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17001
|
Allosteric kinetics of pyruvate kinase of Saccharomyces carlsbergensis
|
17002
|
Allosteric kinetics of pyruvate kinase of Saccharomyces carlsbergensis
|
17003
|
Allosteric kinetics of pyruvate kinase of Saccharomyces carlsbergensis
|
17004
|
Allosteric kinetics of pyruvate kinase of Saccharomyces carlsbergensis
|
17005
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17006
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17007
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17008
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17009
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17010
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17011
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17012
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17013
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17014
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17015
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17016
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17017
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17018
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17019
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17020
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17021
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17022
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17023
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17024
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17025
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17026
|
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
|
17027
|
Role of arginase in sciatectomized muscle
|
17028
|
Role of arginase in sciatectomized muscle
|
17029
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17030
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17031
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17032
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17033
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17034
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17035
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17036
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17037
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17038
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17039
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17040
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17041
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17042
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17043
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17044
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17045
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17046
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17047
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17048
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17049
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17050
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17051
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17052
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17053
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17054
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17055
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17056
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17057
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17058
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17059
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17060
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17061
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17062
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17063
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17064
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17065
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17066
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17067
|
The active sites of fructose 6-phosphate,2-kinase: fructose-2, 6-bisphosphatase from rat testis. Roles of ...
|
17068
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17069
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17070
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17071
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17072
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17073
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17074
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17075
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17076
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17077
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17078
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17079
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17080
|
Rat kidney L-alpha-hydroxy acid oxidase: isolation of enzyme with one flavine coenzyme per two subunits
|
17081
|
Identification and isolation on a large scale of guanylate kinase from human erythrocytes. Effects of ...
|
17082
|
Identification and isolation on a large scale of guanylate kinase from human erythrocytes. Effects of ...
|
17083
|
Identification and isolation on a large scale of guanylate kinase from human erythrocytes. Effects of ...
|
17084
|
Identification and isolation on a large scale of guanylate kinase from human erythrocytes. Effects of ...
|
17085
|
Identification and isolation on a large scale of guanylate kinase from human erythrocytes. Effects of ...
|
17086
|
Identification and isolation on a large scale of guanylate kinase from human erythrocytes. Effects of ...
|
17087
|
Inositol polyphosphate multikinase is a nuclear PI3-kinase with transcriptional regulatory activity
|
17088
|
Inositol polyphosphate multikinase is a nuclear PI3-kinase with transcriptional regulatory activity
|
17089
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17090
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17091
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17092
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17093
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17094
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17095
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17096
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17097
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17098
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17099
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17100
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17101
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17102
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17103
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17104
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17105
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17106
|
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
|
17107
|
Purification and Characterization of a Tripeptidase from Lactococcus lactis subsp. cremoris Wg2
|
17108
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17109
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17110
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17111
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17112
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17113
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17114
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17115
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17116
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17117
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17118
|
Identification of the GTP binding site of human glutamate dehydrogenase by cassette mutagenesis and ...
|
17119
|
Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle ...
|
17120
|
Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle ...
|
17121
|
Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle ...
|
17122
|
Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle ...
|
17123
|
Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle ...
|
17124
|
Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle ...
|
17125
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17126
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17127
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17128
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17129
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17130
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17131
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17132
|
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward ...
|
17133
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17134
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17135
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17136
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17137
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17138
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17139
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17140
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17141
|
Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase
|
17142
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17143
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17144
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17145
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17146
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17147
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17148
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17149
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17150
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17151
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17152
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17153
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17154
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17155
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17156
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17157
|
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
|
17158
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17159
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17160
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17161
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17162
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17163
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17164
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17165
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17166
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17167
|
Inhibition of rat liver arginase by an intermediate in NO biosynthesis, NG-hydroxy-L-arginine: implications ...
|
17168
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17169
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17170
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17171
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17172
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17173
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17174
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17175
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17176
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17177
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17178
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17179
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17180
|
Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.)
|
17181
|
An arginine regulated gamma-guanidobutyrate ureahydrolase from tench liver (Tinca tinca L.)
|
17182
|
An arginine regulated gamma-guanidobutyrate ureahydrolase from tench liver (Tinca tinca L.)
|
17183
|
An arginine regulated gamma-guanidobutyrate ureahydrolase from tench liver (Tinca tinca L.)
|
17184
|
An arginine regulated gamma-guanidobutyrate ureahydrolase from tench liver (Tinca tinca L.)
|
17185
|
An arginine regulated gamma-guanidobutyrate ureahydrolase from tench liver (Tinca tinca L.)
