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PGDH1 is essential for Arabidopsis development.
Genetic and molecular evidence were provided for the essential role of EDA9 for embryo and pollen development.
Data indicate that 3-phosphoglycerate dehydrogenases PGDH (At1g17745) and EDA9 (At4g34200) were expressed preferentially in roots while 3-PGDH (At3g19480) was expressed mainly in the aerial parts and was not expressed or very poorly in roots.
PHGDH expression is regulated by PlncRNA-1 in breast cancer.
Study provides evidence that a unique metabolic program is activated in a lung adenocarcinoma subset, described by PHGDH, which confers cell growth.
Data indicate that the expression of PHGDH is increased in pancreatic cancer and is an independent molecular prognostic factor for pancreatic cancer patients. In addition, PHGDH controls cell proliferation, migration and invasion abilities.
Data show there was a significant negative correlation between PHGDH copy-number alteration and EPAS1 (HIF2A) expression.
Therefore, we show for the first time that the nuclear localization of Cat L and its substrate Cux1can be positively regulated by Snail NLS and importin beta1, suggesting that Snail, Cat L and Cux1 all utilize importin beta1 for nuclear import.
High PHGDH expression is associated with idiopathic pulmonary fibrosis.
This report present 6 individuals from 3 unrelated families with infantile serine biosynthesis defect due to PGDH deficiency.
Overexpression of Phgdh may be generally associated with CK5 cells, and oncogenic function may be determined by isoform expression.
High expression of PHGDH is associated with Colon Cancer.
p53-mediated repression of PHGDH enhances the apoptotic response upon serine starvation in melanoma cells.
Phosphoglycerate Dehydrogenase deficiency is associated with Neu-Laxova syndrome.
We report on the identification of homozygous mutations in PHGDH and serine deficiency in individuals with Neu-Laxova syndrome. This disorder thus seems to be an extremely severe expression of PHGDH deficiency.
PHGDH overexpression is found in cervical cancer, in particular, in bigger tumors and with advanced stages. Its expression is positively correlated with squamous cell carcinoma antigen level
The potential mechanisms by which PHGDH promotes cancer are discussed.
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
in some cancer cells a relatively large amount of glycolytic carbon is diverted into serine and glycine metabolism through phosphoglycerate dehydrogenase.
results reveal that certain breast cancers are dependent upon increased serine pathway flux caused by PHGDH overexpression and demonstrate the utility of in vivo negative-selection RNAi screens for finding potential anticancer targets
Studies in bacteria showed that addition of substrate at the active site is ordered, with HPAP binding before NADH. Also, NADH can compete with the substrate for binding to the allosteric site and thereby eliminate the substrate inhibition.
The crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase has been solved with bound effector, 1-serine, and substrate, hydroxypyruvic acid phosphate. The human enzyme was also examined.
The frequency of antibodies to Phgdh is much higher in patients with autoimmune hepatitis than in patients with other types of hepatitis or normal controls.
This gene encodes the enzyme which is involved in the early steps of L-serine synthesis in animal cells. L-serine is required for D-serine and other amino acid synthesis. The enzyme requires NAD/NADH as a cofactor and forms homotetramers for activity. Mutations in this gene have been found in a family with congenital microcephaly, psychomotor retardation and other symptoms. Multiple alternatively spliced transcript variants have been found, however the full-length nature of most are not known.
, 3-phosphoglycerate dehyrogenase
, 3-phosphoglycerate dehydrogenase