ArticleScientific reports2020
Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins.
Article in Scientific reports, 2020. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- The unusual properties of lactoferrin during its nascent phase.Scientific reports · 2023Article
- Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins.International journal of molecular sciences · 2023Review
- 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
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chymotrypsinogen, when reduced and taken to its molten globule-like conformation, displays a single cysteine with an unusual kinetic propensity toward oxidized glutathione (GSSG) and other organic thiol reagents. A single residue, identified by mass spectrometry like Cys1, reacts with GSSG about 1400 times faster than an unperturbed protein cysteine. A reversible protein-GSSG complex and a low pK
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Registered trials
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