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19003
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19004
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19005
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19006
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19007
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19008
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19009
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19010
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19011
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19012
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19013
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19014
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19015
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19016
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19017
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19018
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19019
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19020
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19021
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19022
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19023
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19024
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19025
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19026
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19027
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19028
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19029
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19030
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19031
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19032
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19033
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19034
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19035
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19036
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19037
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19038
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19039
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19040
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19041
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19042
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19043
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19044
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19045
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19046
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19047
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19048
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19049
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19050
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19051
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19052
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19053
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19054
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19055
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19056
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19057
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19058
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19059
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19060
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19061
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19062
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19063
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19064
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19065
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19066
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19067
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19068
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19069
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19070
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19071
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19072
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19073
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19074
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19075
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19076
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19077
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19078
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19079
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19080
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19081
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19082
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19083
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19084
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19085
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19086
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19087
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19088
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19089
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19090
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19091
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19092
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19093
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19094
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19095
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19096
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19097
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19098
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19099
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19100
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19101
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19102
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19103
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19104
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19105
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19106
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19107
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19108
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19109
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19110
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19111
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19112
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19113
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19114
|
Purification and characterization of prostaglandin F synthase from bovine liver
|
19184
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19185
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19186
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19187
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19188
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19189
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19190
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19191
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19192
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19193
|
AMP-deaminase from normal and cirrhotic human liver: a comparative study
|
19194
|
Inhibition of phosphoglycerate kinase by salicylates
|
19195
|
Inhibition of phosphoglycerate kinase by salicylates
|
19196
|
Inhibition of phosphoglycerate kinase by salicylates
|
19197
|
Inhibition of phosphoglycerate kinase by salicylates
|
19198
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19199
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19200
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19201
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19202
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19203
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19204
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19205
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19206
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19207
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19208
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19209
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19210
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19211
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19212
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19213
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19214
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19215
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19216
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19217
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19218
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19219
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19220
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19221
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19222
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19223
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19224
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19225
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19226
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19227
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19228
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19229
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19230
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19231
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19232
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19233
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19234
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19235
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19236
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19237
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19238
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19239
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19240
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19241
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19242
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19243
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19244
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19245
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19246
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19247
|
Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose ...
|
19248
|
Effects of novel anti-viral adenosine analogues on the activity of S-adenosylhomocysteine hydrolase from human ...
|
19249
|
Effects of novel anti-viral adenosine analogues on the activity of S-adenosylhomocysteine hydrolase from human ...
|
19250
|
Effects of novel anti-viral adenosine analogues on the activity of S-adenosylhomocysteine hydrolase from human ...
|
19251
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19252
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19253
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19254
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19255
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19256
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19257
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19258
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19259
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19260
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19261
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19262
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19263
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19264
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19265
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19266
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19267
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19268
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19269
|
Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from ...
|
19270
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19271
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19272
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19273
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19274
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19275
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19276
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19277
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19278
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19279
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19280
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19281
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19282
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19283
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19284
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19285
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19286
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19287
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19288
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19289
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19290
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19291
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19292
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19293
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19294
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19295
|
Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic ...
|
19296
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19297
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19298
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19299
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19300
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19301
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19302
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19303
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19304
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19305
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19306
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19307
|
Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D ...
|
19308
|
Purification and kinetic mechanism of a mammalian methionine synthase from pig liver
|
19309
|
Purification and kinetic mechanism of a mammalian methionine synthase from pig liver
|
19310
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19311
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19312
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19313
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19314
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19315
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19316
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19317
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19318
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19319
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19320
|
Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human ...
|
19321
|
Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase
|
19322
|
Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase
|
19323
|
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
|
19324
|
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
|
19325
|
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
|
19326
|
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
|
19327
|
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
|
19328
|
INHIBITION BY 5-AZAURACIL OF THE URIDINE PHOSPHORYLASE AND DEOXYURIDINE PHOSPHORYLASE ACTIVITIES IN CELL-FREE ...
|
19329
|
INHIBITION BY 5-AZAURACIL OF THE URIDINE PHOSPHORYLASE AND DEOXYURIDINE PHOSPHORYLASE ACTIVITIES IN CELL-FREE ...
