期刊
JOURNAL OF PROTEOMICS
卷 74, 期 11, 页码 2228-2242出版社
ELSEVIER
DOI: 10.1016/j.jprot.2011.05.004
关键词
Carbonylation; Frataxin; Metal binding; Metal-catalyzed oxidation; Mitochondria; Reactive oxygen species
资金
- Faculty of Agricultural Sciences, Aarhus University
- European 6th Framework Program Grant Proteomage [LSHMCT-518230]
Proteins can become oxidatively modified in many different ways, either by direct oxidation of amino acid side chains and protein backbone or indirectly by conjugation with oxidation products of polyunsaturated fatty acids and carbohydrates. While reversible oxidative modifications are thought to be relevant in physiological processes, irreversible oxidative modifications are known to contribute to cellular damage and disease. The most well-studied irreversible protein oxidation is carbonylation. In this work we first examine how protein carbonylation occurs via metal-catalyzed oxidation (MCO) in vivo and in vitro with an emphasis on cellular metal ion homeostasis and metal binding. We then review proteomic methods currently used for identifying carbonylated proteins and their sites of modification. Finally, we discuss the identified carbonylated proteins and the pattern of carbonylation sites in relation to cellular metabolism using the mitochondrion as a case story. (C) 2011 Elsevier B.V. All rights reserved.
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