期刊
TRENDS IN PHARMACOLOGICAL SCIENCES
卷 36, 期 1, 页码 32-40出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tips.2014.10.014
关键词
tissue transglutaminase; TG2; cross-link; enzyme inhibition; reversible inhibitor; irreversible inhibitor
Tissue transglutaminase (TG2) catalyzes the cross-linking of proteins by the formation of isopeptide bonds between glutamine (Gin) and lysine (Lys) side chains. Although TG2 is essential for the stabilization of the extracellular matrix, its unregulated activity has been implicated in celiac disease, fibrosis, and cancer metastasis, among other disorders. Given the importance and range of TG2-related pathologies, recent work has focused on the development of potent and selective inhibitors against TG2. In this review, we present the latest and most noteworthy irreversible and reversible inhibitors of TG2, and offer perspectives for the design of future inhibitors, in the hope that lead compounds with therapeutic potential may soon be discovered.
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