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J Biol Chem. 2010 Aug 6;285(32):24299-305. doi: 10.1074/jbc.R110.112771. Epub 2010 May 24.

Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems.

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1
Department of Pediatrics and Cell Biology and Physiology, Children's Hospital of Pittsburgh and Magee-Womens Hospital, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15201, USA. gsilverman@upmc.edu

Erratum in

  • J Biol Chem. 2010 Dec 3;285(49):38740.

Abstract

Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.

PMID:
20498369
PMCID:
PMC2915665
DOI:
10.1074/jbc.R110.112771
[Indexed for MEDLINE]
Free PMC Article
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