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.

Since the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between the various cellular compartments, with concomitant movement of other proteins. Such events can also result in the release of molecular chaperones from cells. In bacteria, molecular chaperones are involved in the trafficking of other proteins and are themselves released into the external milieu. The increasing appreciation of the role of molecular chaperones and Protein-Folding Catalysts in the interplay between bacteria and the cells of their hosts is now an important area of research for understanding the mechanisms of infectious diseases. This volume brings together experts in the biochemistry, cellular biology, immunology and molecular biology of molecular chaperones and Protein-Folding Catalysts with a focus on the mechanisms of cellular trafficking of these proteins and the role of these variegated trafficking mechanisms in both human and animal health and disease.

Presents current information on the molecular mechanisms of drug action. Provides 159 essays describing groups of drugs and drug targets. Several essays deal with general principles of pharmacology, such as drug tolerance, drug addiction, or drug metabolism.

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.

This books provides the most up-to-date reviews on current advances in our understanding of the regulation of heat shock protein responses. Key basic scientists and clinical research laboratories from major universities, academic medical centers and pharmaceutical companies around the world have contributed chapters that review present research activity and importantly project this field into the future. For easy readability, the book is sub divided into four sections, including, Section I - HSP and Stress Responses; Section II - Chaperone Functions of HSP; Section III - HSP in Human Diseases; Section IV - Prognosis & Diagnosis of HSP. The book is a must read for researchers involved in biomedical research, drug discovery and design to improve human health.

All living organisms are exposed to rapidly changing environmental conditions which may lead to external stress. How organisms cope with stress - especially on the molecular level - is explained in Stress Proteins. Cells react to external stress - where the temperature-induced reaction known as "heat shock response" is the best studied example of stress - by activating special genes and subsequently synthesizing stress proteins. Surprisingly, this stress response is not only similar for all types of stress but even the involved stress proteins are virtually identical in all organisms from prokaryotic to eukaryotic cells, from bacteria to humans. This universality shows that stress proteins are vital for surviving and indicates that these proteins play an essential role in normal cell functions, in cell growth and metabolism. This explains the great interest in stress response research.

Since the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between the various cellular compartments, with concomitant movement of other proteins. Such events can also result in the release of molecular chaperones from cells. In bacteria, molecular chaperones are involved in the trafficking of other proteins and are themselves released into the external milieu. The increasing appreciation of the role of molecular chaperones and Protein-Folding Catalysts in the interplay between bacteria and the cells of their hosts is now an important area of research for understanding the mechanisms of infectious diseases. This volume brings together experts in the biochemistry, cellular biology, immunology and molecular biology of molecular chaperones and Protein-Folding Catalysts with a focus on the mechanisms of cellular trafficking of these proteins and the role of these variegated trafficking mechanisms in both human and animal health and disease.