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ISBN 10: 0123864712
ISBN 13: 978-0123864710
Author: James Whisstock, Phillip Bird
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.
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 Knock-Out 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
Modelling 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
Human SCCA Serpins Inhibit Staphylococcal Cysteine Proteases by Forming Classic "Serpin-Like" Covalent Complexes
Plants and the Study of Serpin Biology
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Tags: James Whisstock, Phillip Bird, Biology, Enzymology
