The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Oxidant Sensing by Reversible Disulfide Bond Formation
Open accessAbstract
Maintenance of the cellular redox balance is crucial for cell survival. An increase in reactive oxygen, nitrogen, or chlorine species can lead to oxidative stress conditions, potentially damaging DNA, lipids, and proteins. Proteins are very sensitive to oxidative modifications, particularly methionine and cysteine residues. The reversibility of some of these oxidative protein modifications makes them ideally suited to take on regulatory roles in protein function. This is especially true for disulfide bond formation, which has the potential to mediate extensive yet fully reversible structural and functional changes, rapidly adjusting the protein's activity to the prevailing oxidant levels.
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Citations
Cites
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“It is therefore not surprising that zinc centers, originally thought of as redox-inert and purely structural features in proteins, are now increasingly recognized as common redox units in redoxregulated proteins (see examples in supplemental Table S1) (3, 45).”
BackgroundInfluential
Cited by
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520
Redox metabolism: ROS as specific molecular regulators of cell signaling and function
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Role of Metabolic H2O2 Generation
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Metadata
- Authors
- Cremers, C. M., & Jakob, U.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 288
- Issue
- 37
- Pages
- 26489-26496
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2009808081
- Cited by
- 431
- References
- 95
- FWCI
- 11.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
