Moonlighting glyceraldehyde-3-phosphate dehydrogenase: posttranslational modification, protein and nucleic acid interactions in normal cells and in human pathology
Author:
Affiliation:
1. Department of Pharmacology, Lewis Katz School of Medicine, Temple University, Philadelphia, PA, USA
Funder
National Institutes of Health
National Science Foundation
W.W. Charitable Trust
Publisher
Informa UK Limited
Subject
Molecular Biology,Biochemistry
Link
https://www.tandfonline.com/doi/pdf/10.1080/10409238.2020.1787325
Reference77 articles.
1. Oxidation of glyceraldehyde-3-phosphate dehydrogenase enhances its binding to nucleic acids
2. Human Glyceraldehyde-3-phosphate Dehydrogenase Plays a Direct Role in Reactivating Oxidized Forms of the DNA Repair Enzyme APE1
3. Posttranscriptional regulation of angiotensin II type 1 receptor expression by glyceraldehyde 3-phosphate dehydrogenase
4. Mutant Huntingtin: Nuclear translocation and cytotoxicity mediated by GAPDH
5. Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein
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