An overview of the serpin superfamily

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-l...

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Autores principales: Law, Ruby HP, Zhang, Qingwei, McGowan, Sheena, Buckle, Ashley M, Silverman, Gary A, Wong, Wilson, Rosado, Carlos J, Langendorf, Chris G, Pike, Rob N, Bird, Philip I, Whisstock, James C
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1779521/
https://www.ncbi.nlm.nih.gov/pubmed/16737556
http://dx.doi.org/10.1186/gb-2006-7-5-216
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author Law, Ruby HP
Zhang, Qingwei
McGowan, Sheena
Buckle, Ashley M
Silverman, Gary A
Wong, Wilson
Rosado, Carlos J
Langendorf, Chris G
Pike, Rob N
Bird, Philip I
Whisstock, James C
author_facet Law, Ruby HP
Zhang, Qingwei
McGowan, Sheena
Buckle, Ashley M
Silverman, Gary A
Wong, Wilson
Rosado, Carlos J
Langendorf, Chris G
Pike, Rob N
Bird, Philip I
Whisstock, James C
author_sort Law, Ruby HP
collection PubMed
description 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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spelling pubmed-17795212007-01-19 An overview of the serpin superfamily Law, Ruby HP Zhang, Qingwei McGowan, Sheena Buckle, Ashley M Silverman, Gary A Wong, Wilson Rosado, Carlos J Langendorf, Chris G Pike, Rob N Bird, Philip I Whisstock, James C Genome Biol Review 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. BioMed Central 2006 2006-05-30 /pmc/articles/PMC1779521/ /pubmed/16737556 http://dx.doi.org/10.1186/gb-2006-7-5-216 Text en Copyright © 2006 BioMed Central Ltd
spellingShingle Review
Law, Ruby HP
Zhang, Qingwei
McGowan, Sheena
Buckle, Ashley M
Silverman, Gary A
Wong, Wilson
Rosado, Carlos J
Langendorf, Chris G
Pike, Rob N
Bird, Philip I
Whisstock, James C
An overview of the serpin superfamily
title An overview of the serpin superfamily
title_full An overview of the serpin superfamily
title_fullStr An overview of the serpin superfamily
title_full_unstemmed An overview of the serpin superfamily
title_short An overview of the serpin superfamily
title_sort overview of the serpin superfamily
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1779521/
https://www.ncbi.nlm.nih.gov/pubmed/16737556
http://dx.doi.org/10.1186/gb-2006-7-5-216
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