|
19330
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19331
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19332
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19333
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19334
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19335
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19336
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19337
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19338
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19339
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19340
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19341
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19342
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19343
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19344
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19345
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19346
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19347
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19348
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19349
|
Regulation of Protein Kinase D by Multisite Phosphorylation IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS ...
|
19350
|
Metabolism of the ketoaldehyde 2-keto-3-deoxyglucose
|
19351
|
Metabolism of the ketoaldehyde 2-keto-3-deoxyglucose
|
19352
|
Metabolism of the ketoaldehyde 2-keto-3-deoxyglucose
|
19353
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19354
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19355
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19356
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19357
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19358
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19359
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19360
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19361
|
A second dihydroorotate dehydrogenase (Type A) of the human pathogen Enterococcus faecalis: expression, ...
|
19362
|
The sialic acids. X. Purification and properties of cytidine 5`-monophosphosialic acid synthetase
|
19363
|
The sialic acids. X. Purification and properties of cytidine 5`-monophosphosialic acid synthetase
|
19364
|
The sialic acids. X. Purification and properties of cytidine 5`-monophosphosialic acid synthetase
|
19365
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19366
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19367
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19368
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19369
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19370
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19371
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19372
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19373
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19374
|
Partial purification and regulatory properties of phosphofructokinase from Aspergillus niger
|
19375
|
Pyridoxine biosynthesis in yeast: participation of ribose 5-phosphate ketol-isomerase
|
19376
|
Pyridoxine biosynthesis in yeast: participation of ribose 5-phosphate ketol-isomerase
|
19377
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19378
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19379
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19380
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19381
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19382
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19383
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19384
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19385
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19386
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19387
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19388
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19389
|
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed ...
|
19390
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19391
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19392
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19393
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19394
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19395
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19396
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19397
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19398
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19399
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19400
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19401
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19402
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19403
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19404
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19405
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19406
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19407
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19408
|
The human UDP-glucuronosyltransferase: identification of key residues within the nucleotide-sugar binding site
|
19409
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19410
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19411
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19412
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19413
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19414
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19415
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19416
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19417
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19418
|
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, ...
|
19419
|
Purification and characterization of biliverdin reductase from rat liver
|
19420
|
Purification and characterization of biliverdin reductase from rat liver
|
19421
|
Purification and characterization of biliverdin reductase from rat liver
|
19422
|
Purification and characterization of biliverdin reductase from rat liver
|
19423
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19424
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19425
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19426
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19427
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19428
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19429
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19430
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19431
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19432
|
Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the ...
|
19433
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19434
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19435
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19436
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19437
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19438
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19439
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19440
|
Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (pdc) and comparison to ...
|
19441
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19442
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19443
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19444
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19445
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19446
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19447
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19448
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19449
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19450
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19451
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19452
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19453
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19454
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19455
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19456
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19457
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19458
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19459
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19460
|
Site-directed mutagenesis of a loop at the active site of E1 (alpha2beta2) of the pyruvate dehydrogenase ...
|
19461
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19462
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19463
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19464
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19465
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19466
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19467
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19468
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19469
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19470
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19471
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19472
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19473
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19474
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19475
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19476
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19477
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19478
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19479
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19480
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19481
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19482
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19483
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19484
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19485
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19486
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19487
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19488
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19489
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19490
|
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
|
19491
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19492
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19493
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19494
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19495
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19496
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19497
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19498
|
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by ...
|
19499
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19500
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19501
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19502
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19503
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19504
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19505
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19506
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19507
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19508
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19509
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19510
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19511
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19512
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19513
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19514
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19515
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19516
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19517
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19518
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19519
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19520
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19521
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19522
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19523
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19524
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19525
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19526
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19527
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19528
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19529
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19530
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19531
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19532
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19533
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19534
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19535
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19536
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19537
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19538
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19539
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19540
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19541
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19542
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19543
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19544
|
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
|
19545
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19546
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19547
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19548
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19549
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19550
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19551
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19552
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19553
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19554
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19555
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19556
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19557
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19558
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19559
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19560
|
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the ...
|
19561
|
Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused ...
|
19562
|
Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused ...
|
19563
|
Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused ...
|
19564
|
Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused ...
|
19565
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19566
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19567
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19568
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19569
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19570
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19571
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19572
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19573
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19574
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19575
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19576
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19577
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19578
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19579
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19580
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19581
|
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo ...
