期刊
FREE RADICAL RESEARCH
卷 50, 期 2, 页码 172-194出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/10715762.2015.1090571
关键词
Chemistry; reactive oxygen species; redox status; sulfenic acid; thiols
资金
- National Institutes of Health [R01 CA136810, R33 CA177461]
- Wake Forest Postdoctoral Program in Translational Radiation Oncology [T32 CA113267]
- PRIME-IRACDA postdoctoral fellowship [K12 GM102773]
Selective modification of proteins at cysteine residues by reactive oxygen, nitrogen or sulfur species formed under physiological and pathological states is emerging as a critical regulator of protein activity impacting cellular function. This review focuses primarily on protein sulfenylation (-SOH), a metastable reversible modification connecting reduced cysteine thiols to many products of cysteine oxidation. An overview is first provided on the chemistry principles underlining synthesis, stability and reactivity of sulfenic acids in model compounds and proteins, followed by a brief description of analytical methods currently employed to characterize these oxidative species. The following chapters present a selection of redox-regulated proteins for which the -SOH formation was experimentally confirmed and linked to protein function. These chapters are organized based on the participation of these proteins in the regulation of signaling, metabolism and epigenetics. The last chapter discusses the therapeutic implications of altered redox microenvironment and protein oxidation in disease.
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