|
17186
|
Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3)
|
17187
|
Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3)
|
17188
|
Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3)
|
17189
|
Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3)
|
17190
|
Metabolism of melatonin by human cytochromes p450
|
17191
|
Metabolism of melatonin by human cytochromes p450
|
17192
|
Metabolism of melatonin by human cytochromes p450
|
17193
|
Metabolism of melatonin by human cytochromes p450
|
17194
|
A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase
|
17195
|
A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase
|
17196
|
A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase
|
17197
|
A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase
|
17198
|
A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase
|
17199
|
A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase
|
17200
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17201
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17202
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17203
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17204
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17205
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17206
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17207
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17208
|
Functional characterization of single nucleotide polymorphisms with amino acid substitution in CYP1A2, CYP2A6, ...
|
17209
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17210
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17211
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17212
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17213
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17214
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17215
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17216
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17217
|
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
|
17218
|
Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases/phosphodiesterases
|
17219
|
Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases/phosphodiesterases
|
17220
|
Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases/phosphodiesterases
|
17221
|
A novel non-catalytic mechanism employed by the C-terminal Src-homologous kinase to inhibit Src-family kinase ...
|
17222
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17223
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17224
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17225
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17226
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17227
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17228
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17229
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17230
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17231
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17232
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17233
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17234
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17235
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17236
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17237
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17238
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17239
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17240
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17241
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17242
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17243
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17244
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17245
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17246
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17247
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17248
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17249
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17250
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17251
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17252
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17253
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17254
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17255
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17256
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17257
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17258
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17259
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17260
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17261
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17262
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17263
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17264
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17265
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17266
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17267
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17268
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17269
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17270
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17271
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17272
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17273
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17274
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17275
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17276
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17277
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17278
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17279
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17280
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17281
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17282
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17283
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17284
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17285
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17286
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17287
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17288
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17289
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17290
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17291
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17292
|
Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis
|
17293
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17294
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17295
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17296
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17297
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17298
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17299
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17300
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17301
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17302
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17303
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17304
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17305
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17306
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17307
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17308
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17309
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17310
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17311
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17312
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17313
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17314
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17315
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17316
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17317
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17318
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17319
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17320
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17321
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17322
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17323
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17324
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17325
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17326
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17327
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17328
|
Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic ...
|
17329
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17330
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17331
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17332
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17333
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17334
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17335
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17336
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17337
|
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases
|
17338
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17339
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17340
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17341
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17342
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17343
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17344
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17345
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17346
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17347
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17348
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17349
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17350
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17351
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17352
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17353
|
Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
|
17354
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17355
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17356
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17357
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17358
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17359
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17360
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17361
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17362
|
Isoenzymes of phosphofructokinase in the rat. Demonstration of the three non-identical subunits by ...
|
17363
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17364
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17365
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17366
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17367
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17368
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17369
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17370
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17371
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17372
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17373
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17374
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17375
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17376
|
New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase ...
|
17377
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17378
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17379
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17380
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17381
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17382
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17383
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17384
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17385
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17386
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17387
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17388
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17389
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17390
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17391
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17392
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17393
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17394
|
Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the ...
|
17395
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17396
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17397
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17398
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17399
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17400
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17401
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17402
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17403
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17404
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17405
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17406
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17407
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17408
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17409
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17410
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17411
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17412
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17413
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17414
|
Purification and characterization of guinea pig liver morphine 6-dehydrogenase
|
17415
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17416
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17417
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17418
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17419
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17420
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17421
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17422
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17423
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17424
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17425
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17426
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17427
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17428
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17429
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17430
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17431
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17432
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17433
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17434
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17435
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17436
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17437
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17438
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17439
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17440
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17441
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17442
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17443
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17444
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17445
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17446
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17447
|
Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by ...
|
17448
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17449
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17450
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17451
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17452
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17453
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17454
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17455
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17456
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17457
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17458
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17459
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17460
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17461
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17462
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17463
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17464
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17465
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17466
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17467
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17468
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17469
|
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on ...
|
17470
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17471
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17472
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17473
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17474
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17475
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17476
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17477
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17478
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17479
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17480
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17481
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17482
|
Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium ...
