To improve SABIO-RK data interoperability, semantic markup was added to web pages as described and defined by
This structured information makes it easier to discover, collate and analyse our data.
22001
|
Crystal structure of rat biliverdin reductase
|
22002
|
Crystal structure of rat biliverdin reductase
|
22003
|
Crystal structure of rat biliverdin reductase
|
22004
|
Crystal structure of rat biliverdin reductase
|
22005
|
Crystal structure of rat biliverdin reductase
|
22006
|
Crystal structure of rat biliverdin reductase
|
22007
|
Crystal structure of rat biliverdin reductase
|
22008
|
Crystal structure of rat biliverdin reductase
|
22009
|
Crystal structure of rat biliverdin reductase
|
22010
|
Crystal structure of rat biliverdin reductase
|
22011
|
Crystal structure of rat biliverdin reductase
|
22012
|
Crystal structure of rat biliverdin reductase
|
22013
|
Crystal structure of rat biliverdin reductase
|
22014
|
Crystal structure of rat biliverdin reductase
|
22015
|
Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release.
|
22016
|
Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release.
|
22017
|
Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release.
|
22018
|
Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release.
|
22019
|
Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release.
|
22020
|
Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release.
|
22021
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22022
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22023
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22024
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22025
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22026
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22027
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22028
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22029
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22030
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22031
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22032
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22033
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22034
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22035
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22036
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22037
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22038
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22039
|
Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin ...
|
22040
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22041
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22042
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22043
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22044
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22045
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22046
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22047
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22048
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22049
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22050
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22051
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22052
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22053
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22054
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22055
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22056
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22057
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22058
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22059
|
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
|
22060
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22061
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22062
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22063
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22064
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22065
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22066
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22067
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22068
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22069
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22070
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22071
|
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in ...
|
22072
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22073
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22074
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22075
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22076
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22077
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22078
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22079
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22080
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22081
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22082
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22083
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22084
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22085
|
Transport of alpha-aminoisobutyric acid by Streptococcus pyogenes and its derived L-form
|
22086
|
The purification and properties of the alpha-glycerophosphate-oxidizing enzyme of Streptococcus faecalis 10C1
|
22087
|
Halibut muscle 3-phosphoglycerate kinase. Chemical and physical properties of the enzyme and its substrate ...
|
22088
|
Halibut muscle 3-phosphoglycerate kinase. Chemical and physical properties of the enzyme and its substrate ...
|
22089
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22090
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22091
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22092
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22093
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22094
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22095
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22096
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22097
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22098
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22099
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22100
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22101
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22102
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22103
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22104
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22105
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22106
|
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione ...
|
22107
|
Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization
|
22108
|
Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization
|
22109
|
Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in ...
|
22110
|
Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in ...
|
22111
|
Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in ...
|
22112
|
Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in ...
|
22113
|
Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in ...
|
22114
|
Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in ...
|
22115
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22116
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22117
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22118
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22119
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22120
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22121
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22122
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22123
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22124
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22125
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22126
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22127
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22128
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22129
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22130
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22131
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22132
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22133
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22134
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22135
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22136
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22137
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22138
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22139
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22140
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22141
|
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for ...
|
22142
|
Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants
|
22143
|
Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants
|
22144
|
Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants
|
22145
|
Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants
|
22146
|
One step purification and characterization of the pyrrolidone carboxyl peptidase of Streptococcus pyogenes ...
|
22147
|
One step purification and characterization of the pyrrolidone carboxyl peptidase of Streptococcus pyogenes ...
