caa a22 4500 463185714 CHVBK 20180406164852.0 cr unu---uuuuu 170326e20070501xx s 000 0 eng 10.1007/s00726-006-0427-6 doi (NATIONALLICENCE)springer-10.1007/s00726-006-0427-6 Mannick J. B. Department of Medicine, University of Massachusetts Medical School, Worcester, MA, U.S.A. aut Regulation of apoptosis by protein S-nitrosylation [Elektronische Daten] [J. B. Mannick] Summary.: S-nitrosylation/denitrosylation of critical cysteine residues on proteins serves as a redox switch that regulates the function of a wide array of proteins. A key signaling pathway that is regulated by S-nitrosylation is apoptotic cell death. Here we will review the proteins in apoptotic pathways that are known to be S-nitrosylated by endogenous NO production. The targets and functional consequences of S-nitrosylation during apoptosis are multifaceted, allowing cells to fine tune their response to apoptotic signals. Springer-Verlag, 2006 Keywords: S-nitrosylation - Apoptosis - Nitric oxide - Caspases - GAPDH - NMDA - Thioredoxin, Ask1, FLIP nationallicence Amino Acids Springer-Verlag 32/4(2007-05-01), 523-526 0939-4451 32:4<523 2007 32 726 https://doi.org/10.1007/s00726-006-0427-6 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0427-6 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Mannick J. B. Department of Medicine, University of Massachusetts Medical School, Worcester, MA, U.S.A aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 32/4(2007-05-01), 523-526 0939-4451 32:4<523 2007 32 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer