ArticleInternational journal of molecular sciences2019
Ultra-Rapid Glutathionylation of Ribonuclease: Is this the Real Incipit of its Oxidative Folding?
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- The unusual properties of lactoferrin during its nascent phase.Scientific reports · 2023Article
- The Anfinsen Dogma: Intriguing Details Sixty-Five Years Later.International journal of molecular sciences · 2022Article
- Oxidative Folding of Proteins: The "Smoking Gun" of Glutathione.International journal of molecular sciences · 2021Review
- New Factors Enhancing the Reactivity of Cysteines in Molten Globule-Like Structures.International journal of molecular sciences · 2020Article
- Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many details of oxidative folding of proteins remain obscure, in particular, the role of oxidized glutathione (GSSG). This study reveals some unknown aspects. When a reduced ribonuclease A refolds in the presence of GSSG, most of its eight cysteines accomplish a very fast glutathionylation. In particular, one single cysteine, identified as Cys95 by mass spectrometry, displays 3600 times higher reactivity when compared with an unperturbed protein cysteine. Furthermore, the other five cysteines show 40-50 times higher reactivity toward GSSG. This phenomenon is partially due to a low p
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Registered trials
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