Biology of serpins
Biology of serpins [electronic resource] /
edited by James C. Whisstock and Phillip I. Bird.
- 1st ed.
- San Diego, CA : Academic Press, 2011.
- 1 online resource (l, 405 p.) : ill.
- Methods in enzymology, v. 499 0076-6879 ; .
- Methods in enzymology ; v. 499. .
Includes 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.
9780123864710 (electronic bk.) 0123864712 (electronic bk.)
Serpins.
Proteins.
Protein folding.
Proteins--Biotechnology.
Protein folding.
Proteins.
Proteins--Biotechnology.
Serpins.
Serpins.
Electronic books.
QP601 / .M49 v.499
612.01575
QU 136
Includes 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.
9780123864710 (electronic bk.) 0123864712 (electronic bk.)
Serpins.
Proteins.
Protein folding.
Proteins--Biotechnology.
Protein folding.
Proteins.
Proteins--Biotechnology.
Serpins.
Serpins.
Electronic books.
QP601 / .M49 v.499
612.01575
QU 136
