Literature DB >> 23045136

Overview of protein glutathionylation.

Aleksandra Filipovska1, Michael P Murphy.   

Abstract

Many proteins contain free thiols that can be modified by the reversible formation of mixed disulfides with glutathione. Protein glutathionylation is of significance for defense against oxidative damage and in redox signaling. Here we outline the mechanisms and possible significance of protein glutathionylation.

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Year:  2006        PMID： 23045136     DOI： 10.1002/0471140856.tx0610s28

Source DB:  PubMed          Journal:  Curr Protoc Toxicol        ISSN： 1934-9254


  3 in total

1.  Adaptive phylogeography: functional divergence between haemoglobins derived from different glacial refugia in the bank vole.

Authors:  Petr Kotlík; Silvia Marková; Libor Vojtek; Antonín Stratil; Vlastimil Slechta; Pavel Hyršl; Jeremy B Searle
Journal:  Proc Biol Sci       Date:  2014-07-07       Impact factor: 5.349

2.  Pleiotropic functions of glutathione S-transferase P.

Authors:  Jie Zhang; Christina Grek; Zhi-Wei Ye; Yefim Manevich; Kenneth D Tew; Danyelle M Townsend
Journal:  Adv Cancer Res       Date:  2014       Impact factor: 6.242

3.  Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells.

Authors:  Yugo Tsuchiya; Sew Yeu Peak-Chew; Clare Newell; Sheritta Miller-Aidoo; Sriyash Mangal; Alexander Zhyvoloup; Jovana Bakovic; Oksana Malanchuk; Gonçalo C Pereira; Vassilios Kotiadis; Gyorgy Szabadkai; Michael R Duchen; Mark Campbell; Sergio Rodriguez Cuenca; Antonio Vidal-Puig; Andrew M James; Michael P Murphy; Valeriy Filonenko; Mark Skehel; Ivan Gout
Journal:  Biochem J       Date:  2017-07-11       Impact factor: 3.857
  3 in total

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