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HSP70 Heat-Shock Proteins --- Protein Folding --- Transcription Factors --- Heat-Shock Response --- metabolism --- metabolism --- physiology

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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.

molecular chaperone --- therapeutics --- neurodegenerative disease --- heat-shock response --- protein misfolding --- neuroprotection --- neurodegeneration --- heat-shock protein --- proteostasis --- amyloid protein

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Multi-disciplinary peer-reviewed journal that captures the eclectic spirit of the cellular stress response field in a single, concentrated source of current information.

Histology. Cytology --- Drug Toxicity --- Heat-Shock Response --- Metals --- Molecular Chaperones --- Oxidative Stress --- Cytology --- Stress (Physiology) --- Oxidative stress --- Molecular chaperones --- Cytologie --- Stress --- Stress oxydatif --- Molécules chaperonnes --- toxicity --- Periodicals. --- Périodiques --- Cell Survival. --- Drug-Related Side Effects and Adverse Reactions. --- Heat-Shock Response. --- Molecular Chaperones. --- Oxidative Stress. --- Cytology. --- Molecular chaperones. --- toxicity. --- 576 --- 57 --- Cellular and subcellular biology. Cytology --- Biological sciences in general --- Periodicals --- Health Sciences --- Life Sciences --- Pathology --- Biology --- Cytology, Cell Biology --- Micro and Molecular Biology --- Toxicology --- 576 Cellular and subcellular biology. Cytology --- Proteins

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This book presents a large amount of information related to the heat shock response and heat shock factor (HSF), describes core observations about molecular mechanisms and pathophysiological roles, and provides fundamental concepts on the basis of information from diverse aspects. This adaptive response to high temperature or protein misfolding is a fundamental mechanism to maintain the capacity of protein homeostasis, or proteostasis, and is evolutionally conserved among all living organisms, including bacteria and humans, on the earth. Furthermore, physiological and pathological roles of HSF have been extensively studied in fruit fly, worm, and mouse models. It has been revealed that HSF plays roles in development of the brain, reproductive and sensory organs, and in ageing, inflammation, and circadian rhythm. Analysis of the mechanisms have uncovered that HSF exerts a wide range of effects on gene expression and epigenetic status on the whole genome. Moreover, loss or gain of HSF function is also closely related to protein-misfolding diseases including neurodegenerative diseases, psychiatric diseases, heart diseases, and cancers. Therefore, HSF is now thought to be a promising therapeutic target for treatment of these refractory diseases. For undergraduate students, this is a highly understandable source of information on heart shock response and HSF, covering the basis of HSF biology, the physiological role of HSF, and disease associated with HSF function. This book not only serves as a guide to the heat shock response and HSF for students and young researchers in other fields, but also is a cornerstone for future work in the field related to the heat shock response and HSF.

Heat shock proteins --- Heat-Shock Response --- Heat-Shock Proteins --- Protein Folding --- Physiology --- Transcription Factors --- Biophysical Processes --- Proteins --- Biological Science Disciplines --- Stress, Physiological --- Molecular Chaperones --- Physiological Processes --- Natural Science Disciplines --- Biophysical Phenomena --- Amino Acids, Peptides, and Proteins --- Physical Phenomena --- Disciplines and Occupations --- Chemicals and Drugs --- Physiological Phenomena --- Phenomena and Processes --- Cytology --- Biology --- Health & Biological Sciences --- Heat shock proteins. --- Stress proteins --- Cytology. --- Biochemistry. --- Human physiology. --- Cell Biology. --- Protein Science. --- Human Physiology. --- Animal Biochemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Human biology --- Human body --- Composition --- Cell biology. --- Proteins . --- Proteids --- Biomolecules --- Polypeptides --- Proteomics

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Alzheimer’s disease (AD) is an age-related neurological disease that affects tens of millions of people, in addition to their carers. Hallmark features of AD include plaques composed of amyloid beta, as well as neurofibrillary tangles of tau protein. However, despite more than a century of study, the cause of Alzheimer’s disease remains unresolved. The roles of amyloid beta and tau are being questioned and other causes of AD are now under consideration. The contributions of researchers, model organisms, and various hypotheses will be examined in this Special Issue.

HOTAIR --- neurosciences --- sleep disturbance --- positron emission tomography (PET) --- vitamin B complex --- neurodegeneration --- Tau --- miR-15/107 --- default-mode network --- complement receptor 1 --- neuronal differentiation --- epigenetics --- brain glucose metabolism --- oligomerization --- genetic risk --- A?O receptors --- prion --- ryanodine receptor --- type 3 diabetes --- complement --- cognitive behavioral therapy for insomnia --- cognitive function --- epigenome-wide association study --- Alzheimer’s disease --- calcium signaling --- ?-secretase --- tau --- Prolyl isomerases --- NEAT1 --- complement C3b/C4b receptor --- proteostasis --- amyloid beta --- yeast --- slow-wave sleep --- amyloid ? --- nutrition --- 4 --- protein aggregation --- apolipoprotein E --- dementia --- MALAT1 --- inositol 1 --- lncRNAs --- molecular biology --- methylenetetrahydrofolate reductase MTHFR gene --- 5-trisphosphate receptor --- CR1 density --- miR-34c --- aggregation --- heat shock protein --- dendritic spine --- S-adenosylmethionine --- beta amyloid --- ion channel --- inflammation --- sleep fragmentation --- cystathionine-?-lyase CTH gene --- DNA methylation --- heat shock response --- microglia --- drug target discovery --- amyloid-? oligomer --- therapy --- CR1 length polymorphism --- methylome --- APOE gene --- ubiquitin --- magnetic resonance imaging (MRI) --- neuronal degeneration --- type 2 diabetes --- Pin1 --- mild cognitive impairment --- dairy products --- endoplasmic reticulum --- oxidative stress --- Hispanics --- CDK5R1