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High-Throughput Identification of Catalytic Redox-Active Cysteine Residues

Fomenko, Dmitri E., Xing, Weibing, Adair, Blakely M., Thomas, David J., Gladyshev, Vadim N.·2007·Science

Abstract

Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases. This method is independent of protein family, structure, and taxon. We used it to selectively detect the majority of known proteins with redox-active Cys and to make additional predictions, one of which was verified. Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins.

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Metadata

Authors
Fomenko, D. E., Xing, W., Adair, B. M., Thomas, D. J., & Gladyshev, V. N.
Venue
Science
Published
2007-01-19
Volume
315
Issue
5810
Pages
387-389
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2001499411
Cited by
187
References
0
FWCI
7.18
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: High-Throughput Identification of Catalytic Redox-Active Cysteine Residues. https://app.cochat.ai/papers/10.1126/science.1133114
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Fomenko, D. E., Xing, W., Adair, B. M., Thomas, D. J., & Gladyshev, V. N. (2007). High-Throughput Identification of Catalytic Redox-Active Cysteine Residues. Science. https://doi.org/10.1126/science.1133114

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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.