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Cited by 558

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Woo, Hyun Ae, Chae, Ho Zoon, Hwang, Sung Chul, Yang, Kap-Seok, Kang, Sang Won, Kim, Kanghwa, Rhee, Sue Goo·2003·Science

Abstract

The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. However, by metabolic labeling of mammalian cells with 35 S, we show that the sulfinic form of peroxiredoxin I, produced during the exposure of cells to H 2 O 2 , is rapidly reduced to the catalytically active thiol form. The mammalian cells' ability to reduce protein sulfinic acid might serve as a mechanism to repair oxidatively damaged proteins or represent a new type of cyclic modification by which the function of various proteins is regulated.

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Crossref · 10.1126/science.1080273

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Metadata

Authors
Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K.-S., Kang, S. W., Kim, K., & Rhee, S. G.
Venue
Science
Published
2003-04-25
Volume
300
Issue
5619
Pages
653-656
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2017642315
Cited by
558
References
2
FWCI
14.58
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation. https://app.cochat.ai/papers/10.1126/science.1080273
The paper
Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K.-S., Kang, S. W., Kim, K., & Rhee, S. G. (2003). Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation. Science. https://doi.org/10.1126/science.1080273

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.