|
22148
|
Adenine nucleotides affect the binding of 3-phosphoglycerate to pig muscle 3-phosphoglycerate kinase
|
22149
|
Adenine nucleotides affect the binding of 3-phosphoglycerate to pig muscle 3-phosphoglycerate kinase
|
22150
|
Adenine nucleotides affect the binding of 3-phosphoglycerate to pig muscle 3-phosphoglycerate kinase
|
22151
|
Adenine nucleotides affect the binding of 3-phosphoglycerate to pig muscle 3-phosphoglycerate kinase
|
22152
|
Adenine nucleotides affect the binding of 3-phosphoglycerate to pig muscle 3-phosphoglycerate kinase
|
22153
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22154
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22155
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22156
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22157
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22158
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22159
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22160
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22161
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22162
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22163
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22164
|
Probing the active site of aromatase with 2-methyl-substituted androstenedione analogs
|
22165
|
Activity of liver glutamine transaminase toward L-gamma-glutamyl hydrazones of alpha-keto acids
|
22166
|
Activity of liver glutamine transaminase toward L-gamma-glutamyl hydrazones of alpha-keto acids
|
22167
|
Evolution of enzymatic activities in the enolase superfamily: partitioning of reactive intermediates by ...
|
22168
|
Evolution of enzymatic activities in the enolase superfamily: partitioning of reactive intermediates by ...
|
22169
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22170
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22171
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22172
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22173
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22174
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22175
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22176
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22177
|
Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-lyase (C-DES) from Synechocystis. ...
|
22178
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22179
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22180
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22181
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22182
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22183
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22184
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22185
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22186
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22187
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22188
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22189
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22190
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22191
|
Pantothenoylcysteine-4` -phosphate decarboxylase from horse liver
|
22192
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22193
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22194
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22195
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22196
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22197
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22198
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22199
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22200
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22201
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22202
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22203
|
Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous ...
|
22204
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22205
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22206
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22207
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22208
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22209
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22210
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' ...
|
22211
|
Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity ...
|
22212
|
Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity ...
|
22213
|
Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity ...
|
22214
|
Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity ...
|
22215
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22216
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22217
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22218
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22219
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22220
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22221
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22222
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22223
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22224
|
Enolases from fluoride-sensitive and fluoride-resistant streptococci
|
22225
|
Purification and partial characterisation of 4-aminobutyrate 2-ketoglutarate transaminase from human brain
|
22226
|
Purification and partial characterisation of 4-aminobutyrate 2-ketoglutarate transaminase from human brain
|
22227
|
Purification and partial characterisation of 4-aminobutyrate 2-ketoglutarate transaminase from human brain
|
22228
|
Purification and partial characterisation of 4-aminobutyrate 2-ketoglutarate transaminase from human brain
|
22229
|
Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a ...
|
22230
|
Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a ...
|
22231
|
Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a ...
|
22232
|
Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a ...
|
22233
|
Lysine-ketoglutarate reductase in human tissues
|
22234
|
Lysine-ketoglutarate reductase in human tissues
|
22235
|
Lysine-ketoglutarate reductase in human tissues
|
22236
|
Lysine-ketoglutarate reductase in human tissues
|
22237
|
Lysine-ketoglutarate reductase in human tissues
|
22238
|
Lysine-ketoglutarate reductase in human tissues
|
22239
|
Lysine-ketoglutarate reductase in human tissues
|
22240
|
Lysine-ketoglutarate reductase in human tissues
|
22241
|
Lysine-ketoglutarate reductase in human tissues
|
22242
|
Individual variation in hepatic aldehyde oxidase activity
|
22243
|
Individual variation in hepatic aldehyde oxidase activity
|
22244
|
Individual variation in hepatic aldehyde oxidase activity
|
22245
|
Individual variation in hepatic aldehyde oxidase activity
|
22246
|
Individual variation in hepatic aldehyde oxidase activity
|
22247
|
Individual variation in hepatic aldehyde oxidase activity
|
22248
|
Individual variation in hepatic aldehyde oxidase activity
|
22249
|
Individual variation in hepatic aldehyde oxidase activity
|
22250
|
Individual variation in hepatic aldehyde oxidase activity
|
22251
|
Individual variation in hepatic aldehyde oxidase activity
|
22252
|
Individual variation in hepatic aldehyde oxidase activity
|
22253
|
Individual variation in hepatic aldehyde oxidase activity
|
22254
|
Individual variation in hepatic aldehyde oxidase activity
|
22255
|
Individual variation in hepatic aldehyde oxidase activity
|
22256
|
Individual variation in hepatic aldehyde oxidase activity
|
22257
|
Individual variation in hepatic aldehyde oxidase activity
|
22258
|
Individual variation in hepatic aldehyde oxidase activity
|
22259
|
Individual variation in hepatic aldehyde oxidase activity
|
22260
|
Individual variation in hepatic aldehyde oxidase activity
|
22261
|
Individual variation in hepatic aldehyde oxidase activity
|
22262
|
Individual variation in hepatic aldehyde oxidase activity
|
22263
|
Individual variation in hepatic aldehyde oxidase activity
|
22264
|
