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This book surveys the current knowledge concerning the expression and function of stress proteins in different organisms, ranging from prokaryotes to humans. It provides an overview of the diversity and complex evolutionary history of cell stress proteins and describes their function and expression in different eukaryote models. The book will appeal to researchers and scientists in biochemistry, cell biology, microbiology, immunology, and genetics.
Heat shock proteins are emerging as important molecules in the development of cancer and as key targets in cancer therapy. These proteins enhance the growth of cancer cells and protect tumors from treatments such as drugs or surgery. However, new drugs have recently been developed particularly those targeting heat shock protein 90. As heat shock protein 90 functions to stabilize many of the oncogenes and growth promoting proteins in cancer cells, such drugs have broad specificity in many types of cancer cell and offer the possibility of evading the development of resistance through point mutation or use of compensatory pathways. Heat shock proteins have a further property that makes them tempting targets in cancer immunotherapy. These proteins have the ability to induce an inflammatory response when released in tumors and to carry tumor antigens to antigen presenting cells. They have thus become important components of anticancer vaccines. Overall, heat shock proteins are important new targets in molecular cancer therapy and can be approached in a number of contrasting approaches to therapy.
Heat shock proteins (HSPs) were discovered as polypeptides induced by stress that can be found in all kingdoms of cellular organisms. Their functions were, a first enigmatic and these proteins were thus classified by molecular weight, as in—Hsp27, Hsp70, Hsp90, Hsp110. More recently, each of these size-classified molecules has attributed a role in protein folding, and they thus came to be known, as a class, as molecular chaperones. However, the they possess properties beyond chaperoning. Indeed, their discovery in the extracellular spaces suggested roles in regulation of the immune responses.
The book Heat Shock Protein 90 in Human Diseases and Disorders provides the most comprehensive review on contemporary knowledge on the role of HSP90. Using an integrative approach, the contributors provide a synopsis of novel mechanisms, previously unknown signal transduction pathways. To enhance the ease of reading and comprehension, this book has been subdivided into various section including; Section I, reviews current progress on our understanding Oncogenic Aspects of HSP90; Section II, focuses on Bimolecular Aspects of HSP90; Section III, emphasizes and HSP90 in Natural Products Development and Section IV; give the most up to date reviews on Clinical Aspects of HSP90. Key basic and clin...
A widespread appreciation for the role that calcium plays in cell physiology and patho physiology has now been achieved due to the pioneering studies of many of the scientists who attended the VIIth International Spring Symposium on Health Sciences at George Washington University in Washington, D. C. The participants in this unique meeting rep resented diverse fields of basic and clinical research, such as molecular physiology, oncology, molecular genetics, cardiology, bioenergetics, pathology, and endocrinology. The content of the proceedings of the symposium represents work in these and other areas of biomedical research. Organization of the book is aimed at striking a balance between the ...
With the prevalence of neurodegenerative diseases on the rise as average life expectancy increases, the hunt for effective treatments and preventive measures for these disorders is a pressing challenge. Neurodegenerative disorders such as Alzheimer’s disease, Huntington’s disease, Parkinson’s disease and amyotrophic lateral sclerosis have been termed ‘protein misfolding disorders’ that are char- terized by the neural accumulation of protein aggregates. Manipulation of the cellular stress response involving the induction of heat shock proteins offers a the- peutic strategy to counter conformational changes in neural proteins that trigger pathogenic cascades resulting in neurodegener...
This original and truly multidisciplinary book explores how a variety of separate fields have been impacted by COVID-19 and how they can contribute to tackling the problems created by the disease. Covering the humanities, social sciences, physical sciences, life sciences, and health sciences, it offers varied perspectives on the positive and negative impacts of the COVID-19 pandemic on the human race and specifically on Indonesians. The book will be of interest to researchers working in many different fields, university students, the general public, and policy makers concerned with business and the economy, management, culture, and the provision of health services.
The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological functions, the development of ligand-based structural complexes and the consequent pharmacological or biotechnological applications of these processes. The involvement of molecular chaperones in several processes ranging from regulation of transcription factors and protein-protein interactions in bacteria to proteostasis, signaling pathways and cancer are also addressed. The book is an essential consulting tool for researchers, working professionals in academia or industry, and students of all levels who wish to obtain the most relevant and updated information currently available about protein folding and chaperones.
This book provides the most up-to-date review on new mechanisms and provides exciting insights into how heat shock proteins modulate the hosts’ immune response. Written by leaders in the field of heat shock protein immunobiology, the chapters systematically and in a step-wise fashion take the reader through the fascinating sequence of events by which heat shock proteins activate immune responses and provide answers as to its biological significance to the host.
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?