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PGDH1 (show HPGD Proteins) 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 (show HPGD Proteins) (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.
These results indicate that the PHGDH gene expression, dictated by IL-2R signaling, is a crucial event for DNA synthesis during S phase of activated T cells.
Using transgenic mice expressing enhanced GFP under the Srr (show SRR Proteins) promoter and mice with targeted deletion of Srr (show SRR Proteins) or 3-Phosphoglycerate dehydrogenase, we demonstrate predominantly neuronal sources of d-serine dependent on astrocytic supply of l-serine.
Elevated levels of 4E-BP1 (show EIF4EBP1 Proteins) may be involved in a mechanism to arrest brain development in Phgdh knock out embryos.
Phgdh deletion reveals a pivotal role for L-serine biosynthesis in controlling the level of brain D-serine, an N-methyl-D-aspartate receptor (show GRIN1 Proteins) co-agonist
Data suggest expression of Phgdh in endometrium is regulated by Hoxa10.
the Phgdh-dependent phosphorylated pathway is essential for normal embryonic development, especially for brain morphogenesis
the presence of cis (show CISH Proteins)-acting elements confer the cell type specificity of Phgdh transcription in the distal promoter region.
The mouse Phgdh gene spans approximately 27 kilobases in length and comprises 12 exons with 11 intervening introns and is mapped to chromosome 3, region F2-F3 by FISH.
either Phgdh or ASCT1 (show SLC1A4 Proteins) is provided to each segment of renal tubules, suggesting that metabolic interplay mediated by L-serine biosynthesis and supply may exist in the kidney
Inactivation of Phgdh gene with changes in gene expression and associated regulatory networks resulting from serine deficiency are reported.
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 (show EPAS1 Proteins)) 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 (show HPGD Proteins) deficiency.
Overexpression of Phgdh may be generally associated with CK5 (show KRT5 Proteins) cells, and oncogenic function may be determined by isoform expression.
High expression of PHGDH is associated with Colon Cancer.
p53 (show TP53 Proteins)-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 (show ERBB2 Proteins)-Laxova syndrome. This disorder thus seems to be an extremely severe expression of PHGDH deficiency.
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