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Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing compartments of the eukaryotic cells. The heat-inducible form HSPA1A (HSP70), its constitutive cytosolic cognate HSPA8 (Hsc70), its endoplasmic reticulum form HSPA5 (BiP), and its mitochondrial form HSPA9 (Mortalin), as well as the more distantly related HSPHs (HSP110s), make up 1-2 % of the total mass of proteins in human cells. They use the energy of ATP-hydrolysis to prevent and forcefully revert the process of protein misfolding and aggregation during and following various stresses, presumably by working as unfoldases to lift aberrant conformers out of kinetic traps. As such, HSP70s, in cooperation with their J-domain co-chaperones and nucleotide exchange factors (NEFs) and co-disaggregases, form an efficient network of cellular defenses against the accumulation of cytotoxic misfolded protein conformers, which may cause degenerative diseases such as Parkinson's and Alzheimer's disease, diabetes, and aging in general. In addition to their function in repair of stress-induced damage, HSP70s fulfill many housekeeping functions, including assisting the de novo folding and maturation of proteins, driving the translocation of protein precursors across narrow membrane pores into organelles, and by controlling the oligomeric state of key regulator protein complexes involved in signal transduction and vesicular trafficking. For reasons not well understood, HSP70s are also found on the surface of some animal cells, in particular cancer cells where they may serve as specific targets for cancer immunotherapy. Here, we gathered seven mini reviews, each presenting a complementary aspect of HSP70’s structure and function in bacteria and eukaryotes, under physiological and stressful conditions. These articles highlight how, the various members of this conserved family of molecular chaperones, assisted by their various J-domain and NEF cochaperones and co-disaggregases, harness ATP hydrolysis to perform a great diversity of life-sustaining cellular functions using a similar molecular mechanism.

Misfolding diseases --- Heat-Shock Proteins --- unfoldase --- proteostasis --- Disaggregase --- Misfolding diseases --- Heat-Shock Proteins --- unfoldase --- proteostasis --- Disaggregase

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Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing compartments of the eukaryotic cells. The heat-inducible form HSPA1A (HSP70), its constitutive cytosolic cognate HSPA8 (Hsc70), its endoplasmic reticulum form HSPA5 (BiP), and its mitochondrial form HSPA9 (Mortalin), as well as the more distantly related HSPHs (HSP110s), make up 1-2 % of the total mass of proteins in human cells. They use the energy of ATP-hydrolysis to prevent and forcefully revert the process of protein misfolding and aggregation during and following various stresses, presumably by working as unfoldases to lift aberrant conformers out of kinetic traps. As such, HSP70s, in cooperation with their J-domain co-chaperones and nucleotide exchange factors (NEFs) and co-disaggregases, form an efficient network of cellular defenses against the accumulation of cytotoxic misfolded protein conformers, which may cause degenerative diseases such as Parkinson's and Alzheimer's disease, diabetes, and aging in general. In addition to their function in repair of stress-induced damage, HSP70s fulfill many housekeeping functions, including assisting the de novo folding and maturation of proteins, driving the translocation of protein precursors across narrow membrane pores into organelles, and by controlling the oligomeric state of key regulator protein complexes involved in signal transduction and vesicular trafficking. For reasons not well understood, HSP70s are also found on the surface of some animal cells, in particular cancer cells where they may serve as specific targets for cancer immunotherapy. Here, we gathered seven mini reviews, each presenting a complementary aspect of HSP70’s structure and function in bacteria and eukaryotes, under physiological and stressful conditions. These articles highlight how, the various members of this conserved family of molecular chaperones, assisted by their various J-domain and NEF cochaperones and co-disaggregases, harness ATP hydrolysis to perform a great diversity of life-sustaining cellular functions using a similar molecular mechanism.

Misfolding diseases --- Heat-Shock Proteins --- unfoldase --- proteostasis --- Disaggregase

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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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Protein folding. --- Protein Folding. --- Protein Folding, Globular --- Folding, Globular Protein --- Folding, Protein --- Foldings, Globular Protein --- Foldings, Protein --- Globular Protein Folding --- Globular Protein Foldings --- Protein Foldings --- Protein Foldings, Globular --- Proteostasis --- Protein Multimerization --- Intrinsically Disordered Proteins --- Folding of proteins --- Proteins --- Folding --- Conformation

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Abnormal proteins are known to be associated with various pathologies. Most notably, these include amyloidoses, monoclonal protein deposits associated with plasma cell dyscrasia/multiple myeloma, cryoglobulins and various related organized and non-organized deposits. Amyloid and Related Disorders presents an overview of the most recent developments in this area including clinical presentation, etiology, pathogenesis, and differential diagnosis. The rationale for various therapies, including transplantation, is discussed and tissue diagnosis (its pitfalls and strategies for avoiding them) and laboratory support are included.   The involvement of all major organ systems including renal/genitourinary, cardiac, gastrointestinal, pulmonary, peripheral nerve/central nervous system, soft tissue and bone marrow pathology is covered.  This approach provides a unifying concept of these pathologic processes, which have systemic involvement, and which have, hitherto, not been universally appreciated. Awareness of these diseases among a wider audience of pathologists may increase the rate of their diagnosis as well as that of earlier diagnosis. This volume will be invaluable to specialized and general pathologists as well as cytopathologists; other medical professionals may also benefit from this concise update on the systemic amyloidoses.

Amyloidosis. --- Multiprotein Complexes --- Proteostasis Deficiencies --- Proteins --- Amino Acids, Peptides, and Proteins --- Macromolecular Substances --- Metabolic Diseases --- Nutritional and Metabolic Diseases --- Chemicals and Drugs --- Diseases --- Amyloidosis --- Amyloid --- Medicine --- Health & Biological Sciences --- Pathology --- Metabolism --- Disorders. --- Protein metabolism disorders --- Amyloid degeneration --- Medicine. --- Internal medicine. --- Nephrology. --- Pathology. --- Medicine & Public Health. --- Internal Medicine. --- Lymphoproliferative disorders --- Disorders --- Medicine, Internal --- Internal medicine --- Kidneys --- Disease (Pathology) --- Medical sciences --- Medicine, Preventive