Introduction of an intramolecular crosslink at the active site of glyceraldehyde 3-phosphate dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference21 articles.
1. Glyceraldehyde 3-phosphate dehydrogenases
2. Subunit structure of glyceraldehyde-3-phosphate dehydrogenase
3. Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate Dehydrogenase
4. S-N Transfer and Dual Acetylation in the S-Acetylation and N-Acetylation of 3-Phosphoglyceraldehyde Dehydrogenase by Substrates
5. The Enzymatic Significance of S-Acetylation and N-Acetylation of 3-Phosphoglyceraldehyde Dehydrogenase
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1. Dynamic Oligomeric Properties;GAPDH: Biological Properties and Diversity;2012-06-14
2. Reactions of Glyceraldehyde 3-Phosphate Dehydrogenase Sulfhydryl Groups with Bis-Electrophiles Produce DNA–Protein Cross-Links but Not Mutations;Chemical Research in Toxicology;2008-02
3. Photochemical Nucleophile Mapping: Identification of Tyr311 within the Catalytic Domain of Rabbit Muscle Glyceraldehyde-3-phosphate Dehydrogenase;Photochemistry and Photobiology;2006
4. Inactivation and conformation changes of the glycated and non-glycated d-glyceraldehyde-3-phosphate dehydrogenase during guanidine-HCl denaturation;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-11
5. Isolation and some properties of glycated d-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle;Biochemical Journal;1995-07-01
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