ArticleProtein science : a publication of the Protein Society2009
Conformational changes in redox pairs of protein structures.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Integrated analysis of the redoxome and zinc proteome links ribosomal protein oxidation to zinc homeostasis.Redox biology · 2026Article
- A disulfide redox switch mechanism regulates glycoside hydrolase function.Nature communications · 2026Article
- Remarkably Selective Binding, Behavior Modification, and Switchable Release of (Bipyridine)JACS Au · 2023Article
- Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.Antioxidants (Basel, Switzerland) · 2021Review
- Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome.Antioxidants & redox signaling · 2020Review
- Global redox proteome and phosphoproteome analysis reveals redox switch in Akt.Nature communications · 2019Article
- Turnip Mosaic Virus Is a Second Example of a Virus Using Transmission Activation for Plant-to-Plant Propagation by Aphids.Journal of virology · 2019Article
- Cross-strand disulfides in the hydrogen bonding site of antiparallel β-sheet (aCSDhs): Forbidden disulfides that are highly strained, easily broken.Protein science : a publication of the Protein Society · 2019Article
- Prediction of reversible disulfide based on features from local structural signatures.BMC genomics · 2017Article
- From structure to redox: The diverse functional roles of disulfides and implications in disease.Proteomics · 2017Review
- Prediction of redox-sensitive cysteines using sequential distance and other sequence-based features.BMC bioinformatics · 2016Article
- Mapping native disulfide bonds at a proteome scale.Nature methods · 2015Article
- Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins.Frontiers in pharmacology · 2015Article
- Characterization of the redox transition of the XRCC1 N-terminal domain.Structure (London, England : 1993) · 2014Article
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology.Frontiers in pharmacology · 2014Article
- Application of iTRAQ Reagents to Relatively Quantify the Reversible Redox State of Cysteine Residues.International journal of proteomics · 2012Article
- Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox-active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox-active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox-active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox-activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.
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