The glutaredoxin mono- And di-thiol mechanisms for deglutathionylation are functionally equivalent: Implications for redox systems biology

Bioscience Reports

Volumn 35, Issue , 2015, Pages

  Mashamaite, Lefentse N ^a   Rohwer, Johann M ^b   Pillay, Ché S ^a  

^a UNIVERSITY OF KWAZULU NATAL   (South Africa)

^b STELLENBOSCH UNIVERSITY   (South Africa)

Author keywords

Kinetics; Redox regulation; Redoxin; Thiol

Indexed keywords

CYSTEINE; DITHIOL DERIVATIVE; GLUTAREDOXIN; MONOTHIOL; THIOL; UNCLASSIFIED DRUG; SACCHAROMYCES CEREVISIAE PROTEIN; THIOL DERIVATIVE;

ARTICLE; CHEMICAL MODIFICATION; DEGLUTATHIONYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME REGULATION; ENZYME STRUCTURE; MATHEMATICAL MODEL; OXIDATION REDUCTION REACTION; SYSTEMS BIOLOGY; BIOLOGICAL MODEL; HUMAN; KINETICS; METABOLISM; SACCHAROMYCES CEREVISIAE;

GLUTAREDOXINS; HUMANS; KINETICS; MODELS, BIOLOGICAL; OXIDATION-REDUCTION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SULFHYDRYL COMPOUNDS; SYSTEMS BIOLOGY;

EID: 84923647159     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20140157     Document Type: Article

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