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Protein Promiscuity in H2O2Signaling
Author(s) -
David Young,
Brandán Pedre,
Daria Ezeriņa,
Barbara De Smet,
Aleksandra Lewandowska,
MariaArmineh Tossounian,
Nandita Bodra,
Jingjing Huang,
Leonardo Astolfi Rosado,
Frank Van Breusegem,
Joris Messens
Publication year - 2018
Publication title -
antioxidants and redox signaling
Language(s) - Uncategorized
Resource type - Journals
eISSN - 1557-7716
pISSN - 1523-0864
DOI - 10.1089/ars.2017.7013
Subject(s) - peroxiredoxin , microbiology and biotechnology , thioredoxin , redox , oxidative stress , signal transduction , transcription factor , oxidative phosphorylation , biology , biochemistry , cell signaling , chemistry , protein kinase a , peroxidase , kinase , enzyme , gene , organic chemistry
Decrypting the cellular response to oxidative stress relies on a comprehensive understanding of the redox signaling pathways stimulated under oxidizing conditions. Redox signaling events can be divided into upstream sensing of oxidants, midstream redox signaling of protein function, and downstream transcriptional redox regulation. Recent Advances: A more and more accepted theory of hydrogen peroxide (H 2 O 2 ) signaling is that of a thiol peroxidase redox relay, whereby protein thiols with low reactivity toward H 2 O 2 are instead oxidized through an oxidative relay with thiol peroxidases.

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