Title Molecular targets in protein misfolding and neurodegenerative disease / Pierfausto Seneci

Published London : Academic Press, 2015 ©2015

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Description 1 online resource (314 pages) : illustrations (some color) Contents Cover; Title Page; Copyright Page; Dedication; Contents; Abbreviations; Chapter 1 -- Protein Misfolding, Neurodegeneration and Tau; 1.1 -- The neurodegeneration scenario; 1.2 -- Protein folding: physiological benefits and pathological consequences; 1.3 -- Tau: An intrinsically disordered, flexible, and aggregation-prone protein; 1.4 -- Tauopathies: Aggregation-prone tau in neurodegenerative disease (NDD); 1.4.1 -- Class 0 Tauopathies; 1.4.2 -- Class I Tauopathies; 1.4.3 -- Class II Tauopathies; 1.4.4 -- Class III Tauopathies; 1.4.5 -- Class IV Tauopathies; 1.4.6 -- Tau Mutations; References Chapter 2 -- Targeting the Protein Quality Control (PQC) Machinery2.1 -- Molecular chaperones, PQC, and neurodegeneration; 2.2 -- Molecular targets; 2.2.1 -- Hsp27; 2.2.2 -- Hsp70; 2.2.3 -- Hsp90; 2.3 -- Disease-modifying compounds; References; Chapter 3 -- Proteasomal Degradation of Soluble, Misfolded Proteins; 3.1 -- UPS-mediated degradation of misfolded proteins; 3.2 -- UPS-mediated degradation of misfolded proteins in NDDs; 3.3 -- UPS-targets; 3.3.1 -- CHIP; 3.3.2 -- USP14; 3.4 -- Disease-modifying compounds; References; Chapter 4 -- Unselective Disposal of Cellular Aggregates 4.1 -- Autophagy-mediated degradation of protein aggregates4.2 -- Autophagy-mediated degradation of protein aggregates in NDDs; 4.3 -- Macroautophagy-targets; 4.3.1 -- mTORC1; 4.4 -- Disease-modifying compounds; References; Chapter 5 -- Selective Disposal of Insoluble Protein Aggregates; 5.1 -- Aggrephagy-mediated degradation of protein aggregates; 5.2 -- Selective autophagy-mediated degradation of protein aggregates in NDDs; 5.3 -- Selective autophagy-targets; 5.3.1 -- p62; 5.3.2 -- HDAC6; 5.4 -- Disease-modifying compounds; References; Chapter 6 -- Assembly and Disassembly of Protein Aggregates 6.1 -- Introduction6.2 -- Disordered protein aggregates and ordered amyloid fibrils; 6.2.1 -- The Target: Interfering with (Neuro)toxic Tau Species in the Aggregation Process; 6.3 -- Chaperone-driven disaggregation of protein aggregates; 6.3.1 -- The Target: Hsp110; 6.4 -- Disease-modifying compounds; References; Conclusions; Index Summary Aimed at "drug discoverers"--I.e. any scientist who is interested in neurodegenerative diseases in general, and in finding disease-modifying treatments in particular - the first edition of Molecular Targets in Protein Misfolding and Neurodegenerative Disease will contain both a detailed, discipline-specific coverage (paragraphs on medicinal chemistry, on clinical and preclinical characterization of compounds in development, on target identification and validation, on genetic factors influencing a pathology, etc.) and a drug discovery-oriented, overall evaluation of each target (validation, druggability, existing leads, etc.). Together these will satisfy the needs of various audiences, including in vitro biologists, pharmacologists, medicinal chemists, etc Bibliography Includes bibliographical references at the end of each chapters and index Notes Print version record Subject Molecular neurobiology. Nervous system -- Diseases Tauopathies -- drug therapy Tauopathies -- etiology Nervous System Diseases Molecular Targeted Therapy -- methods Protein Folding -- drug effects SCIENCE -- Life Sciences -- Zoology -- General. Molecular neurobiology Nervous system -- Diseases Form Electronic book ISBN 9780128004999 0128004991 0128001860 9780128001868 1322639523 9781322639529

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