver Acetylglutamate Synthase by pH and Arginine Concentration
|
7123
|
Modulation of the Activity of Rat Liver Acetylglutamate Synthase by pH and Arginine Concentration
|
7124
|
pH-Sensitive Control of Arginase by Mn(II) Ions at Submicromolar Concentrations
|
7125
|
pH-Sensitive Control of Arginase by Mn(II) Ions at Submicromolar Concentrations
|
7126
|
pH-Sensitive Control of Arginase by Mn(II) Ions at Submicromolar Concentrations
|
7127
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7128
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7129
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7130
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7131
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7132
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7133
|
Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and ...
|
7134
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7135
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7136
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7137
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7138
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7139
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7140
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7141
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7142
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7143
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7144
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7145
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7146
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7147
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7148
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7149
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7150
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7151
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7152
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7153
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7154
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7155
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7156
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7157
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7158
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7159
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7160
|
Further kinetic characterization of the non-allosteric phosphofructokinase from Escherichia coli K-12
|
7161
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7162
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7163
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7164
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7165
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7166
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7167
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7168
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7169
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7170
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7171
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7172
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7173
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7174
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7175
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7176
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7177
|
Glutamate 325 is a General Acid-Base Catalyst in the Reaction Catalyzed by Fructose-2,6-bisphosphatase
|
7178
|
Evidence for an essential carboxyl group for yeast phosphoglycerate kinase. Reaction with Woodward`s reagent K
|
7179
|
Evidence for an essential carboxyl group for yeast phosphoglycerate kinase. Reaction with Woodward`s reagent K
|
7180
|
Evidence for an essential carboxyl group for yeast phosphoglycerate kinase. Reaction with Woodward`s reagent K
|
7181
|
Evidence for an essential carboxyl group for yeast phosphoglycerate kinase. Reaction with Woodward`s reagent K
|
7182
|
Evidence for an essential carboxyl group for yeast phosphoglycerate kinase. Reaction with Woodward`s reagent K
|
7183
|
Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of pseudomonas ...
|
7184
|
Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of pseudomonas ...
|
7185
|
Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of pseudomonas ...
|
7186
|
Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of pseudomonas ...
|
7187
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7188
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7189
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7190
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7191
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7192
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7193
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7194
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7195
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7196
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7197
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7198
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7199
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7200
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7201
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7202
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7203
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7204
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7205
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7206
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7207
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7208
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7209
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7210
|
cDNA cloning, expression, and mutagenesis study of liver-type Prostaglandin F Synthase
|
7211
|
Identification and Significance of Glucokinase in Transplantable Insulinomas
|
7212
|
Identification and Significance of Glucokinase in Transplantable Insulinomas
|
7213
|
Identification and Significance of Glucokinase in Transplantable Insulinomas
|
7214
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7215
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7216
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7217
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7218
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7219
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7220
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7221
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7222
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7223
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7224
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7225
|
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase ...
|
7226
|
Purification and characterization of glucose-6-phosphate isomerase from Bacillus stearothermophilus
|
7227
|
Purification and characterization of glucose-6-phosphate isomerase from Bacillus stearothermophilus
|
7228
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7229
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7230
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7231
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7232
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7233
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7234
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7235
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7236
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7237
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7238
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7239
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7240
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7241
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7242
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7243
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7244
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7245
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7246
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7247
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7248
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7249
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7250
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7251
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7252
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7253
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7254
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7255
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7256
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7257
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7258
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7259
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7260
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7261
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7262
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7263
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7264
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7265
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7266
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7267
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7268
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7269
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7270
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7271
|
Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human ...
|
7272
|
Catalytic, noncatalytic, and inhibitory phenomena: kinetic analysis of (4-hydroxyphenyl)pyruvate dioxygenase ...
