An overview of the serpin superfamily

Ruby H.P. Law; Qingwei Zhang; Sheena McGowan; Ashley M. Buckle; Gary A. Silverman; Wilson Wong; Carlos J. Rosado; Chris G. Langendorf; Rob N. Pike; Philip I. Bird; James C. Whisstock

doi:10.1186/gb-2006-7-5-216

An overview of the serpin superfamily

Ruby H.P. Law, Qingwei Zhang, Sheena McGowan, Ashley M. Buckle, Gary A. Silverman, Wilson Wong, Carlos J. Rosado, Chris G. Langendorf, Rob N. Pike, Philip I. Bird, James C. Whisstock

Research output: Contribution to journal › Review article › peer-review

573 Scopus citations

Abstract

Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways. Serpins are conformationally labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers.

Original language	English
Article number	216
Journal	Genome biology
Volume	7
Issue number	5
DOIs	https://doi.org/10.1186/gb-2006-7-5-216
State	Published - May 30 2006

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abstract = "Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways. Serpins are conformationally labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers.",

author = "Law, {Ruby H.P.} and Qingwei Zhang and Sheena McGowan and Buckle, {Ashley M.} and Silverman, {Gary A.} and Wilson Wong and Rosado, {Carlos J.} and Langendorf, {Chris G.} and Pike, {Rob N.} and Bird, {Philip I.} and Whisstock, {James C.}",

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AU - Wong, Wilson

AU - Rosado, Carlos J.

AU - Langendorf, Chris G.

AU - Pike, Rob N.

AU - Bird, Philip I.

AU - Whisstock, James C.

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AB - Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways. Serpins are conformationally labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers.

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An overview of the serpin superfamily

Abstract

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