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rdf:type |
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lifeskim:mentions |
umls-concept:C0013935,
umls-concept:C0015127,
umls-concept:C0017337,
umls-concept:C0025914,
umls-concept:C0026809,
umls-concept:C0070861,
umls-concept:C0205082,
umls-concept:C0243067,
umls-concept:C0332453,
umls-concept:C0599894,
umls-concept:C1274040,
umls-concept:C1314792,
umls-concept:C1521840
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pubmed:issue |
5
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pubmed:dateCreated |
2004-1-26
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pubmed:abstractText |
D-3-Phosphoglycerate dehydrogenase (Phgdh; EC 1.1.1.95) is the first committed enzyme of L-serine biosynthesis in the phosphorylated pathway. To determine the physiological importance of Phgdh-dependent L-serine biosynthesis in vivo, we generated Phgdh-deficient mice using targeted gene disruption in embryonic stem cells. The absence of Phgdh led to a drastic reduction of L-serine metabolites such as phosphatidyl-L-serine and sphingolipids. Phgdh null embryos have small bodies with abnormalities in selected tissues and died after days post-coitum 13.5. Striking abnormalities were evident in the central nervous system in which the Phgdh null mutation culminated in hypoplasia of the telencephalon, diencephalon, and mesencephalon; in particular, the olfactory bulbs, ganglionic eminence, and cerebellum appeared as indistinct structures. These observations demonstrate that the Phgdh-dependent phosphorylated pathway is essential for normal embryonic development, especially for brain morphogenesis.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:AzumaNorihiroN,
pubmed-author:FuruyaShigekiS,
pubmed-author:HashikawaTsutomuT,
pubmed-author:HirabayashiYoshioY,
pubmed-author:ItoharaShigeyoshiS,
pubmed-author:MitomaJunyaJ,
pubmed-author:OsukaSohS,
pubmed-author:ShinodaYokoY,
pubmed-author:TanakaHideyukiH,
pubmed-author:WatanabeMasahikoM,
pubmed-author:YoshidaKazuyukiK
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pubmed:issnType |
Print
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pubmed:day |
30
|
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pubmed:volume |
279
|
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3573-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14645240-Alleles,
pubmed-meshheading:14645240-Animals,
pubmed-meshheading:14645240-Blotting, Southern,
pubmed-meshheading:14645240-Blotting, Western,
pubmed-meshheading:14645240-Brain,
pubmed-meshheading:14645240-Carbohydrate Dehydrogenases,
pubmed-meshheading:14645240-Cytosol,
pubmed-meshheading:14645240-Exons,
pubmed-meshheading:14645240-Heterozygote,
pubmed-meshheading:14645240-Immunohistochemistry,
pubmed-meshheading:14645240-Introns,
pubmed-meshheading:14645240-Liver,
pubmed-meshheading:14645240-Mice,
pubmed-meshheading:14645240-Mice, Inbred C57BL,
pubmed-meshheading:14645240-Mice, Transgenic,
pubmed-meshheading:14645240-Microscopy, Fluorescence,
pubmed-meshheading:14645240-Mutation,
pubmed-meshheading:14645240-Nervous System,
pubmed-meshheading:14645240-Phenotype,
pubmed-meshheading:14645240-Phosphoglycerate Dehydrogenase,
pubmed-meshheading:14645240-Phosphorylation,
pubmed-meshheading:14645240-Polymerase Chain Reaction,
pubmed-meshheading:14645240-Serine,
pubmed-meshheading:14645240-Stem Cells,
pubmed-meshheading:14645240-Time Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Targeted disruption of the mouse 3-phosphoglycerate dehydrogenase gene causes severe neurodevelopmental defects and results in embryonic lethality.
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pubmed:affiliation |
Neuronal Circuit Mechanisms Research Group, RIKEN Brain Science Institute, Saitama 351-0198, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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