|
7273
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7274
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7275
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7276
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7277
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7278
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7279
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7280
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7281
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7282
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7283
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7284
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7285
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7286
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7287
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7288
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7289
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7290
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7291
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7292
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7293
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7294
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7295
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7296
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7297
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7298
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7299
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7300
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7301
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7302
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7303
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7304
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7305
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7306
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7307
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7308
|
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase ...
|
7309
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7310
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7311
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7312
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7313
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7314
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7315
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7316
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7317
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7318
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7319
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7320
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7321
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7322
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7323
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7324
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7325
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7326
|
Steady-State and Pre-Steady-State Kinetic Analysis of Mycobacterium tuberculosis Pantothenate Synthetase
|
7327
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7328
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7329
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7330
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7331
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7332
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7333
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7334
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7335
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7336
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7337
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7338
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7339
|
A Case for Reverse Protonation: Identification of Glu160 as an Acid/Base Catalyst in Thermoanaerobacterium ...
|
7340
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7341
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7342
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7343
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7344
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7345
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7346
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7347
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7348
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7349
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7350
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7351
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7352
|
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides ...
|
7353
|
Isolation and characterization of enolase from the rhesus monkey (Macaca mulatta)
|
7354
|
Isolation and characterization of enolase from the rhesus monkey (Macaca mulatta)
|
7355
|
Isolation and characterization of enolase from the rhesus monkey (Macaca mulatta)
|
7356
|
Isolation and characterization of enolase from the rhesus monkey (Macaca mulatta)
|
7357
|
The purification and characterization of Escherichia coli enolase
|
7358
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7359
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7360
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7361
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7362
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7363
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7364
|
Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the ...
|
7365
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7366
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7367
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7368
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7369
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7370
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7371
|
The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning ...
|
7372
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7373
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7374
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7375
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7376
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7377
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7378
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7379
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7380
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7381
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7382
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7383
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7384
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7385
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7386
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7387
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7388
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7389
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7390
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7391
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7392
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7393
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7394
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7395
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7396
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7397
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7398
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7399
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7400
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7401
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7402
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7403
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7404
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7405
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7406
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7407
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7408
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7409
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7410
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7411
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7412
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7413
|
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and ...
|
7414
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7415
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7416
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7417
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7418
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7419
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7420
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7421
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7422
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7423
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7424
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7425
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7426
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7427
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7428
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7429
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7430
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7431
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7432
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7433
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7434
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7435
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7436
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7437
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7438
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7439
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7440
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7441
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7442
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7443
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7444
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7445
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7446
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7447
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7448
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7449
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7450
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7451
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7452
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7453
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7454
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7455
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7456
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7457
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7458
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7459
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7460
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7461
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7462
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7463
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7464
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7465
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7466
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7467
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7468
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7469
|
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation ...
|
7470
|
Purification and properties of arginase from human liver and erythrocytes
|
7471
|
Purification and properties of arginase from human liver and erythrocytes
|
7472
|
Purification and properties of arginase from human liver and erythrocytes
|
7473
|
Purification and properties of arginase from human liver and erythrocytes
|
7474
|
The purification and characterization of arginase from saccharomyces cerevisiae
|
7475
|
Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli ...
|
7476
|
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
|
7477
|
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
|
7478
|
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
|
7479
|
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
|
7480
|
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
|
7481
|
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
|
7482
|
Calorimetric determination of thermodynamic parameters of reaction reveals different enthalpic compensations ...
|
7483
|
Calorimetric determination of thermodynamic parameters of reaction reveals different enthalpic compensations ...
|
7484
|
Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21
|
7485
|
Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21
|
7486
|
Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21
|
7487
|
Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21
|
7488
|
Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21
|
7489
|
Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21
|
7490
|
Periplasmic phosphatases in salmonella typhimurium LT2
|
7491
|
Periplasmic phosphatases in salmonella typhimurium LT2
|
7492
|
Polyamine-deficient neurospora crassa mutants and synthesis of cadaverine
|
7493
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7494
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7495
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7496
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7497
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7498
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7499
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7500
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7501
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7502
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7503
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7504
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7505
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7506
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7507
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7508
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7509
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7510
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7511
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7512
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7513
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7514
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7515
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7516
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7517
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7518
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7519
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7520
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7521
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7522
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7523
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7524
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7525
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7526
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7527
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7528
|
The effects of temperature and pH on the kinetic properties of heart muscle lactate dehydrogenase from anuran ...
