Articles with "protein glutathionylation" as a keyword



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Isotopically Labeled Clickable Glutathione to Quantify Protein S‐Glutathionylation

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Published in 2019 at "ChemBioChem"

DOI: 10.1002/cbic.201900528

Abstract: Protein S‐glutathionylation is one of the important cysteine oxidation events that regulate various redox‐mediated biological processes. Despite several existing methods, there are few proteomic approaches to identify and quantify specific cysteine residues susceptible to S‐glutathionylation.… read more here.

Keywords: glutathionylation; labeled clickable; protein glutathionylation; isotopically labeled ... See more keywords
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Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.

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Published in 2019 at "Chemico-biological interactions"

DOI: 10.1016/j.cbi.2018.12.003

Abstract: Protein S-glutathionylation reactions are a ubiquitous oxidative modification required to control protein function in response to changes in redox buffering capacity. These reactions are rapid and reversible and are, for the most part, enzymatically mediated… read more here.

Keywords: buffering capacity; redox buffering; protein glutathionylation; glutathionylation ... See more keywords
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Protein Glutathionylation and Glutaredoxin: Role in Neurodegenerative Diseases

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Published in 2022 at "Antioxidants"

DOI: 10.3390/antiox11122334

Abstract: Oxidative stress has been implicated in the pathogenesis and progression of many neurodegenerative disorders including Parkinson’s disease and Alzheimer’s disease. One of the major enzyme systems involved in the defense against reactive oxygen species are… read more here.

Keywords: glutathione glutaredoxin; glutaredoxin; role; brain ... See more keywords