Handbook of molecular chaperones : roles, structures and mechanisms
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Bibliographic Information
Handbook of molecular chaperones : roles, structures and mechanisms
（Cell biology research progress series）
Nova Science Publishers, c2010
- : hard
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Includes bibliographical references and index
Description and Table of Contents
Description
Molecular chaperones are a ubiquitous class of proteins that play important roles in protein folding and in the protection of cells from several stresses associated with the disruption of three native dimensional structures of proteins. The most important of these proteins are the so-called heat shock proteins (HSPs), also known as stress proteins. This book examines some of the biological aspects of this intriguing family of proteins that are important for consideration of the "proteiomics of HSPs". This book also reviews current research on protein folding in the endoplasmic reticulum (ER) and the functions of ER-resident molecular chaperones in protein folding in the ER. The biochemical, structural and functional information on Redox Enzyme Maturation Proteins (REMPs) are also reviewed in detail. Furthermore, recent progress in molecular biology has provided new insights into the molecular basis of diseases and molecular targets for diagnosis and therapy of human diseases. The role of molecular biology research in molecular imaging is examined, as well as the applications of molecular imaging in diagnostics, gene therapy and drug development. Other chapters in this book explore the role of protists as promising objects for the study of adaptive mechanisms at the biochemical and the molecular level, the different trends in the evolution of molecular adaptations to adverse environmental conditions, and a review of the molecular mechanisms of bicyclol in the protection against liver damage.
Table of Contents
- Preface
- Molecular Chaperones of the Endoplasmic Reticulum
- Type III Secretion Chaperones: A Molecular Toolkit for all Occasions
- Advances in Heat Shock Proteomics: Towards a Better Understanding of the Physiology & Pathophysiology of Molecular Chaperones
- System Specific Chaperones for Membrane Redox Enzyme Maturation in Bacteria
- Role of Molecular Biology in Molecular Imaging
- Yeast Protein Aggregates, Containing Chaperones & Glucose Metabolism Enzymes
- Structure & Multiple Functions of Cyclophilin 40: A Divergent Loop Cyclophilin
- Free-Living Protists as a Model for Studying Heat Shock Proteins in the Cell
- Quality Control in the Secretory Pathway
- Structure, Properties & Multiple Functions of Human Small Heat Shock Protein HspB8 (Hsp22, H11 Protein Kinase or E2IG1)
- Small Stress Proteins & their Therapeutic Potential
- The eukaryotic chaperonin CCT (TRiC): Structure, Mechanisms of Action & Substrate Diversity
- The role of molecular chaperones in plant stress response
- Chaperone Activity of Intrinsically Disordered Proteins
- Fluorescence Study on Aggregation of a-Crystallin & Insulin
- The Induction of Hepatic Heat Shock Protein 27 & 70 by an Anti-Hepatitis Drug-Bicyclol & its Role in Protection against Liver Injury
- Plant Heat Shock Proteins as Molecular Chaperones in Normal & Stress Conditions
- Different Mechanisms Responsible for Stress Resistance Operate in the Same Insect Order
- Bi-Directional Hsp Response in Homeothermic Livestock
- The Chaperonin Containing T-complex Polypeptide: Do Monomeric Subunits Have Discrete Individual Functions?
- Evidence for In Vivo Phosphorylation of Hsp26 from Saccharomyces Cerevisiae
- Index.
by "Nielsen BookData"
