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Protein Misfolding, Aggregation and Conformational Diseases, Part B: Molecular Mechanisms of Conformational Diseases, is a comprehensive volume providing a broad and detailed discussion of the relationships of protein misfolding and aggregation with the pathogenesis of numerous conformational diseases. While the Part A was dedicated to the description of the general mechanisms underlying protein misfolding, aggregation, and development of protein deposition disorders, this volume summarizes recent achievements in the understanding of the molecular mechanisms of conformational diseases. Research indicates that these mechanisms are highly diverse and range from the altered protein structure leading to the enhanced propensity for aggregation/deposition or the impaired functions and ending with changes in supra-molecular structures or posttranslational modification. Protein Misfolding, Aggregation and Conformational Diseases, Part B: Molecular Mechanisms of Conformational Diseases, is an ideal book for pharmaceutical scientists, molecular and cellular biologists, biochemists, immunologists, protein scientists, and biophysicists.

Protein folding. --- Cell aggregation. --- Proteins --- Pathophysiology. --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Aggregation, Cell --- Cell patterning --- Cell interaction --- Microbial aggregation --- Folding of proteins --- Folding --- Conformation --- Immunology. --- Cytology. --- Cell Biology. --- Immunobiology --- Life sciences --- Serology --- Cell biology --- Cellular biology --- Biology --- Cells --- Cytologists --- Cell biology.

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The past five years have seen a major leap forward in our understanding of the way proteins fold into their three-dimensional, functional conformations. The rapidly expanding literature covers in vivo as well as in vitro studies and forms the basis for an important biotechnology industry. In this volume, a group of leading scientists review and assess the experimental evidence that underpins these advances and look for signs of a general picture of how proteins fold. Contributors show how such conformational changes are leading to new insights into membrane translocation, pore formation, and the clinically important aggregation phenomena. Students and researchers of biochemistry and molecular biology will find this book to be the ideal introduction to an exciting field.

General biophysics --- Molecular biology --- Macromolecules --- Protein folding --- Protéines --- Repliement --- Protein Folding. --- Folding of proteins --- Proteins --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Protein Multimerization --- Intrinsically Disordered Proteins --- Folding --- Conformation --- Protein folding. --- Protéines --- Protein Folding --- Proteostasis --- fysicochemie

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Misfoldedaggregatedproteinoncewasconsideredasinterestingasyesterday’strash—a bothersome by-product of important and productive activities, to be disposed of and forgotten as quickly as possible. Yesterday’s trash has become today’s focus of cons- erable scienti?c interest for at least two reasons: (1) protein aggregates are at the core of a number of chronic degenerative diseases such as Alzheimer’s disease, and (2) - gregation poses signi?cant obstacles to the manufacture of safe, ef?cacious, and stable protein products. As interest in protein misfolding, aggregation, and stability has soared beyond the core group of traditional protein-folding scientists, and as substantial scienti?c progress in understanding and controlling protein misfolding has been achieved, the need to summarize the state of the art became manifest. Although there are many excellent texts and edited collections on protein structure and folding, these volumes tend to relegate protein misfolding and aggregation to a minor role. Review articles and books focused on the biological role of protein aggregates in diseases have been published recently. Misbehaving Proteins: Protein (Mis)folding, Aggregation, and Stability differs from theseotherrecenteffortsinitsemphasisonfundamentalcomputationalandexperimental studies and in its linkage of disparate consequences of protein misfolding (e.g., from clinical manifestations to manufacturing headaches) to their common causes.

Protein folding. --- Cell aggregation. --- Folding of proteins --- Proteins --- Aggregation, Cell --- Cell patterning --- Cell interaction --- Microbial aggregation --- Folding --- Conformation --- Proteomics. --- Biochemistry. --- Biochemical engineering. --- Biotechnology. --- Analytical biochemistry. --- Biochemistry, general. --- Biochemical Engineering. --- Analytical Chemistry. --- Analytic biochemistry --- Biochemistry --- Chemistry, Analytic --- Chemical engineering --- Genetic engineering --- Bio-process engineering --- Bioprocess engineering --- Biotechnology --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Molecular biology --- Composition --- Bioanalytic chemistry --- Bioanalytical chemistry --- Analytical chemistry --- Analytical chemistry. --- Analysis, Chemical --- Analytic chemistry --- Chemical analysis

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A. K. Wallis R. B. Freedman Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding? C. Schiene-Fischer T. Aumüller G. Fischer Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins   G. R. Hilton H. Lioe F. Stengel A. J. Baldwin J. L. P. Benesch Small Heat-Shock Proteins: Paramedics of the Cell E. R. P. Zuiderweg E. B. Bertelsen A. Rousaki M. P. Mayer J. E. Gestwicki A. Ahmad Allostery in the Hsp70 Chaperone Proteins S. E. Jackson Hsp90: Structure and Function R. A. Dabbs A. R. Wyatt J. J. Yerbury H. Ecroyd M. R. Wilson Extracellular Chaperones.

Molecular chaperones. --- Protein folding. --- Folding of proteins --- Proteins --- Chaperone proteins --- Chaperones, Molecular --- Chaperonins --- Folding --- Conformation --- Bioorganic chemistry. --- Biochemistry. --- Biotechnology. --- Bioorganic Chemistry. --- Protein Science. --- Biological and Medical Physics, Biophysics. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Bio-organic chemistry --- Biological organic chemistry --- Biochemistry --- Chemistry, Organic --- Chemical engineering --- Genetic engineering --- Composition --- Proteins . --- Biophysics. --- Biological physics. --- Biological physics --- Physics --- Proteids --- Biomolecules --- Polypeptides --- Proteomics

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Prions --- Protein folding --- Prions. --- Protein folding. --- Folding of proteins --- Proteins --- Infectious protein particles --- Prion proteins --- Protein particles, Infectious --- Proteinaceous infection particles --- PrP proteins --- Folding --- Protein Folding --- Conformation --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Proteostasis --- Protein Multimerization --- Intrinsically Disordered Proteins --- Mink Encephalopathy Virus --- Encephalopathy Virus, Mink --- Scrapie --- Agriculture Sciences --- Soil Chemistry, Microbiology, Fertility & Fertilizers --- Prion --- protein folding --- protein assembly disorders --- prion diseases --- prions --- Protein Folding.