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- W3156453517 endingPage "101975" @default.
- W3156453517 startingPage "101975" @default.
- W3156453517 abstract "Glutaredoxin, Grx, is a small protein containing an active site cysteine pair and was discovered in 1976 by Arne Holmgren. The Grx system, comprised of Grx, glutathione, glutathione reductase, and NADPH, was first described as an electron donor for Ribonucleotide Reductase but, from the first discovery in E.coli, the Grx family has impressively grown, particularly in the last two decades. Several isoforms have been described in different organisms (from bacteria to humans) and with different functions. The unique characteristic of Grxs is their ability to catalyse glutathione-dependent redox regulation via glutathionylation, the conjugation of glutathione to a substrate, and its reverse reaction, deglutathionylation. Grxs have also recently been enrolled in iron sulphur cluster formation. These functions have been implied in various physiological and pathological conditions, from immune defense to neurodegeneration and cancer development thus making Grx a possible drug target. This review aims to give an overview on Grxs, starting by a phylogenetic analysis of vertebrate Grxs, followed by an analysis of the mechanisms of action, the specific characteristics of the different human isoforms and a discussion on aspects related to human physiology and diseases." @default.
- W3156453517 created "2021-04-26" @default.
- W3156453517 creator A5002187739 @default.
- W3156453517 creator A5003606073 @default.
- W3156453517 creator A5011472004 @default.
- W3156453517 creator A5013726918 @default.
- W3156453517 date "2021-07-01" @default.
- W3156453517 modified "2023-10-17" @default.
- W3156453517 title "Glutaredoxin: Discovery, redox defense and much more" @default.
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