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1 te of the ACT-domain of the Escherichia coli phosphoglycerate dehydrogenase.
2 xtracts of M. maripaludis were shown to have phosphoglycerate dehydrogenase and phosphoserine aminotr
4 etate methyltransferase deficiency and for 3-phosphoglycerated dehydrogenase deficiency appear promis
8 resents a second structural motif of the D-3-phosphoglycerate dehydrogenase family, one that contains
13 The heterologously expressed and purified phosphoglycerate dehydrogenase from M. maripaludis had e
16 structure of Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase has been solved with boun
17 10 interacted with the chloroplastic protein phosphoglycerate dehydrogenase in a yeast (Saccharomyces
19 that predicts that catalytic activity in D-3-phosphoglycerate dehydrogenase is regulated by the movem
21 e catalytic activity of Escherichia coli D-3-phosphoglycerate dehydrogenase (PGDH) by binding to its
26 ructural homology with the ASB domain of d-3-phosphoglycerate dehydrogenase (PGDH) from Mycobacterium
28 ric hybrid tetramers of Escherichia coli d-3-phosphoglycerate dehydrogenase (PGDH) have been made by
29 topped-flow analysis of Escherichia coli d-3-phosphoglycerate dehydrogenase (PGDH) reveals that the p
32 ulatory and substrate binding domains of D-3-phosphoglycerate dehydrogenase (PGDH, EC 1.1.1.95) from
33 e, we present a detailed characterization of phosphoglycerate dehydrogenases (PGDHs) as components of
35 nately regulate expression of genes encoding phosphoglycerate dehydrogenase (PHGDH) and five downstre
39 BA, but not GH, caused a 2-fold increase in phosphoglycerate dehydrogenase (PHGDH) protein expressio
40 mes of the de novo serine synthesis pathway (phosphoglycerate dehydrogenase (PHGDH), phosphoserine am
41 uman cancers often exhibit overexpression of phosphoglycerate dehydrogenase (PHGDH), the metabolic en
45 of residues in the regulatory domains of D-3-phosphoglycerate dehydrogenase provide the first direct
49 n part to the genomic copy number gain for 3-phosphoglycerate dehydrogenase, the enzyme that controls
51 sphate pathway (PPP), while 2-PG activates 3-phosphoglycerate dehydrogenase to provide feedback contr
53 topped flow analysis of Escherichia coli D-3-phosphoglycerate dehydrogenase was performed by followin
54 and mice with targeted deletion of Srr or 3-Phosphoglycerate dehydrogenase, we demonstrate predomina
55 same fold; (iii) the C-terminal domain of 3-phosphoglycerate dehydrogenase, which binds serine and i
56 e structure of a truncated form of human d-3-phosphoglycerate dehydrogenase with cofactor and a subst
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