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1 te of the ACT-domain of the Escherichia coli phosphoglycerate dehydrogenase.
4 xtracts of M. maripaludis were shown to have phosphoglycerate dehydrogenase and phosphoserine aminotr
5 mes in the serine synthesis pathway, such as phosphoglycerate dehydrogenase and phosphoserine aminotr
6 1 enhances the expression of the key enzymes phosphoglycerate dehydrogenase and phosphoserine aminotr
8 strongest associations were observed for D-3-phosphoglycerate dehydrogenase (D-3PGDH), cysteine and g
9 etate methyltransferase deficiency and for 3-phosphoglycerated dehydrogenase deficiency appear promis
10 intenance of the purine metabolizing enzyme, phosphoglycerate dehydrogenase, during LPS plus ATP trea
14 resents a second structural motif of the D-3-phosphoglycerate dehydrogenase family, one that contains
19 The heterologously expressed and purified phosphoglycerate dehydrogenase from M. maripaludis had e
22 structure of Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase has been solved with boun
23 10 interacted with the chloroplastic protein phosphoglycerate dehydrogenase in a yeast (Saccharomyces
25 that predicts that catalytic activity in D-3-phosphoglycerate dehydrogenase is regulated by the movem
26 tarate, facilitated by increased activity of phosphoglycerate dehydrogenase, leads to epigenetic alte
28 e catalytic activity of Escherichia coli D-3-phosphoglycerate dehydrogenase (PGDH) by binding to its
33 ructural homology with the ASB domain of d-3-phosphoglycerate dehydrogenase (PGDH) from Mycobacterium
35 ric hybrid tetramers of Escherichia coli d-3-phosphoglycerate dehydrogenase (PGDH) have been made by
36 topped-flow analysis of Escherichia coli d-3-phosphoglycerate dehydrogenase (PGDH) reveals that the p
39 ulatory and substrate binding domains of D-3-phosphoglycerate dehydrogenase (PGDH, EC 1.1.1.95) from
40 e, we present a detailed characterization of phosphoglycerate dehydrogenases (PGDHs) as components of
43 nately regulate expression of genes encoding phosphoglycerate dehydrogenase (PHGDH) and five downstre
45 anically, NAT10 promotes the expression of 3-phosphoglycerate dehydrogenase (PHGDH) and phosphoserine
49 EVs, leading to a paracrine upregulation of phosphoglycerate dehydrogenase (PHGDH) in monocytes when
52 ction of circulating serine by inhibition of phosphoglycerate dehydrogenase (PHGDH) leads to the accu
53 hat altered expression of the LOAD biomarker phosphoglycerate dehydrogenase (PHGDH) modulates AD path
55 BA, but not GH, caused a 2-fold increase in phosphoglycerate dehydrogenase (PHGDH) protein expressio
56 nificance with multiple testing adjustments, phosphoglycerate dehydrogenase (PHGDH) was the only gene
57 mes of the de novo serine synthesis pathway (phosphoglycerate dehydrogenase (PHGDH), phosphoserine am
58 acid generated by the sequential actions of phosphoglycerate dehydrogenase (PHGDH), phosphoserine am
61 uman cancers often exhibit overexpression of phosphoglycerate dehydrogenase (PHGDH), the metabolic en
62 0) show that MEKi-resistant cells upregulate phosphoglycerate dehydrogenase (PHGDH), the rate-limitin
63 etween lipid metabolism and ERneg BC through phosphoglycerate dehydrogenase (PHGDH), the rate-limitin
66 4 (ATF4) and its downstream effector genes, phosphoglycerate dehydrogenase (PHGDH), which encodes a
71 d genes associated with serine biosynthesis (Phosphoglycerate dehydrogenase, Phgdh; phosphoserine ami
72 of residues in the regulatory domains of D-3-phosphoglycerate dehydrogenase provide the first direct
76 n part to the genomic copy number gain for 3-phosphoglycerate dehydrogenase, the enzyme that controls
78 sphate pathway (PPP), while 2-PG activates 3-phosphoglycerate dehydrogenase to provide feedback contr
79 ns indirectly enhance the ability of SerA (3-phosphoglycerate dehydrogenase) to perform a new functio
81 topped flow analysis of Escherichia coli D-3-phosphoglycerate dehydrogenase was performed by followin
82 and mice with targeted deletion of Srr or 3-Phosphoglycerate dehydrogenase, we demonstrate predomina
84 same fold; (iii) the C-terminal domain of 3-phosphoglycerate dehydrogenase, which binds serine and i
85 e structure of a truncated form of human d-3-phosphoglycerate dehydrogenase with cofactor and a subst