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Serpins Flex Their Muscle.

Authors :
Silverman, Gary A.
Whisstock, James C.
Bottomley, Stephen P.
Huntington, James A.
Kaiserman, Dion
Luke, Cliff J.
Pak, Stephen C.
Reichhart, Jean-Marc
Bird, Phillip I.
Source :
Journal of Biological Chemistry. 8/6/2010, Vol. 285 Issue 32, p24299-24305. 7p. 2 Diagrams, 2 Charts.
Publication Year :
2010

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219258
Volume :
285
Issue :
32
Database :
Academic Search Index
Journal :
Journal of Biological Chemistry
Publication Type :
Academic Journal
Accession number :
53446812
Full Text :
https://doi.org/10.1074/jbc.R110.112771