Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation.
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RNA-binding proteins related to stress response and differentiation in protozoaThe sweet side of RNA regulation: glyceraldehyde-3-phosphate dehydrogenase as a noncanonical RNA-binding proteinProtein Recognition in Drug-Induced DNA Alkylation: When the Moonlight Protein GAPDH Meets S23906-1/DNA Minor Groove AdductsThe structure, function and evolution of proteins that bind DNA and RNASubcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocationGAPDH: a common enzyme with uncommon functionsStructural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversityProtein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH)The diverse functions of GAPDH: views from different subcellular compartmentsGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) prevents lipopolysaccharide (LPS)-induced, sepsis-related severe acute lung injury in mice.Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolutionComparative proteomic analysis reveals growth inhibition by 3-N-alkyloxyestradiol derivative (SERM) in prostate cancer cells.Glyceraldehyde 3-phosphate dehydrogenase-telomere association correlates with redox status in Trypanosoma cruziHuman hepatocellular carcinoma in a mouse model: assessment of tumor response to percutaneous ablation by using glyceraldehyde-3-phosphate dehydrogenase antagonistsGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces cancer cell senescence by interacting with telomerase RNA component.Phosphatidic acid binds to cytosolic glyceraldehyde-3-phosphate dehydrogenase and promotes its cleavage in ArabidopsisMoonlighting enzymes in parasitic protozoa.Novel insight into the role of GAPDH playing in tumor.Glyceraldehyde-3-phosphate dehydrogenase: a promising target for molecular therapy in hepatocellular carcinomaNuclear GAPDH: changing the fate of Müller cells in diabetes.Tumor glycolysis as a target for cancer therapy: progress and prospects.Acetylation control of metabolic enzymes in cancer: an updated version.Moonlighting proteins in cancer.Retrospective Proteomic Screening of 100 Breast Cancer Tissues.Occurrence of a multimeric high-molecular-weight glyceraldehyde-3-phosphate dehydrogenase in human serumInteractions between abscisic acid and plastidial glycolysis in Arabidopsis.Calcium- and Nitric Oxide-Dependent Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Response to Long Chain Bases in Tobacco BY-2 Cells.D-Glyceraldehyde-3-Phosphate Dehydrogenase Structure and Function.Identification of driver genes associated with chemotherapy resistance of Ewing's sarcoma
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Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 02 October 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
@en
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
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type
label
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
@en
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
@nl
prefLabel
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
@en
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
@nl
P2093
P2860
P1476
Direct binding of glyceraldehy ...... apy-induced rapid degradation.
@en
P2093
Besim Ogretmen
Christopher Davies
Eleanor K Spicer
Elif Apohan
Neil A Demarse
Suriyan Ponnusamy
P2860
P304
P356
10.1016/J.JMB.2009.09.062
P407
P50
P577
2009-10-02T00:00:00Z