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An overview of the serpin superfamily.
Law RH,
Zhang Q,
McGowan S,
Buckle AM,
Silverman GA,
Wong W,
Rosado CJ,
Langendorf CG,
Pike RN,
Bird PI,
Whisstock JC.
Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne VIC 3800, Australia.
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.
PMID: 16737556 [PubMed - indexed for MEDLINE]
PMCID: PMC1779521
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Cited by 7 PubMed Central articles
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Alpha1-antitrypsin and the maintenance of hemostatic balance.
Emmerich J.
Haematologica. 2009 Jun; 94(6):762-3.
[Haematologica. 2009]
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ReviewProtein misfolding and the serpinopathies.
Belorgey D, Hägglöf P, Karlsson-Li S, Lomas DA.
Prion. 2007 Jan; 1(1):15-20. Epub 2007 Jan 6.
[Prion. 2007]
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Single nucleotide polymorphisms associated with coronary heart disease predict incident ischemic stroke in the atherosclerosis risk in communities study.
Morrison AC, Bare LA, Luke MM, Pankow JS, Mosley TH, Devlin JJ, Willerson JT, Boerwinkle E.
Cerebrovasc Dis. 2008; 26(4):420-4. Epub 2008 Sep 18.
[Cerebrovasc Dis. 2008]
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