S-nitrosylation and S-glutathionylation of GAPDH: Similarities, differences, and relationships

Author:

Medvedeva M.V.,Kleimenov S. Yu,Samygina V.R.,Muronetz V.I.,Schmalhausen E.V.

Funder

Russian Science Foundation

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference36 articles.

1. On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control;Sirover;Biochim. Biophys. Acta,1810

2. The role of posttranslational modification in moonlighting glyceraldehyde-3-phosphate dehydrogenase structure and function;Sirover;Amino Acids,2021

3. S-nitrosation versus S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione;Giustarini;Antioxid. Redox. Signal.,2005

4. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase;Mohr;J. Biol. Chem.,1999

5. Products of S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase: relation between S-nitrosylation and oxidation;Schmalhausen;Biochim. Biophys. Acta Gen. Subj.,2022

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