The Resource Biology of serpins, edited by James C. Whisstock and Phillip I. Bird, (electronic resource)

Biology of serpins, edited by James C. Whisstock and Phillip I. Bird, (electronic resource)

Label
Biology of serpins
Title
Biology of serpins
Statement of responsibility
edited by James C. Whisstock and Phillip I. Bird
Contributor
Subject
Language
eng
Summary
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
Member of
Cataloging source
BTCTA
Dewey number
612.01575
Illustrations
illustrations
Index
index present
LC call number
QP601
LC item number
.M49 v.499
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
Series statement
Methods in enzymology,
Series volume
v. 499
Label
Biology of serpins, edited by James C. Whisstock and Phillip I. Bird, (electronic resource)
Publication
Bibliography note
Includes bibliographical references and indexes
http://library.link/vocab/branchCode
  • net
Contents
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
Control code
ocn704379416
Edition
1st ed
Extent
1 online resource (l, 405 p.)
Form of item
online
Isbn
9780123864710
Other physical details
ill
http://library.link/vocab/recordID
.b29949737
Specific material designation
remote
System control number
  • (OCoLC)704379416
  • sciencedirect0123864712

Library Locations

    • Deakin University Library - Geelong Waurn Ponds CampusBorrow it
      75 Pigdons Road, Waurn Ponds, Victoria, 3216, AU
      -38.195656 144.304955
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