Individual variation in hepatic aldehyde oxidase activity
|
22265
|
Individual variation in hepatic aldehyde oxidase activity
|
22266
|
Individual variation in hepatic aldehyde oxidase activity
|
22267
|
Individual variation in hepatic aldehyde oxidase activity
|
22268
|
Individual variation in hepatic aldehyde oxidase activity
|
22269
|
Individual variation in hepatic aldehyde oxidase activity
|
22270
|
Individual variation in hepatic aldehyde oxidase activity
|
22271
|
Individual variation in hepatic aldehyde oxidase activity
|
22272
|
Individual variation in hepatic aldehyde oxidase activity
|
22273
|
Individual variation in hepatic aldehyde oxidase activity
|
22274
|
Individual variation in hepatic aldehyde oxidase activity
|
22275
|
Individual variation in hepatic aldehyde oxidase activity
|
22276
|
Individual variation in hepatic aldehyde oxidase activity
|
22277
|
Individual variation in hepatic aldehyde oxidase activity
|
22278
|
Individual variation in hepatic aldehyde oxidase activity
|
22279
|
Individual variation in hepatic aldehyde oxidase activity
|
22280
|
Individual variation in hepatic aldehyde oxidase activity
|
22281
|
Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible ...
|
22282
|
Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible ...
|
22283
|
Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible ...
|
22284
|
Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible ...
|
22285
|
Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible ...
|
22286
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22287
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22288
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22289
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22290
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22291
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22292
|
Human IMP dehydrogenase. Kinetics and regulatory properties
|
22293
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22294
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22295
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22296
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22297
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22298
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22299
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22300
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22301
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22302
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22303
|
Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the ...
|
22304
|
Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an ...
|
22305
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22306
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22307
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22308
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22309
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22310
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22311
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22312
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22313
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22314
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22315
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22316
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22317
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22318
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22319
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22320
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22321
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22322
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22323
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22324
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22325
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22326
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22327
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22328
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22329
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22330
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22331
|
Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within ...
|
22332
|
Sulfonamide resistance in Streptococcus pyogenes is associated with differences in the amino acid sequence of ...
|
22333
|
Sulfonamide resistance in Streptococcus pyogenes is associated with differences in the amino acid sequence of ...
|
22334
|
Sulfonamide resistance in Streptococcus pyogenes is associated with differences in the amino acid sequence of ...
|
22335
|
Sulfonamide resistance in Streptococcus pyogenes is associated with differences in the amino acid sequence of ...
|
22336
|
Metabolic activation of pradefovir by CYP3A4 and its potential as an inhibitor or inducer
|
22337
|
Metabolic activation of pradefovir by CYP3A4 and its potential as an inhibitor or inducer
|
22338
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22339
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22340
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22341
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22342
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22343
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22344
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22345
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22346
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22347
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22348
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22349
|
Glucose phosphorylation. Site-directed mutations which impair the catalytic function of hexokinase
|
22350
|
The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of ...
|
22351
|
The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of ...
|
22352
|
The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of ...
|
22353
|
The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of ...
|
22354
|
The vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of ...
|
22355
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22356
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22357
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22358
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22359
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22360
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22361
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22362
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22363
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22364
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22365
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22366
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22367
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22368
|
Characterization of chicken-liver glutathione S-transferase (GST) A1-1 and A2-2 isoenzymes and their ...
|
22369
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22370
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22371
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22372
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22373
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22374
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22375
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22376
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22377
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22378
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22379
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22380
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22381
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22382
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22383
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22384
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22385
|
A single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme ...
