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Author:   Natalya K Nagradova
Publisher:   Nova Science Publishers Inc
Imprint:   Nova Science Publishers Inc
Dimensions:   Width: 21.50cm , Height: 0.70cm , Length: 14.00cm
Weight:   0.162kg
ISBN:  

9781606924662

ISBN 10:   1606924664
Pages:   75
Publication Date:   01 April 2009
Audience:   College/higher education ,  Professional and scholarly ,  Undergraduate ,  Postgraduate, Research & Scholarly
Format:   Paperback
Publisher's Status:   Active
Availability:   Out of stock  
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Table of Contents

Preface; Introduction; Eukaryotic Protein Disulfide Isomerase (PDI); The Role of Protein Disulfide Isomerase in the Endoplasmic Reticulum; Modular Organization of the PDI Molecule and the Role of Different Domains; Functional Properties of PDI Active CentersThe pKa Values of Essential Cysteine Residues; Disulfide Isomerization: The Essential Function of PDI; The Most Significant Cellular Function of PDI Is the Isomerization of Non-Native Disulfide Bonds; The Mechanism of the Isomerization Reaction Catalyzed by PDI Depends on the Structure of Protein Substrate; Relationship between the Overall Structure of PDI Molecule and Its Activity as a Protein Disulfide Isomerase; Is PDI Capable of Discriminating between Native and Non-Native Disulfides?; Dithiol Oxidation Catalyzed by PDI; Ero1p: An Enzyme Producing Disulfide Bonds for Oxidative Protein Folding in the Endoplasmic Reticulum; The Evidence that Oxidizing Equivalents Flow from Ero1p to Substrate Proteins via PDI; The Mechanism of Ero1p Oxidative Activity in Protein Disulfide Bond Formation; The X-Ray Crystal Structure of Ero1p Reveals the Spatial Relationship between Functional Cysteines and the Bound FAD; Two Catalytic Centers of PDI Are Not Equivalent; The Role of Glutathione in Oxidative Protein Folding in Endoplasmic Reticulum; Oxidized Glutathione Does Not Provide the Oxidation Equivalents Necessary for the Formation of Disulfide Bonds; GSH Imported into the Endoplasmic Reticulum from Cytosol Can Directly Reduce PDI; Disulfide Bond Formation and Isomerization in Prokaryotes; A Pathway for Disulfide Bond Formation in the Periplasm; DsbA, a Catalyst in Disulfide Bond Formation; DsbB, a Protein Responsible for Reoxidation of DsbA; Similarities in Prokaryotic and Eukaryotic Disulfide Bond-Forming Pathways; A Pathway for Disulfide Bond Isomerization in the Periplasm; DsbC, a Disulfide Isomerase; Dimerization of DsbC Is a Prerequisite for Its Isomerase Activity; Dimerization of DsbC Protects Its Active Sites from Oxidation by DsbB; DsbG, a Paralogue of DsbC; DsbD, a Recycler of Reduced DsbC and DsbG; How Does DsbD Work?; Conclusion; Index.

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