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Cited by 303

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

The Redox Biochemistry of Protein Sulfenylation and Sulfinylation

Open access
Lo Conte, Mauro, Carroll, Kate S.·2013·Journal of Biological Chemistry

Abstract

Controlled generation of reactive oxygen species orchestrates numerous physiological signaling events (Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15). A major cellular target of reactive oxygen species is the thiol side chain (RSH) of Cys, which may assume a wide range of oxidation states (i.e. -2 to +4). Within this context, Cys sulfenic (Cys-SOH) and sulfinic (Cys-SO2H) acids have emerged as important mechanisms for regulation of protein function. Although this area has been under investigation for over a decade, the scope and biological role of sulfenic/sulfinic acid modifications have been recently expanded with the introduction of new tools for monitoring cysteine oxidation in vitro and directly in cells. This minireview discusses selected recent examples of protein sulfenylation and sulfinylation from the literature, highlighting the role of these post-translational modifications in cell signaling.

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Metadata

Authors
Lo Conte, M., & Carroll, K. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2013-09
Volume
288
Issue
37
Pages
26480-26488
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1983016535
Cited by
303
References
7
FWCI
10.22
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The Redox Biochemistry of Protein Sulfenylation and Sulfinylation. https://app.cochat.ai/papers/10.1074/jbc.r113.467738
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Lo Conte, M., & Carroll, K. S. (2013). The Redox Biochemistry of Protein Sulfenylation and Sulfinylation. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r113.467738

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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