|
22386
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22387
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22388
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22389
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22390
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22391
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22392
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22393
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22394
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22395
|
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues ...
|
22396
|
The mature size of rat 4-aminobutyrate aminotransferase is different in liver and brain
|
22397
|
The mature size of rat 4-aminobutyrate aminotransferase is different in liver and brain
|
22398
|
DPNH peroxidase: effector activities of DPN
|
22399
|
Characterization and identification of an epidermal-growth-factor-activated phospholipase A2
|
22400
|
Effects of alternate RNA splicing on glucokinase isoform activities in the pancreatic islet, liver, and ...
|
22401
|
Effects of alternate RNA splicing on glucokinase isoform activities in the pancreatic islet, liver, and ...
|
22402
|
Effects of alternate RNA splicing on glucokinase isoform activities in the pancreatic islet, liver, and ...
|
22403
|
Effects of alternate RNA splicing on glucokinase isoform activities in the pancreatic islet, liver, and ...
|
22404
|
Effects of alternate RNA splicing on glucokinase isoform activities in the pancreatic islet, liver, and ...
|
22405
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
22406
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
22407
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
22408
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
22409
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
22410
|
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. ...
|
22411
|
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
|
22412
|
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
|
22413
|
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
|
22414
|
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
|
22415
|
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
|
22416
|
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
|
22417
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22418
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22419
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22420
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22421
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22422
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22423
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22424
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22425
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22426
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22427
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22428
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22429
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22430
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22431
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22432
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22433
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22434
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22435
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22436
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22437
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22438
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22439
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22440
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22441
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22442
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22443
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22444
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22445
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22446
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22447
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22448
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22449
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22450
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22451
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22452
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22453
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22454
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22455
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22456
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22457
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22458
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22459
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22460
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22461
|
Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
|
22462
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22463
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22464
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22465
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22466
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22467
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22468
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22469
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22470
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22471
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22472
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22473
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22474
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22475
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22476
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22477
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22478
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22479
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22480
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22481
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22482
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22483
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22484
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22485
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22486
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22487
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22488
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22489
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22490
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22491
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22492
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22493
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22494
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22495
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22496
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22497
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22498
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22499
|
Lid L11 of the glutamine amidotransferase domain of CTP synthase mediates allosteric GTP activation of ...
|
22500
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22501
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22502
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22503
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22504
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22505
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22506
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22507
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22508
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22509
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22510
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22511
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22512
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22513
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22514
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22515
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22516
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22517
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22518
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22519
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22520
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22521
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22522
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22523
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22524
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22525
|
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
|
22526
|
On the mechanism and control of the malonyl-CoA-dependent chain elongation of fatty acids. The ...
|
22527
|
On the mechanism and control of the malonyl-CoA-dependent chain elongation of fatty acids. The ...
|
22528
|
On the mechanism and control of the malonyl-CoA-dependent chain elongation of fatty acids. The ...
|
22529
|
On the mechanism and control of the malonyl-CoA-dependent chain elongation of fatty acids. The ...
|
22530
|
On the mechanism and control of the malonyl-CoA-dependent chain elongation of fatty acids. The ...
|
22531
|
On the mechanism and control of the malonyl-CoA-dependent chain elongation of fatty acids. The ...
|
22532
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22533
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22534
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22535
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22536
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22537
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22538
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22539
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22540
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22541
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22542
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22543
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22544
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22545
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22546
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22547
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22548
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22549
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22550
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22551
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22552
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22553
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22554
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22555
|
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the ...
|
22556
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22557
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22558
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22559
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22560
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22561
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22562
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22563
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22564
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22565
|
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of ...
|
22566
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22567
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22568
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22569
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22570
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22571
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22572
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22573
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22574
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22575
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22576
|
Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat ...
|
22577
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22578
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22579
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22580
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22581
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22582
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22583
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22584
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22585
|
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA ...
|
22586
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22587
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22588
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22589
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22590
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22591
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22592
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22593
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22594
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22595
|
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver ...
