SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
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Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondriaSerine and glycine metabolism in cancerModeling cellular compartmentation in one-carbon metabolismTargeting glycogen metabolism in bladder cancerHow pyridoxal 5'-phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric stateALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenasePhylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymesMitochondrial dysfunction remodels one-carbon metabolism in human cellsDisruption of shmt1 impairs hippocampal neurogenesis and mnemonic function in mice.SHMT1 1420 and MTHFR 677 variants are associated with rectal but not colon cancer.Azoxymethane-induced colon carcinogenesis in mice occurs independently of de novo thymidylate synthesis capacity.Essential Function of the Serine Hydroxymethyl Transferase (SHMT) Gene During Rapid Syncytial Cell Cycles in Drosophila.Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiencyPlasmodium serine hydroxymethyltransferase: indispensability and display of distinct localization.Polymorphisms in serine hydroxymethyltransferase 1 and methylenetetrahydrofolate reductase interact to increase cardiovascular disease risk in humans.SHMT1 knockdown induces apoptosis in lung cancer cells by causing uracil misincorporation.Shmt1 and de novo thymidylate biosynthesis underlie folate-responsive neural tube defects in mice.Shmt1 heterozygosity impairs folate-dependent thymidylate synthesis capacity and modifies risk of Apc(min)-mediated intestinal cancer risk.Bioinformatics analysis of the serine and glycine pathway in cancer cellscMyc-mediated activation of serine biosynthesis pathway is critical for cancer progression under nutrient deprivation conditions.Aldehyde dehydrogenase homologous folate enzymes: Evolutionary switch between cytoplasmic and mitochondrial localization.Positive correlation between expression level of mitochondrial serine hydroxymethyltransferase and breast cancer grade.Nuclear localization of de novo thymidylate biosynthesis pathway is required to prevent uracil accumulation in DNAAminomethylphosphonic acid and methoxyacetic acid induce apoptosis in prostate cancer cells.Competition between sumoylation and ubiquitination of serine hydroxymethyltransferase 1 determines its nuclear localization and its accumulation in the nucleus.Serine hydroxymethyltransferase anchors de novo thymidylate synthesis pathway to nuclear lamina for DNA synthesis.Serine hydroxymethyltransferase 1 and 2: gene sequence variation and functional genomic characterizationInhibition of the mevalonate pathway affects epigenetic regulation in cancer cells.Reversal of Cytosolic One-Carbon Flux Compensates for Loss of the Mitochondrial Folate PathwayFolate network genetic variation predicts cardiovascular disease risk in non-Hispanic white malesmiR-370 and miR-373 regulate the pathogenesis of osteoarthritis by modulating one-carbon metabolism via SHMT-2 and MECP-2, respectivelyAminomethylphosphonic acid inhibits growth and metastasis of human prostate cancer in an orthotopic xenograft mouse modelPolymorphisms in 1-carbon metabolism, epigenetics and folate-related pathologies.Glyphosate and AMPA inhibit cancer cell growth through inhibiting intracellular glycine synthesis.Prognostic and therapeutic value of mitochondrial serine hydroxyl-methyltransferase 2 as a breast cancer biomarkerOne-carbon metabolism-genome interactions in folate-associated pathologies.A UV-responsive internal ribosome entry site enhances serine hydroxymethyltransferase 1 expression for DNA damage repair.GABA(A) receptor and glycine receptor activation by paracrine/autocrine release of endogenous agonists: more than a simple communication pathway.Trafficking of intracellular folates.Folate-genetics and colorectal neoplasia: what we know and need to know next.
P2860
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P2860
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
description
2009 nî lūn-bûn
@nan
2009 թուականին հրատարակուած գիտական յօդուած
@hyw
2009 թվականին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@ast
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en-gb
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@nl
type
label
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@ast
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en-gb
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@nl
prefLabel
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@ast
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en-gb
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@nl
P2860
P3181
P1433
P1476
SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
@en
P2093
Donald D Anderson
Patrick J Stover
P2860
P3181
P356
10.1371/JOURNAL.PONE.0005839
P407
P577
2009-01-01T00:00:00Z