|
19582
|
Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate beta-lyases, but ...
|
19583
|
Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate beta-lyases, but ...
|
19584
|
Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate beta-lyases, but ...
|
19585
|
Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate beta-lyases, but ...
|
19586
|
Apo and holo structures of an NADPH-dependent cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae
|
19587
|
Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer
|
19588
|
Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer
|
19589
|
Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer
|
19590
|
Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer
|
19591
|
An improved spectrophotometric assay of pyruvate dehydrogenase in lactate dehydrogenase contaminated ...
|
19592
|
An improved spectrophotometric assay of pyruvate dehydrogenase in lactate dehydrogenase contaminated ...
|
19593
|
An improved spectrophotometric assay of pyruvate dehydrogenase in lactate dehydrogenase contaminated ...
|
19594
|
Characterization of a new plasma membrane-associated ecto-5`-phosphodiesterase/nucleotide-pyrophosphatase from ...
|
19595
|
Characterization of a new plasma membrane-associated ecto-5`-phosphodiesterase/nucleotide-pyrophosphatase from ...
|
19596
|
Characterization of a new plasma membrane-associated ecto-5`-phosphodiesterase/nucleotide-pyrophosphatase from ...
|
19597
|
Characterization of a new plasma membrane-associated ecto-5`-phosphodiesterase/nucleotide-pyrophosphatase from ...
|
19598
|
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
|
19599
|
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
|
19600
|
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
|
19601
|
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
|
19602
|
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
|
19603
|
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
|
19604
|
Aldose reductase activation is a key component of myocardial response to ischemia
|
19605
|
Aldose reductase activation is a key component of myocardial response to ischemia
|
19606
|
Aldose reductase activation is a key component of myocardial response to ischemia
|
19607
|
Aldose reductase activation is a key component of myocardial response to ischemia
|
19608
|
Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by ...
|
19609
|
Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by ...
|
19610
|
Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by ...
|
19611
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19612
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19613
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19614
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19615
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19616
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19617
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19618
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19619
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19620
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19621
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19622
|
Heparinase I from Flavobacterium heparinum-role of positive charge in enzymatic activity
|
19623
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19624
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19625
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19626
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19627
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19628
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19629
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19630
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19631
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19632
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19633
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19634
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19635
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19636
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19637
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19638
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19639
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19640
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19641
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19642
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19643
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19644
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19645
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19646
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19647
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19648
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19649
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19650
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19651
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19652
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19653
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19654
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19655
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19656
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19657
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19658
|
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: ...
|
19659
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19660
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19661
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19662
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19663
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19664
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19665
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19666
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19667
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19668
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19669
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19670
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19671
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19672
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19673
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19674
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19675
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19676
|
Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and ...
|
19677
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19678
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19679
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19680
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19681
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19682
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19683
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19684
|
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain ...
|
19685
|
Arginine modification with butanedione inhibits the potassium ATPase of Streptococcus faecalis
|
19686
|
Arginine modification with butanedione inhibits the potassium ATPase of Streptococcus faecalis
|
19687
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19688
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19689
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19690
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19691
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19692
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19693
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19694
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19695
|
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
|
19696
|
Identification and characterization of the phosphatidylinositol-(4, 5)-bisphosphate 5-phosphatase in human ...
|
19697
|
Identification and characterization of the phosphatidylinositol-(4, 5)-bisphosphate 5-phosphatase in human ...
|
19698
|
Identification and characterization of the phosphatidylinositol-(4, 5)-bisphosphate 5-phosphatase in human ...
|
19699
|
Identification and characterization of the phosphatidylinositol-(4, 5)-bisphosphate 5-phosphatase in human ...
|
19700
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19701
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19702
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19703
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19704
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19705
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19706
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19707
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19708
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19709
|
Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: phosphate dependence and effects of other ...
|
19710
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19711
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19712
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19713
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19714
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19715
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19716
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19717
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19718
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19719
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19720
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19721
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19722
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19723
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19724
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19725
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19726
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19727
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19728
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19729
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19730
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19731
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19732
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19733
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19734
|
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the ...
