ArticleRoyal Society open science2018
Identification of allosteric disulfides from labile bonds in X-ray structures.
Article in Royal Society open science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Determining the Redox Potential of a Protein Disulfide Bond.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Allosteric Disulfide Bridges in Integrins: The Molecular Switches of Redox Regulation of Integrin-Mediated Cell Functions.Antioxidants (Basel, Switzerland) · 2025Review
- Secretory Phospholipases A2, from Snakebite Envenoming to a Myriad of Inflammation Associated Human Diseases-What Is the Secret of Their Activity?International journal of molecular sciences · 2023Review
- A proximity-based in silico approach to identify redox-labile disulfide bonds: The example of FVIII.PloS one · 2022Article
- Structure of Usutu virus SAAR-1776 displays fusion loop asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Scientific review of the aesthetic uses of botulinum toxin type A.Archives of craniofacial surgery · 2021Article
- Article
- A redox-active switch in fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily.Science signaling · 2020Article
- Antioxidative Potency of Dolphin Serum Albumin Is Stronger Than That of Human Serum Albumin Irrespective of Substitution ofFrontiers in physiology · 2020Article
- Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature.Biophysical reviews · 2019Review
- Cys.sqlite: A Structured-Information Approach to the Comprehensive Analysis of Cysteine Disulfide Bonds in the Protein Databank.Journal of chemical information and modeling · 2019Article
- Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.The Journal of biological chemistry · 2019Review
- Identification of allosteric disulfides from labile bonds in X-ray structures.Royal Society open science · 2018Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed. Here, we identify potential allosteric disulfides in all Protein Data Bank X-ray structures from bonds that are present in some molecules of a protein crystal but absent in others, or present in some structures of a protein but absent in others. We reasoned that the labile nature of these disulfides signifies a propensity for cleavage and so possible allosteric regulation of the protein in which the bond resides. A total of 511 labile disulfide bonds were identified. The labile disulfides are more stressed than the average bond, being characterized by high average torsional strain and stretching of the sulfur-sulfur bond and neighbouring bond angles. This pre-stress likely underpins their susceptibility to cleavage. The coagulation, complement and oxygen-sensing hypoxia inducible factor-1 pathways, which are known or have been suggested to be regulated by allosteric disulfides, are enriched in proteins containing labile disulfides. The identification of labile disulfide bonds will facilitate the study of this post-translational modification.
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