|
17483
|
Amine N-methyltransferases from rabbit liver
|
17484
|
Amine N-methyltransferases from rabbit liver
|
17485
|
Amine N-methyltransferases from rabbit liver
|
17486
|
Amine N-methyltransferases from rabbit liver
|
17487
|
Amine N-methyltransferases from rabbit liver
|
17488
|
Amine N-methyltransferases from rabbit liver
|
17489
|
Amine N-methyltransferases from rabbit liver
|
17490
|
Amine N-methyltransferases from rabbit liver
|
17491
|
Amine N-methyltransferases from rabbit liver
|
17492
|
Amine N-methyltransferases from rabbit liver
|
17493
|
Amine N-methyltransferases from rabbit liver
|
17494
|
Amine N-methyltransferases from rabbit liver
|
17495
|
Amine N-methyltransferases from rabbit liver
|
17496
|
Amine N-methyltransferases from rabbit liver
|
17497
|
Amine N-methyltransferases from rabbit liver
|
17498
|
Amine N-methyltransferases from rabbit liver
|
17499
|
Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2
|
17500
|
Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2
|
17501
|
Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2
|
17502
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17503
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17504
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17505
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17506
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17507
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17508
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17509
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17510
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17511
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17512
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17513
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17514
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17515
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17516
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17517
|
Further studies of the role of Ser-16 in the regulation of the activity of phenylalanine hydroxylase
|
17518
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17519
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17520
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17521
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17522
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17523
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17524
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17525
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17526
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17527
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17528
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17529
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17530
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17531
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17532
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17533
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17534
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17535
|
Purification and properties of the aromatic amino acid aminotransferase from gramicidin S-producing Bacillus ...
|
17536
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17537
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17538
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17539
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17540
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17541
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17542
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17543
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17544
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17545
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17546
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17547
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17548
|
Purification and characterization of cytosol phosphoenolpyruvate carboxykinase from bullfrog (Rana ...
|
17580
|
Kinetic properties and regulation by L-ornithine of chicken liver arginase induced by insulin
|
17581
|
Kinetic properties and regulation by L-ornithine of chicken liver arginase induced by insulin
|
17582
|
Kinetic properties and regulation by L-ornithine of chicken liver arginase induced by insulin
|
17589
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17590
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17591
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17592
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17593
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17594
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17595
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17596
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17597
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17598
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17599
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17600
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17601
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17602
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17603
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17604
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17605
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17606
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17607
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17608
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17609
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17610
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17611
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17612
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17613
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17614
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17615
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17616
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17617
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17618
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17619
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17620
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17621
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17622
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17623
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17624
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17625
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17626
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17627
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17628
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17629
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17630
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17631
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17632
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17633
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17634
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17635
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17636
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17637
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17638
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17639
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17640
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17641
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17642
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17643
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17644
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17645
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17646
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17647
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17648
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17649
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17650
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17651
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17652
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17653
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17654
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17655
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17656
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17657
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17658
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17659
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17660
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17661
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17662
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17663
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17664
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17665
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17666
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17667
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17668
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17669
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17670
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17671
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17672
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17673
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17674
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17675
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17676
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17677
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17678
|
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney
|
17679
|
Regulation of lactose catabolism in Streptococcus mutans: purification and regulatory properties of ...
|
17680
|
Regulation of lactose catabolism in Streptococcus mutans: purification and regulatory properties of ...
|
17681
|
Regulation of lactose catabolism in Streptococcus mutans: purification and regulatory properties of ...
|
17682
|
Regulation of lactose catabolism in Streptococcus mutans: purification and regulatory properties of ...
|
17683
|
Regulation of lactose catabolism in Streptococcus mutans: purification and regulatory properties of ...
|
17684
|
Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of ...
|
17685
|
Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of ...
|
17686
|
Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of ...
|
17687
|
Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of ...
|
17688
|
Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of ...
|
17689
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17690
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17691
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17692
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17693
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17694
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17695
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17696
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17697
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17698
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17699
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17700
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17701
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17702
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17703
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17704
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17705
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17706
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17707
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17708
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17709
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17710
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17711
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17712
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17713
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17714
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17715
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17716
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17717
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17718
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17719
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17720
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17721
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17722
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17723
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17724
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17725
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17726
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17727
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17728
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17729
|
Purine Nucleoside Phosphorylase. 1. Structure-Function Studies
|
17730
|
Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8
|
17731
|
Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8
|
17732
|
Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8
|
17733
|
Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8
|
17734
|
Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8
|
17735
|
Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8
|
17736
|
Deletion of the four C-terminal residues of PepC converts an aminopeptidase into an oligopeptidase
|
17737
|
Deletion of the four C-terminal residues of PepC converts an aminopeptidase into an oligopeptidase
|
17738
|
Deletion of the four C-terminal residues of PepC converts an aminopeptidase into an oligopeptidase
|
17739
|
Deletion of the four C-terminal residues of PepC converts an aminopeptidase into an oligopeptidase
|
17740
|
tRNA-guanine transglycosylase from Escherichia coli: gross tRNA structural requirements for recognition
|
17741
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17742
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17743
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17744
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17745
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17746
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17747
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17748
|
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1
|
17759
|
Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium ...
|
17760
|
Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium ...
|
17761
|
Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium ...