|
19735
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19736
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19737
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19738
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19739
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19740
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19741
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19742
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19743
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19744
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19745
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19746
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19747
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19748
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19749
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19750
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19751
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19752
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19753
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19754
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19755
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19756
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19757
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19758
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19759
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19760
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19761
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19762
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19763
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19764
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19765
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19766
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19767
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19768
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19769
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19770
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19771
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19772
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19773
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19774
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19775
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19776
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19777
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19778
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19779
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19780
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19781
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19782
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19783
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19784
|
Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of Cysteine ...
|
19785
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19786
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19787
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19788
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19789
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19790
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19791
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19792
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19793
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19794
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19795
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19796
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19797
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19798
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19799
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19800
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19801
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19802
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19803
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19804
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19805
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19806
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19807
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19808
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19809
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19810
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19811
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19812
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19813
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19814
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19815
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19816
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19817
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19818
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19819
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19820
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19821
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19822
|
Engineering the Substrate specificity of the Abl Tyrosine Kinase
|
19823
|
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to ...
|
19824
|
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to ...
|
19825
|
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to ...
|
19826
|
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to ...
|
19827
|
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to ...
|
19828
|
An inhibitor of the human UDP-GlcNAc 4-epimerase identified from a uridine-based library: a strategy to ...
|
19833
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19834
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19835
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19836
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19837
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19838
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19839
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19840
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19841
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19842
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19843
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19844
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19845
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19846
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19847
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19848
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19849
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19850
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19851
|
Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain
|
19852
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19853
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19854
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19855
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19856
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19857
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19858
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19859
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19860
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19861
|
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of ...
|
19862
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19863
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19864
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19865
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19866
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19867
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19868
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19869
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19870
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19871
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19872
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19873
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19874
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19875
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19876
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19877
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19878
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19879
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19880
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19881
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19882
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19883
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19884
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19885
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19886
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19887
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19888
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19889
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19890
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19891
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19892
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19893
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19894
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19895
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19896
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19897
|
Identification and subcellular localization of sphinganine-phosphatases in rat liver
|
19898
|
Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli ...
|
19899
|
Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli ...
|
19900
|
The mechanism of 6-deoxyhexose synthesis. 3. Purification of deosythymidine diphosphate-glucose oxidoreductase
|
19901
|
The mechanism of 6-deoxyhexose synthesis. 3. Purification of deosythymidine diphosphate-glucose oxidoreductase
|
19902
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19903
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19904
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19905
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19906
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19907
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19908
|
A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, ...
|
19909
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19910
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19911
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19912
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19913
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19914
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19915
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19916
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19917
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19918
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19919
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19920
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19921
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19922
|
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other ...
|
19923
|
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
19924
|
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
19925
|
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
19926
|
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
19927
|
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
19928
|
Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
|
19929
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19930
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19931
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19932
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19933
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19934
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19935
|
Polyol metabolism by a caries-conducive Streptococcus: purification and properties of a nicotinamide adenine ...
|
19936
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19937
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19938
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19939
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19940
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19941
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19942
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19943
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19944
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19945
|
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi
|
19946
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19947
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19948
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19949
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19950
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19951
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19952
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19953
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19954
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19955
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19956
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19957
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19958
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19959
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19960
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19961
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19962
|
Kinetic characterization of recombinant human cytosolic phosphoenolpyruvate carboxykinase with and without a ...
|
19963
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19964
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19965
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19966
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19967
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19968
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19969
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19970
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19971
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19972
|
Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea ...
|
19973
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19974
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19975
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19976
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19977
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19978
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19979
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19980
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19981
|
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas ...
|
19982
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19983
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19984
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19985
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19986
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19987
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19988
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19989
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19990
|
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis
|
19991
|
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: ...
|
19992
|
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: ...
|
19993
|
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: ...
|
19994
|
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: ...
|
19995
|
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: ...
|
19996
|
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: ...
|
19997
|
Purification and characterization of a neutral ceramidase from mouse liver. A single protein catalyzes the ...
|
19998
|
Purification and characterization of a neutral ceramidase from mouse liver. A single protein catalyzes the ...
|
19999
|
Purification and characterization of a neutral ceramidase from mouse liver. A single protein catalyzes the ...
|
20000
|
Purification and characterization of a neutral ceramidase from mouse liver. A single protein catalyzes the ...
|