|
7529
|
Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme
|
7530
|
Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme
|
7531
|
Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme
|
7532
|
Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme
|
7533
|
Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme
|
7534
|
Chemical mechanism of the endogenous argininosuccinate lyase activity of duck lens delta2-crystallin
|
7535
|
Chemical mechanism of the endogenous argininosuccinate lyase activity of duck lens delta2-crystallin
|
7536
|
Assay and kinetics of arginase
|
7537
|
Subcellular localization and kinetic properties of arginase from the liver of genypterus maculatus
|
7538
|
Subcellular localization and kinetic properties of arginase from the liver of genypterus maculatus
|
7539
|
Subcellular localization and kinetic properties of arginase from the liver of genypterus maculatus
|
7540
|
Subcellular localization and kinetic properties of arginase from the liver of genypterus maculatus
|
7541
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7542
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7543
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7544
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7545
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7546
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7547
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7548
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7549
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7550
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7551
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7552
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7553
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7554
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7555
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7556
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7557
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7558
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7559
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7560
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7561
|
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural ...
|
7562
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7563
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7564
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7565
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7566
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7567
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7568
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7569
|
Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile ...
|
7570
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7571
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7572
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7573
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7574
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7575
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7576
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7577
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7578
|
The mechanism of kynurenine hydrolysis catalyzed by kynureninase
|
7579
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7580
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7581
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7582
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7583
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7584
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7585
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7586
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7587
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7588
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7589
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7590
|
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
|
7591
|
Characterisation of arginase from the extreme thermophile bacillus caldovelox
|
7592
|
Characterisation of arginase from the extreme thermophile bacillus caldovelox
|
7593
|
Characterisation of arginase from the extreme thermophile bacillus caldovelox
|
7594
|
Characterisation of arginase from the extreme thermophile bacillus caldovelox
|
7595
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7596
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7597
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7598
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7599
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7600
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7601
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7602
|
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina
|
7603
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7604
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7605
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7606
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7607
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7608
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7609
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7610
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7611
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7612
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7613
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7614
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7615
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7616
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7617
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7618
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7619
|
His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of ...
|
7620
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7621
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7622
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7623
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7624
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7625
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7626
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7627
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7628
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7629
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7630
|
Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400
|
7631
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7632
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7633
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7634
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7635
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7636
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7637
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7638
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7639
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7640
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7641
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7642
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7643
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7644
|
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and ...
|
7645
|
Arginase from human full-term placenta
|
7646
|
Arginase from human full-term placenta
|
7647
|
Arginase from human full-term placenta
|
7648
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7649
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7650
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7651
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7652
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7653
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7654
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7655
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7656
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7657
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7658
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7659
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7660
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7661
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7662
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7663
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7664
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7665
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7666
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7667
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7668
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7669
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7670
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7671
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7672
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7673
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7674
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7675
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7676
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7677
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7678
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7679
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7680
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7681
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7682
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7683
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7684
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7685
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7686
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7687
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7688
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7689
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7690
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7691
|
Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the ...
|
7692
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7693
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7694
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7695
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7696
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7697
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7698
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7699
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7700
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7701
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7702
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7703
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7704
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7705
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7706
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7707
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7708
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7709
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7710
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7711
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7712
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7713
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7714
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7715
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7716
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7717
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7718
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7719
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7720
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7721
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7722
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7723
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7724
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7725
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7726
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7727
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7728
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7729
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7730
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7731
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7732
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7733
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7734
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7735
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7736
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7737
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7738
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7739
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7740
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7741
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7742
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7743
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7744
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7745
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7746
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7747
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7748
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7749
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7750
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7751
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7752
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7753
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7754
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7755
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7756
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7757
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7758
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7759
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7760
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7761
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7762
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7763
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7764
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7765
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7766
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7767
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7768
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7769
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7770
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7771
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7772
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7773
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7774
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7775
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7776
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7777
|
Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its ...