|
22596
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22597
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22598
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22599
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22600
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22601
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22602
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22603
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22604
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22605
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22606
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22607
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22608
|
Carbamyl and acetyl phosphokinase activities of Streptococcus faecalis and Escherichia coli
|
22609
|
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to ...
|
22610
|
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to ...
|
22611
|
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to ...
|
22612
|
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to ...
|
22613
|
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to ...
|
22614
|
Investigations on pantothenic acid and its related compounds. X. Biochemical studies. 5. Purification and ...
|
22615
|
Investigations on pantothenic acid and its related compounds. X. Biochemical studies. 5. Purification and ...
|
22616
|
Investigations on pantothenic acid and its related compounds. X. Biochemical studies. 5. Purification and ...
|
22617
|
Purification and characterization of amino-acid N-choloyltransferase from human liver
|
22618
|
Purification and characterization of amino-acid N-choloyltransferase from human liver
|
22619
|
Purification and characterization of amino-acid N-choloyltransferase from human liver
|
22620
|
Purification and characterization of amino-acid N-choloyltransferase from human liver
|
22621
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22622
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22623
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22624
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22625
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22626
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22627
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22628
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22629
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22630
|
Mouse mitochondrial aldehyde dehydrogenase isozymes: purification and molecular properties
|
22631
|
Kinetic properties of human pancreatic carboxylesterase
|
22632
|
Kinetic properties of human pancreatic carboxylesterase
|
22633
|
Kinetic properties of human pancreatic carboxylesterase
|
22634
|
Kinetic properties of human pancreatic carboxylesterase
|
22635
|
Kinetic properties of human pancreatic carboxylesterase
|
22636
|
Kinetic properties of human pancreatic carboxylesterase
|
22637
|
Kinetic properties of human pancreatic carboxylesterase
|
22638
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22639
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22640
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22641
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22642
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22643
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22644
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22645
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22646
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22647
|
Phosphoryl exchange reaction catalyzed by enzyme I of the bacterial phosphoenolpyruvate: sugar ...
|
22648
|
Biochemical characterization of cytosolic fructose-1,6-bisphosphatase from apple (Malus domestica) leaves
|
22649
|
Biochemical characterization of cytosolic fructose-1,6-bisphosphatase from apple (Malus domestica) leaves
|
22650
|
Biochemical characterization of cytosolic fructose-1,6-bisphosphatase from apple (Malus domestica) leaves
|
22651
|
Biochemical characterization of cytosolic fructose-1,6-bisphosphatase from apple (Malus domestica) leaves
|
22652
|
Biochemical characterization of cytosolic fructose-1,6-bisphosphatase from apple (Malus domestica) leaves
|
22653
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22654
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22655
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22656
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22657
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22658
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22659
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22660
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22661
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22662
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22663
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22664
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22665
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22666
|
Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of ...
|
22667
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22668
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22669
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22670
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22671
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22672
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22673
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22674
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22675
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22676
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22677
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22678
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22679
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22680
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22681
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22682
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22683
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22684
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22685
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22686
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22687
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22688
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22689
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22690
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22691
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22692
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22693
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22694
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22695
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22696
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22697
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22698
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22699
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22700
|
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
|
22701
|
Human hepatic methionine biosynthesis. Purification and characterization of betaine:homocysteine ...
|
22702
|
Human hepatic methionine biosynthesis. Purification and characterization of betaine:homocysteine ...
|
22703
|
Human hepatic methionine biosynthesis. Purification and characterization of betaine:homocysteine ...
|
22704
|
Human hepatic methionine biosynthesis. Purification and characterization of betaine:homocysteine ...
|
22705
|
Transiently reduced activity of carbamyl phosphate synthetase and ornithine transcarbamylase in liver of ...
|
22706
|
Transiently reduced activity of carbamyl phosphate synthetase and ornithine transcarbamylase in liver of ...
|
22707
|
Transiently reduced activity of carbamyl phosphate synthetase and ornithine transcarbamylase in liver of ...
|
22708
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22709
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22710
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22711
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22712
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22713
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22714
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22715
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22716
|
The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and ...
