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Molecular Chaperones of the Endoplasmic Reticulum by Martin Schröder Pdf
An important function of the endoplasmic reticulum is the folding of newly synthesised polypeptide chains. Several general and specialised chaperones operate in the endoplasmic reticulum to assist protein folding. This book reviews our current knowledge of molecular chaperones of the ER, including the HSP70 class chaperones BiP and GRP170, their DnaJ and GrpE co-chaperones, the HSP90 class chaperone GRP94, and the lectin chaperones calnexin, calmegin, and calreticulin. This book provides an overview of the biochemistry and physical chemistry of molecular chaperones with emphasis on molecular chaperones of the endoplasmic reticulum.
Handbook of Molecular Chaperones by Piero Durante,Leandro Colucci Pdf
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.
The book focuses on the latest discoveries on calreticulin, calnexin and other endoplasmic reticulum proteins. Calreticulin has been implicated to affect diverse cellular function and play a role in many pathologies including protein folding disorders, cardiac pathologies, cancer and autoimmunity. This book contains contributions from the world leaders in the area of endoplasmic reticulum function, protein folding, Calcium homeostasis and autoimmunity. It raises many intriguing questions about calreticulin, calnexin and the endoplasmic reticulum and gives a unique opportunity to realize the significance of these calcium-binding chaperones. The book is unique in every respect and we are not aware of any other publication focusing on these aspects of endoplasmic reticulum biology. Because of a central role of endoplasmic reticulum, calreticulin and calnexin in virtually all cellular functions, the book should be of interest to everyone in the biological sciences.
Molecular Chaperones in Health and Disease by Matthias Gaestel Pdf
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
The Molecular Chaperones Interaction Networks in Protein Folding and Degradation by Walid A. Houry Pdf
Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective.
Stress-Inducible Cellular Responses by U. Feige,R.I. Morimoto,Barbara Polla Pdf
This book will deal with heat shock proteins and more generally with stress-related inducible gene expression as a pleiotropic adaptive response to stress. It presents a textbook-like overview of the field not only to heat shock experts, but to physiologists, pharmacologists, physicians, neuropsychologists and others as well. It is intended to be a state-of-the-art and perspective book rather than an up-to-date presentation of recent data. It should provide a basis for new experimetal approaches to fields at the edge of the classical heat shock field. Drugs, UV irradiation and environmental toxics will be considered as important modulators of the stress response. Radical scavengers such as superoxide dismutases and inducible regulatory proteins of metallic ion status such as ferritin as well as immunophilins and protein disulfide isomerases will be considered within the frame of stress proteins. The potential practical applications of heat shock proteins in toxicology and medicine for the diagnosis, prognosis and eventually therapy of clinical conditions associated with an increased oxidative burden will be outlined. The role of heat shock proteins in the modulation of immune responses will also be included. The book considers heat shock from a broad perspective including fields for which heat-shock may become of importance in the very near future such as cellular responses to environmental stresses and complex stress responses under specific conditions. It was also felt timely to incorporate a whole section on medical and technological applications of stress proteins. The book will be invaluable for all those working on stress and is intended for every "stress laboratory" as a source of knowledge and perspectives.
HSF1 and Molecular Chaperones in Biology and Cancer by Marc Laurence Mendillo,David Pincus,Ruth Scherz-Shouval Pdf
Protein homeostasis, or “Proteostasis”, lies at the heart of human health and disease. From the folding of single polypeptide chains into functional proteins, to the regulation of intracellular signaling pathways, to the secreted signals that coordinate cells in tissues and throughout the body, the proteostasis network operates to support cell health and physiological fitness. However, cancer cells also hijack the proteostasis network and many of these same processes to sustain the growth and spread of tumors. The chapters in this book are written by world experts in the many facets of the proteostasis network. They describe cutting-edge insights into the structure and function of the major chaperone and degradation systems in healthy cells and how these systems are co-opted in cancer cells and the cells of the tumor microenvironment. The chapters also cover therapeutic interventions such as the FDA-approved proteasome inhibitors Velcade and Krypolis as well as other therapies currently under clinical investigation to disarm the ability of the proteostasis network to support malignancy. This compendium is the first of its kind and aims to serve as a reference manual for active investigators and a primer for newcomers to the field. This book is dedicated to the memory of Susan Lindquist, a pioneer of the proteostasis field and a champion of the power of basic scientific inquiry to unlock the mechanisms of human disease. The chapter “Reflections and Outlook on Targeting HSP90, HSP70 and HSF1 in Cancer: A Personal Perspective” is available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.
Guidebook to Molecular Chaperones and Protein-Folding Catalysts by Mary-Jane Gething Pdf
The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct folding and transport. This Guidebook catalogues the latest information on nearly 200 of these molecules, including the important class of heat shock proteins; each entry is written by leading researchers in the field.
Molecular Chaperones and Folding Catalysts by Bernd Bakau Pdf
One of the most intriguing discoveries in molecular biology in the last decade is the existence of an evolutionary conserved and essential system, consisting of molecular chaperones and folding catalysts, which promotes the folding of the proteins in the cell. This text summarizes our current knowledge of the cellular roles, the regulation and the mechanism of action of this system. It has a broad scope, covering cell biological, genetic and biochemical aspects of protein folding in cells from bacteria to man. Particularly appropriate to researchers working in basic and applied aspects of molecular medicine, this volume should also prove useful as an up-to-date reference book and as a textbook for specialized university courses.
Molecular Chaperones in the Cell by Peter A. Lund Pdf
In this text, leading experts synthesise our body of knowledge , and the reader gains not only a fuller understanding of the roles of chaperones in the context of cellular processes, but also an insight into the nature of these proteins.
The Networking of Chaperones by Co-chaperones by Gregory L. Blatch Pdf
The Networking of Chaperones by Co-chaperones updates the current understanding of how chaperones are regulated and networked. It is a resource for those in the specialized field of cell stress and chaperones. The book will also be of interest to those in broader cross-cutting field such as cellular networks and systems biology.
Molecular Chaperones by R.J. Ellis,R.A. Laskey,G.H. Lorimer Pdf
Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks by Peter Csermely,László Vígh Pdf
This book makes a novel synthesis of the molecular aspects of the stress response and long term adaptation processes with the system biology approach of biological networks. Authored by an exciting mixture of top experts and young rising stars, it provides a comprehensive summary of the field and identifies future trends.
The Networking of Chaperones by Co-chaperones by Gregory Lloyd Blatch,Adrienne Lesley Edkins Pdf
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
