Biology of serpins [electronic resource] / edited by James C. Whisstock and Phillip I. Bird.
Material type: TextSeries: Methods in enzymology ; v. 499.Publication details: San Diego, CA : Academic Press, 2011. Edition: 1st edDescription: 1 online resource (l, 405 p.) : illISBN: 9780123864710 (electronic bk.); 0123864712 (electronic bk.)Subject(s): Serpins | Proteins | Protein folding | Proteins -- Biotechnology | Protein folding | Proteins | Proteins -- Biotechnology | Serpins | SerpinsGenre/Form: Electronic books.DDC classification: 612.01575 LOC classification: QP601 | .M49 v.499NLM classification: QU 136Online resources: ScienceDirect | ScienceDirectIncludes bibliographical references and indexes.
Analysis of Serpin Secretion, Misfolding, and Surveillance in the Endoplasmic Reticulum -- Serpin-Enzyme Receptors: LDL Receptor-Related Protein 1 -- The Role of Autophagy in Alpha-1-Antitrypsin Deficiency -- Serpins and the Complement System -- Use of Mouse Models to Study Plasminogen Activator Inhibitor-1 -- Plasminogen Activator Inhibitor Type 2: Still an Enigmatic Serpin but a Model for Gene Regulation -- The SerpinB1 Knockout Mouse: A Model for Studying Neutrophil Protease Regulation in Homeostasis and Inflammation -- Investigating Maspin in Breast Cancer Progression Using Mouse Models -- Hsp47 as a collagen-specific molecular chaperone -- Assays for the Antiangiogenic and Neurotrophic Serpin Pigment Epithelium-Derived Factor -- The Drosophila Serpins: Multiple Functions in Immunity and Morphogenesis -- Modeling Serpin Conformational Diseases in Drosophila melanogaster -- Using Caenorhabditis elegans to Study Serpinopathies -- Using C. elegans to Identify the Protease Targets of Serpins In Vivo -- Viral Serpin Therapeutics: From Concept to Clinic -- man SCCA Serpins Inhibit Staphylococcal Cysteine Proteases by Forming Classic "Serpin-Like' Covalent Complexes -- Plants and the Study of Serpin Biology
Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases. This volume of Methods in Ezymology is split into 2 parts and comprehensively covers the subject.
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