|
22717
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22718
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22719
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22720
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22721
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22722
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22723
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22724
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22725
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22726
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22727
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22728
|
An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
|
22729
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22730
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22731
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22732
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22733
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22734
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22735
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22736
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22737
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22738
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22739
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22740
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22741
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22742
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22743
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22744
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22745
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22746
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22747
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22748
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22749
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22750
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22751
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22752
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22753
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22754
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22755
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22756
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22757
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22758
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22759
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22760
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22761
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22762
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22763
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22764
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22765
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22766
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22767
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22768
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22769
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22770
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22771
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22772
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22773
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22774
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22775
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22776
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22777
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22778
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22779
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22780
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22781
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22782
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22783
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22784
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22785
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22786
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22787
|
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
|
22788
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22789
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22790
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22791
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22792
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22793
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22794
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22795
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22796
|
Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of ...
|
22797
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22798
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22799
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22800
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22801
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22802
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22803
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22804
|
Effect of ATP on glucose-6-phosphate isomerase from Bacillus caldotenax
|
22805
|
Role of L-citrulline transport in nitric oxide synthesis in rat aortic smooth muscle cells activated with LPS ...
|
22806
|
Role of L-citrulline transport in nitric oxide synthesis in rat aortic smooth muscle cells activated with LPS ...
|
22807
|
Role of L-citrulline transport in nitric oxide synthesis in rat aortic smooth muscle cells activated with LPS ...
|
22808
|
Role of L-citrulline transport in nitric oxide synthesis in rat aortic smooth muscle cells activated with LPS ...
|
22809
|
Role of L-citrulline transport in nitric oxide synthesis in rat aortic smooth muscle cells activated with LPS ...
|
22810
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22811
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22812
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22813
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22814
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22815
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22816
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22817
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22818
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22819
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22820
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22821
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22822
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22823
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22824
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22825
|
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
|
22826
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22827
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22828
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22829
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22830
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22831
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22832
|
Kinetic parameters and tissue distribution of 5-oxo-L-prolinase determined by a fluorimetric assay
|
22833
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22834
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22835
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22836
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22837
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22838
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22839
|
Analysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases
|
22840
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22841
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22842
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22843
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22844
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22845
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22846
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22847
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22848
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22849
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22850
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22851
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22852
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22853
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22854
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22855
|
The Enhanced Affinity for Thiolate Anion and Activation of Enzyme-bound Glutathione Is Governed by an Arginine ...
|
22856
|
Purification and characterisation of glyoxalase II from human red blood cells
|
22857
|
Purification and characterisation of glyoxalase II from human red blood cells
|
22858
|
Purification and characterisation of glyoxalase II from human red blood cells
|
22859
|
Purification and characterisation of glyoxalase II from human red blood cells
|
22860
|
Purification and characterisation of glyoxalase II from human red blood cells
|
22861
|
Purification and characterisation of glyoxalase II from human red blood cells
|
22862
|
Molecular cloning, heterologous expression, and characterization of human glyoxalase II
|
22863
|
Molecular cloning, heterologous expression, and characterization of human glyoxalase II
|
22864
|
Molecular cloning, heterologous expression, and characterization of human glyoxalase II
|
22865
|
Molecular cloning, heterologous expression, and characterization of human glyoxalase II
|
22866
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22867
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22868
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22869
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22870
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22871
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22872
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22873
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22874
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22875
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22876
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22877
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22878
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22879
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22880
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22881
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22882
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22883
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22884
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22885
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22886
|
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic ...
