How protein chaperones protect cells from neurodegenerative diseases Including contributions from leading experts, Protein Chaperones and Protection from Neurodegenerative Diseases provides an in-depth exploration of how protein chaperones are involved in shielding cells from toxic aggregated or misfolded protein states that cause ALS, Parkinson's, and related diseases. Examining how different protein chaperones ameliorate the toxicity of proteins that are known to cause neurodegenerative damage, the book addresses both research and clinical perspectives on chaperone and anti-chaperone properties. The intersection of molecular chaperones and neurodegeneration is an intensely studied area, partly because of the potential for manipulating the expression of molecular chaperones to thwart the progression of debilitating diseases, and partly because of the ever-aging global population. Discussing the potential to harness the power of protein chaperones, and future directions for research, discovery, and therapeutics, this book is essential reading for scientists working in the fields of biochemistry, molecular medicine, pharmacology and drug discovery, biotechnology and pharmaceutical companies, advanced students, and anyone interested in this cutting-edge topic.

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 neurodegenerative diseases. Heat shock proteins are protein repair agents that provide a line of defense against misfolded, aggregati- prone proteins. Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection reviews current progress on neural heat shock proteins (HSP) in relation to neurodegenerative diseases (Part I), neuroprotection (Part II), ext- cellular HSP (Part III) and aging and control of life span (Part IV). Key basic and clinical research laboratories from major universities and hospitals around the world contribute chapters that review present research activity and importantly project the field into the future. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Neuroscience, Neurodegenerative Diseases, Molecular Medicine, Aging, Physiology, Pharmacology and Pathology.

Protein misfolding and aggregation are hallmarks of several neurodegenerative proteinopathies. Though multiple factors like aging, oxidative stress, mitochondrial dysfunction, proteotoxic insults, genetic inconsistency, etc. are responsible for the dysfunction of the neuronal protein quality control system, targeting protein quality control has become an auspicious approach to halt the propagation of neurodegeneration. Quality Control of Cellular Protein in Neurodegenerative Disorders provides diverse aspects exploring the role of the protein quality control in neurodegenerative disorders and potential therapeutic strategies to combat the development and propagation of neurodegeneration. Featuring coverage on a broad range of topics such as molecular chaperones, protein misfolding, and stress signaling, this book is ideally designed for neurobiologists, neuropsychologists, neurophysiologists, medical professionals, neuropathologists, researchers, academicians, students, and practitioners engaged in studies of the protein quality control system in neuronal cells.

Research focused on protein folding, misfolding, and aggregation is leading to major advances across biochemistry and medicine. The elucidation of a folding code is proving to be of extreme importance in the postgenomic era, where a number of orphan genes have been identified for which no clear function has yet been established. This research is starting to shed light on the molecular and biochemical basis of a number of neurodegenerative diseases of dramatic impact. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies addresses key issues concerning protein misfolding and aggregation in neurodegenerative diseases. Building on recent developments, including the recognition of protein misfolding as both a marker and a causal agent, the text presents the work of those who are actively pursuing more effective treatments, as well as preventative measures, and a possible cure. These include the use of molecular chaperones to control misfolding and novel pharmaceuticals, as well as the potential role of various inhibitors and NSAIDS. A Comprehensive Multifaceted Examination of the Complex Causal Agents Implicated in Protein Misfolding Divided into five sections, this groundbreaking text provides up-to-date accounts for Alzheimer's, Parkinson's, Huntington's, Amyotrophic Lateral Sclerosis and Transmissible Spongiform Encephalitis. It also explores the highly likelihood that multiple factors, including oxidative stress, play a role in these complex diseases.

This book provides essential information on improving protein folding/stability, which is a result of the balance between the intra-molecular interactions of protein functional groups and their interactions with the solvent environment. The protein folding solvent environment mainly consists of salts, small molecule compounds, metabolites, molecular chaperones and other chemical species. Therefore, subtle change in the composition of the environment will alter the protein folding process. The importance of the solvent environment in protein folding is precisely due to the fact that various disease-causing proteopathies can be reversed by manipulating the solvent environment of the malfolded proteins. Hostile environmental stresses represent one of the basic causes of such challenges in protein folding or misfolding. Since cells commonly encounter extreme environmental fluctuations, it is crucial that they equip themselves with strategies to circumvent the hostile environmental conditions. Nature has developed many strategies to ensure that the complex and challenging protein folding reaction occurs with adequate efficiency and fidelity for the success of the organism. Among the strategies employed in a wide range of species and cell types is the elaboration of small organic molecules called osmolytes. Additionally, recent advances have also revealed that certain specific osmolytes might be key biomarkers of cancer, infectious diseases and vaccine flocculation. In fact, a large pool of data has been generated regarding their potential for the therapeutic intervention of neurodegenerative diseases and other metabolic disorders caused by protein aggregation or proteostasis failure. Reflecting the multiple applications of these small molecules in the health and other industries, this book combines contributions by respected leaders in the field and will help to inspire college students, basic researchers, and clinicians to translate these biological roles of osmolytes into clinical practice. It will also shed light on some important future prospects of osmolytes like their role as drug excipients and provide a deeper understanding of their mechanism of action in the prevention of neuro-degenerative diseases.

The book Heat Shock Proteins in Neuroscience provides the most comprehensive review on contemporary knowledge on the role of HSP in signaling pathways relevant to a number of diseases. Using an integrative approach, the contributors provide a synopsis of novel mechanisms, 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 of Neurological Aspects of HSP; Section II, focuses on Aspects of HSP in Neurodegenerative Diseases and Disorders, Section III, emphasizes the importance of HSP in Multiple Sclerosis; Section IV, reviews critical Aspects of HSP in Alzheimer’s Disease and Section V, gives a comprehensive update of the Development of HSP-Based Therapies for Neurological Disorders. Key basic and clinical research laboratories from major universities, academic medical hospitals, biotechnology and pharmaceutical laboratories around the world have contributed chapters that review present research activity and importantly project the field into the future. The book is a must read for starters and professionals in the fields of Neurology and Neurosciences, Translational Medicine, Clinical Research, Human Physiology, Biotechnology, Cell & Molecular Medicine, Pharmaceutical Scientists and Researchers involved in Drug Discovery.

Autophagy and phagocytosis are distinct yet partially morphologically similar processes. Understanding them is vital for the studies of cancer, aging, neurodegeneration, immunology, and infectious diseases. This book presents autophagosome and phagosome methods for novices and advanced researchers alike. Comprehensive and forward-thinking, the book offers a valuable guide to both cellular processes while inciting researchers to explore their potentially important connections.