|
7778
|
Effect of phosphoglucose isomerase and glucose 6-phosphate on UDP-N-acetylglucosamine inhibition of ...
|
7779
|
Effect of phosphoglucose isomerase and glucose 6-phosphate on UDP-N-acetylglucosamine inhibition of ...
|
7780
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7781
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7782
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7783
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7784
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7785
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7786
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7787
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7788
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7789
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7790
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7791
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7792
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7793
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7794
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7795
|
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by ...
|
7796
|
Interpretation of the kinetics of consecutive enzyme-catalyzed reactions
|
7797
|
Interpretation of the kinetics of consecutive enzyme-catalyzed reactions
|
7798
|
Interpretation of the kinetics of consecutive enzyme-catalyzed reactions
|
7799
|
Interpretation of the kinetics of consecutive enzyme-catalyzed reactions
|
7800
|
Purification and characterization of arginase from neurospora crassa
|
7801
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7802
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7803
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7804
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7805
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7806
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7807
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7808
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7809
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7810
|
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain ...
|
7811
|
Arginase in lactating bovine mammary glands: implications in proline synthesis
|
7812
|
Arginase in lactating bovine mammary glands: implications in proline synthesis
|
7813
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7814
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7815
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7816
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7817
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7818
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7819
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7820
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7821
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7822
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7823
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7824
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7825
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7826
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7827
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7828
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7829
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7830
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7831
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7832
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7833
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7834
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7835
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7836
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7837
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7838
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7839
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7840
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7841
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7842
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7843
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7844
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7845
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7846
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7847
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7848
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7849
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7850
|
Delineation of the Roles of Amino Acids Involved in the Catalytic Functions of Leuconostoc mesenteroides ...
|
7851
|
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding ...
|
7852
|
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding ...
|
7853
|
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding ...
|
7854
|
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding ...
|
7855
|
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding ...
|
7856
|
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding ...
|
7857
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7858
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7859
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7860
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7861
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7862
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7863
|
Arginyl-tRNA synthetase from escherichia coli influence of arginine biosynthetic precursors on the charging ...
|
7864
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7865
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7866
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7867
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7868
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7869
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7870
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7871
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7872
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7873
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7874
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7875
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7876
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7877
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7878
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7879
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7880
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7881
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7882
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7883
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7884
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7885
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7886
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7887
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7888
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7889
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7890
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7891
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7892
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7893
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7894
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7895
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7896
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7897
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7898
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7899
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7900
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7901
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7902
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7903
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7904
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7905
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7906
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7907
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7908
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7909
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7910
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7911
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7912
|
Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using ...
|
7913
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7914
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7915
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7916
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7917
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7918
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7919
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7920
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7921
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7922
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7923
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7924
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7925
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7926
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7927
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7928
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7929
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7930
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7931
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7932
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7933
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7934
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7935
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7936
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7937
|
Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate ...
|
7938
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7939
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7940
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7941
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7942
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7943
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7944
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7945
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7946
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7947
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7948
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7949
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7950
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7951
|
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart ...
|
7952
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7953
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7954
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7955
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7956
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7957
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7958
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7959
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7960
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7961
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7962
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7963
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7964
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7965
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7966
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7967
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7968
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7969
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7970
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7971
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7972
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7973
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7974
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7975
|
Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial ...
|
7976
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7977
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7978
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7979
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7980
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7981
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7982
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7983
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7984
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7985
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7986
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7987
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7988
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7989
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7990
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7991
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7992
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7993
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7994
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7995
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7996
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7997
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7998
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
7999
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|
8000
|
Site-directed mutagenesis of essential residues involved in the mechanism of bacterial glycosylasparaginase
|