|
22887
|
Purification and characterization of human-brain aldose reductase
|
22888
|
Purification and characterization of human-brain aldose reductase
|
22889
|
Purification and characterization of human-brain aldose reductase
|
22890
|
Purification and characterization of human-brain aldose reductase
|
22891
|
Purification and characterization of human-brain aldose reductase
|
22892
|
Purification and characterization of human-brain aldose reductase
|
22893
|
Purification and characterization of human-brain aldose reductase
|
22894
|
Purification and characterization of human-brain aldose reductase
|
22895
|
Purification and characterization of human-brain aldose reductase
|
22896
|
Purification and characterization of human-brain aldose reductase
|
22897
|
Purification and characterization of human-brain aldose reductase
|
22898
|
Purification and characterization of human-brain aldose reductase
|
22899
|
Purification and characterization of human-brain aldose reductase
|
22900
|
Purification and characterization of human-brain aldose reductase
|
22901
|
Purification and characterization of human-brain aldose reductase
|
22902
|
Purification and characterization of human-brain aldose reductase
|
22903
|
Purification and characterization of human-brain aldose reductase
|
22904
|
Purification and characterization of human-brain aldose reductase
|
22905
|
Purification and characterization of human-brain aldose reductase
|
22906
|
Purification and characterization of human-brain aldose reductase
|
22907
|
Purification and characterization of human-brain aldose reductase
|
22908
|
Purification and characterization of human-brain aldose reductase
|
22909
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22910
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22911
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22912
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22913
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22914
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22915
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22916
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22917
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22918
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22919
|
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of ...
|
22920
|
Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in ...
|
22921
|
Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in ...
|
22922
|
Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in ...
|
22923
|
Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in ...
|
22924
|
Choline kinase and ethanolamine kinase are separate, soluble enzymes in rat liver
|
22925
|
Choline kinase and ethanolamine kinase are separate, soluble enzymes in rat liver
|
22926
|
Choline kinase and ethanolamine kinase are separate, soluble enzymes in rat liver
|
22927
|
Choline kinase and ethanolamine kinase are separate, soluble enzymes in rat liver
|
22928
|
Isolation of glyoxalase II from bovine liver mitochondria
|
22929
|
Isolation of glyoxalase II from bovine liver mitochondria
|
22930
|
Isolation of glyoxalase II from bovine liver mitochondria
|
22931
|
Isolation of glyoxalase II from bovine liver mitochondria
|
22932
|
Functionally accepted insertions of proteins within protein domains
|
22933
|
Functionally accepted insertions of proteins within protein domains
|
22934
|
Functionally accepted insertions of proteins within protein domains
|
22935
|
Functionally accepted insertions of proteins within protein domains
|
22936
|
Functionally accepted insertions of proteins within protein domains
|
22937
|
Functionally accepted insertions of proteins within protein domains
|
22938
|
Functionally accepted insertions of proteins within protein domains
|
22939
|
Functionally accepted insertions of proteins within protein domains
|
22940
|
Functionally accepted insertions of proteins within protein domains
|
22941
|
Functionally accepted insertions of proteins within protein domains
|
22942
|
Functionally accepted insertions of proteins within protein domains
|
22943
|
Functionally accepted insertions of proteins within protein domains
|
22944
|
Functionally accepted insertions of proteins within protein domains
|
22945
|
Functionally accepted insertions of proteins within protein domains
|
22946
|
Functionally accepted insertions of proteins within protein domains
|
22947
|
Functionally accepted insertions of proteins within protein domains
|
22948
|
Functionally accepted insertions of proteins within protein domains
|
22949
|
Isolation and overexpression of a gene encoding an extracellular beta-(1,3-1,4)-glucanase from Streptococcus ...
|
22950
|
Isolation and overexpression of a gene encoding an extracellular beta-(1,3-1,4)-glucanase from Streptococcus ...
|
22951
|
Isolation and overexpression of a gene encoding an extracellular beta-(1,3-1,4)-glucanase from Streptococcus ...
|
22952
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22953
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22954
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22955
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22956
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22957
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22958
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22959
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22960
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22961
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22962
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22963
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22964
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22965
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22966
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22967
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22968
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22969
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22970
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22971
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22972
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22973
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22974
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22975
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22976
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22977
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22978
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22979
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22980
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22981
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22982
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22983
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22984
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22985
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22986
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22987
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22988
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22989
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22990
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22991
|
Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial ...
|
22992
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22993
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22994
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22995
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22996
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22997
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22998
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
22999
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|
23000
|
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases
|