|
17762
|
Purification and Characterization of an Aminopeptidase from Lactococcus lactis subsp. cremoris AM2
|
17763
|
Purification of a putative K+-ATPase from Streptococcus faecalis
|
17764
|
Purification of a putative K+-ATPase from Streptococcus faecalis
|
17765
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17766
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17767
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17768
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17769
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17770
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17771
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17772
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17773
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17774
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17775
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17776
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17777
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17778
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17779
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17780
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17781
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17782
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17783
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17784
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17785
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17786
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17787
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17788
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17789
|
Functional characterization of OXA-57, a class D beta-lactamase from Burkholderia pseudomallei
|
17790
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17791
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17792
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17793
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17794
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17795
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17796
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17797
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17798
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17799
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17800
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17801
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17802
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17803
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17804
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17805
|
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
|
17806
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17807
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17808
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17809
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17810
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17811
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17812
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17813
|
Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.
|
17814
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17815
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17816
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17817
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17818
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17819
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17820
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17821
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17822
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17823
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17824
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17825
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17826
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17827
|
An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. ...
|
17828
|
Inhibition of yeast phosphoglycerate kinase by lanthanide-ATP complexes
|
17829
|
Inhibition of yeast phosphoglycerate kinase by lanthanide-ATP complexes
|
17830
|
Inhibition of yeast phosphoglycerate kinase by lanthanide-ATP complexes
|
17831
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17832
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17833
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17834
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17835
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17836
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17837
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17838
|
Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of ...
|
17846
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17847
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17848
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17849
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17850
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17851
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17852
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17853
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17854
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17855
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17856
|
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of ...
|
17857
|
Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin ...
|
17858
|
Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin ...
|
17859
|
Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin ...
|
17860
|
Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin ...
|
17861
|
Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin ...
|
17862
|
Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin ...
|
17863
|
Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes simplex Virus Type 1 ...
|
17864
|
Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes simplex Virus Type 1 ...
|
17865
|
Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes simplex Virus Type 1 ...
|
17866
|
Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes simplex Virus Type 1 ...
|
17867
|
Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes simplex Virus Type 1 ...
|
17868
|
Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes simplex Virus Type 1 ...
|
17869
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17870
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17871
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17872
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17873
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17874
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17875
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17876
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17877
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17878
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17879
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17880
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17881
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17882
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17883
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17884
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17885
|
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
|
17886
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17887
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17888
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17889
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17890
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17891
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17892
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17893
|
Arginine-specific modification of rabbit muscle phosphoglucose isomerase: differences in the inactivation by ...
|
17894
|
Isolation and characterization of cytosolic alanine aminotransferase isoforms from starved rat liver
|
17895
|
Isolation and characterization of cytosolic alanine aminotransferase isoforms from starved rat liver
|
17896
|
Isolation and characterization of cytosolic alanine aminotransferase isoforms from starved rat liver
|
17897
|
Isolation and characterization of cytosolic alanine aminotransferase isoforms from starved rat liver
|
17900
|
Partial purification and kinetic properties of human placental cytosolic aspartate transaminase
|
17901
|
Partial purification and kinetic properties of human placental cytosolic aspartate transaminase
|
17902
|
Partial purification and kinetic properties of human placental cytosolic aspartate transaminase
|
17903
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17904
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17905
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17906
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17907
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17908
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17909
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17910
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17911
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17912
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17913
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17914
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17915
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17916
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17917
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17918
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17919
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17920
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17921
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17922
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17923
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17924
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17925
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17926
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17927
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17928
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17929
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17930
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17931
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17932
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17933
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17934
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17935
|
UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation
|
17936
|
Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa ...
|
17937
|
Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa ...
|
17938
|
Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa ...
|
17939
|
Human fatty acid synthase: properties and molecular cloning
|
17940
|
Human fatty acid synthase: properties and molecular cloning
|
17941
|
Human fatty acid synthase: properties and molecular cloning
|
17942
|
Human fatty acid synthase: properties and molecular cloning
|
17968
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17969
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17970
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17971
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17972
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17973
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17974
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17975
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17976
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17977
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17978
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17979
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17980
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17981
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17982
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17983
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17984
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17985
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17986
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17987
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17988
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17989
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17990
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17991
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17992
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17993
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17994
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17995
|
The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of ...
|
17996
|
Hydrolytic metabolism of pyrethroids by human and other mammalian carboxylesterases
|
17997
|
Hydrolytic metabolism of pyrethroids by human and other mammalian carboxylesterases
|
17998
|
Hydrolytic metabolism of pyrethroids by human and other mammalian carboxylesterases
|
17999
|
Hydrolytic metabolism of pyrethroids by human and other mammalian carboxylesterases
|
18000
|
Hydrolytic metabolism of pyrethroids by human and other mammalian carboxylesterases
|