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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.
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.
Soon to be a feature film from the creators of Downton Abbey starring Elizabeth McGovern, The Chaperone is a New York Times-bestselling novel about the woman who chaperoned an irreverent Louise Brooks to New York City in the 1920s and the summer that would change them both. Only a few years before becoming a famous silent-film star and an icon of her generation, a fifteen-year-old Louise Brooks leaves Wichita, Kansas, to study with the prestigious Denishawn School of Dancing in New York. Much to her annoyance, she is accompanied by a thirty-six-year-old chaperone, who is neither mother nor friend. Cora Carlisle, a complicated but traditional woman with her own reasons for making the trip, has no idea what she’s in for. Young Louise, already stunningly beautiful and sporting her famous black bob with blunt bangs, is known for her arrogance and her lack of respect for convention. Ultimately, the five weeks they spend together will transform their lives forever. For Cora, the city holds the promise of discovery that might answer the question at the core of her being, and even as she does her best to watch over Louise in this strange and bustling place she embarks on a mission of her own. And while what she finds isn’t what she anticipated, she is liberated in a way she could not have imagined. Over the course of Cora’s relationship with Louise, her eyes are opened to the promise of the twentieth century and a new understanding of the possibilities for being fully alive. Drawing on the rich history of the 1920s, ’30s, and beyond—from the orphan trains to Prohibition, flappers, and the onset of the Great Depression to the burgeoning movement for equal rights and new opportunities for women—Laura Moriarty’s The Chaperone illustrates how rapidly everything, from fashion and hemlines to values and attitudes, was changing at this time and what a vast difference it all made for Louise Brooks, Cora Carlisle, and others like them.
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.
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.
Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?, by A. Katrine Wallis and Robert B. Freedman Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins, by Cordelia Schiene-Fischer, Tobias Aumüller and Gunter Fischer Small Heat-Shock Proteins: Paramedics of the Cell, by Gillian R. Hilton, Hadi Lioe, Florian Stengel, Andrew J. Baldwin und Justin L. P. Benesch Allostery in the Hsp70 Chaperone Proteins, by Erik R. P. Zuiderweg, Eric B. Bertelsen, Aikaterini Rousaki, Matthias P. Mayer, Jason E. Gestwicki and Atta Ahmad Hsp90: Structure and Function, by Sophie E. Jackson Extracellular Chaperones, by Rebecca A. Dabbs, Amy R. Wyatt, Justin J. Yerbury, Heath Ecroyd and Mark R. Wilson
Author : Sebastian Hiller,Maili Liu,Lichun He Publisher : Royal Society of Chemistry Page : 413 pages File Size : 51,7 Mb Release : 2023-11-01 Category : Science ISBN : 9781839162824
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 Chaperones and Cell Signalling by Brian Henderson,A. Graham Pockley Pdf
This book reviews understanding of the biological roles of extracellular molecular chaperones. It provides an overview of the structure and function of molecular chaperones, their role in the cellular response to stress and their disposition within the cell. It also questions the basic paradigm of molecular chaperone biology - that these proteins are first and foremost protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving concept of proteins (such as molecular chaperones) as multi-functional molecules for which the term 'moonlighting proteins' has been introduced is discussed. The role of exogenous molecular chaperones as cell regulators is examined and the physiological and pathophysiological role that molecular chaperones play is described. In the final section, the potential therapeutic use of molecular chaperones is described and the final chapter asks the question - what does the future hold for the extracellular biology of molecular chaperones?
The Networking of Chaperones by Co-Chaperones by Adrienne L. Edkins,Gregory L. Blatch Pdf
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is the dynamic integration of the processes of protein folding, degradation and translocation to ensure that cellular function is finely tuned in space and time. This third edition of the book The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by co-chaperones, a diverse cohort of non-client proteins. Since the second edition was released, not only has knowledge deepened on how co-chaperones act as nodes to network and functionalise chaperones, but an understanding of their broader biological function has started to emerge. The third edition provides new and updated chapters highlighting recent developments and emerging themes on co-chaperones, such as their extracellular functions, their role in human disease and their status as putative drug targets. The book is a useful 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.
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.
Molecular Chaperones and Neurodegeneration by Cintia Roodveldt,Tiago F. Outeiro,Janice E. Braun Pdf
Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell. For over two decades until the present time, new functions have been discovered and several molecular mechanisms have been elucidated for many chaperones, while the field is being continuously challenged by new open questions. Probably as a consequence of the increasing research on the molecular bases of neurodegenerative diseases, and the realisation that many such disorders are linked to protein misfolding processes, unleashing the roles and mechanisms of chaperones in the context of neurodegeneration has become a prime scientific goal. This e-book contains a diversity of reviews, perspective and original research articles highlighting the importance and potential of this emerging subject.
Timothy D. Machajewski,Zhenhai Gao,David P. Rotella
Author : Timothy D. Machajewski,Zhenhai Gao,David P. Rotella Publisher : Royal Society of Chemistry Page : 443 pages File Size : 55,8 Mb Release : 2014 Category : Medical ISBN : 9781849736664
Inhibitors of Molecular Chaperones as Therapeutic Agents by Timothy D. Machajewski,Zhenhai Gao,David P. Rotella Pdf
This book aims to provide a comprehensive examination of the field of molecular chaperone inhibition and its application to pharmaceutical research. With several small molecule inhibitors in oncology clinical development, there is clearly intense interest in the chaperones as a molecular target. Filling a significant gap in the market by providing a detailed comparison of discovery programs across the industry, this text will find broad interest among researchers in the field of molecular chaperone pharmaceutical research, oncology research, and medicinal chemistry. Arranged into three main sections the book covers structure and function, small molecule inhibitors and concludes with a section discussing clinical perspectives. With specific chapters covering the discovery of key molecules such as, BIIB028, STA-9090, Serenex Hsp90 inhibitor, NVP-AUY922 and NVP-HSP990, this comprehensive text will be an essential treatise for researchers working in academia and industry.
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.
Molecular Chaperones in Human Disorders by Anonim Pdf
Molecular Chaperones in Human Disorders, Volume 114 in the Advances in Protein Chemistry and Structural Biology series, provides an overview of current developments in mechanisms underlying DNA repair and their involvement in maintaining chromatin repair, the balance between chromosomal repair pathways, tumorigenesis, immune signaling and infection-induced inflammation. Chapters in this new release cover Functional principles and regulation of molecular chaperones, Chaperones and retinal disorders, Protein misfolding and degradation in genetic diseases, Chaperone dysfunction in hereditary myopathic diseases, Diseases caused by functional disorder of molecular chaperones residing in the endoplasmic reticulum, and many other timely topics. Describes advances in our understanding on DNA repair mechanisms and the involvement of their dysregulation in promoting diseases Provides an ideal resource for a very wide audience of specialists, researchers and students Contains timely chapters written by well-renown authorities in their field Presents information that is well supported by a number of high quality illustrations, figures and tables