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


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.

SUBMITTER: Silverman GA 

PROVIDER: S-EPMC2915665 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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

Silverman Gary A GA   Whisstock James C JC   Bottomley Stephen P SP   Huntington James A JA   Kaiserman Dion D   Luke Cliff J CJ   Pak Stephen C SC   Reichhart Jean-Marc JM   Bird Phillip I PI  

The Journal of biological chemistry 20100524 32


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 withi  ...[more]

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