Format:
Online-Ressource (XI, 155 p. 36 illus., 30 illus. in color, digital)
ISBN:
9783642354915
Series Statement:
Research and Perspectives in Alzheimer's Disease
Content:
The misfolding and aggregation of specific proteins is an early and obligatory event in many of the age-related neurodegenerative diseases of humans, and appears to occur many years before the onset of clinical symptoms. The initial cause of this pathogenic cascade and the means whereby disease spreads through the nervous system, remain uncertain. A recent surge of research, first instigated by pathologic similarities between prion disease and Alzheimer’s disease, has increasingly implicated corruptive protein templating, or seeding, as a prime factor in the neurodegenerative process. The prion-like corruption of proteins also characterizes such clinically and etiologically diverse neurological disorders as Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, and frontotemporal lobar degeneration. Understanding the misfolding, aggregation, trafficking and pathogenicity of affected proteins thus could reveal universal principles and common therapeutic targets for some of the most devastating and intractable human brain disorders
Note:
Includes index
,
Proteopathic Seeds and Neurodegenerative Diseases; Foreword; Contents; List of Contributors; Widening Spectrum of Prions Causing Neurodegenerative Diseases; Plaques, Tangles, and Inclusions; Aβ Prions; Inherited CJD and AD; Tau Prions; A New Psychiatry; Late-Onset Neurodegeneration; Fungal Prions; Amyloids; Synuclein Prions; SOD1 Prions; Huntingtin Prions; Nonpathogenic Mammalian Prions; Concluding Remarks; References; β-Amyloid Fibril Structures, In Vitro and In Vivo; Introduction; Organization of β-Sheets in Amyloid Fibrils; Polymorphism of Amyloid Fibrils
,
Structures of Nonfibrillar AggregatesStructural Studies of Aβ Fibrils from Human Brain Tissue; References; Structure-Activity Relationship of Amyloids; Amyloid Crystal Structures of Short Amyloidogenic Peptides: The Cross-β Spine at Atomic Resolution; The Bigger Picture: Amyloid Fibrils of HET-s(218-289); The Amyloid Compared to Other Protein Aggregates; Structure-Activity Relationship; The Structure-Activity Relationship in the HET-s Amyloid Prion; Peptide Hormone Amyloids in the Formation of Secretory Granules; Distinct Aggregates, Distinct Activities; Conclusion; References
,
Seeding and Cross-seeding in Amyloid DiseasesAmyloid and Amyloid Fibrils; Fibril Formation; Serum Amyloid A and AA Amyloidosis; Amyloid Enhancing Factor Is Aggregated Protein; Cross-seeding; Mechanisms of Cross-seeding; Is There a Link Between Different Amyloid Diseases?; Seeding and Cross-seeding of Human Amyloidosis by Environmental Factors; Conclusion; References; The Prion-Like Aspect of Alzheimer Pathology; Historical Perspective; Nature of the β-Amyloid-Inducing Agent; Inductive Spreading of β-Amyloid Aggregates; Similar Principles for Tau Lesions?; Conclusions
,
Implications and SpeculationsReferences; Amyloid-β Transmissibility; Introduction: Protein Misfolding Disorders; Misfolded Aβ Aggregates and AD; Mechanisms and Intermediates in Protein Misfolding Aggregation: The ``Seeding´´ Model; Proteins Behaving as Pathogens: The Case of Prion Diseases; Could AD Be Transmissible?; Concluding Remarks; References; Prion-Like Properties of Assembled Tau Protein; Prions and Tauopathies; Experimental Transmission of Tauopathy; Conclusion; References; Accumulating Evidence Suggests that Parkinson´s Disease Is a Prion-Like Disorder; Introduction
,
PD Progression and α-Syn Cell-to-Cell Transfer: Short Review of Our Current Knowledgeα-Syn Misfolding and Aggregation; Evidence for Cell-to-Cell Transfer and Possible Mechanisms; Recent In Vivo Studies; Recent In Vitro Studies; Release of α-Syn by Cells; Uptake of α-Syn by Recipient Cells and Nucleation; Intracellular Transport of α-Syn; Origin of the Seeding and Transfer In Vivo: What Is Missing in the Literature?; What Causes α-Syn Seeding?; In Vivo Evidence for Prion-Like Propagation of α-Syn: What Is Missing in the Literature?
,
Can α-Syn Induce a Nucleation Process After Cell-to-Cell Transfer?
,
Preface -- Widening Spectrum of Prions Causing Neurodegenerative Diseases (Stanley B. Prusiner).- b-Amyloid Fibril Structures, In Vitro and In Vivo (Robert Tycko).- Structure-Activity Relationship of Amyloids (Jason Greenwald and Roland Riek).- Seeding and Cross-seeding in Amyloid Diseases (Per Westermark and Gunilla T. Westermark).- The Prion-like Aspect of Alzheimer Pathology (Sarah K. Fritschi, Bahareh Eftekharzadeh, Giusi Manfredi, Tsuyoshi Hamaguchi, Götz Heilbronner, Amudha Nagarathinam, Franziska Langer, Yvonne S. Eisele, Lary Walker, Mathias Jucker).- Amyloid-β Transmissibility (Duran-Aniotz C, Morales R, Moreno-Gonzalez I, Soto C).- Prion-like Properties of Assembled Tau Protein (Florence Clavaguera, Markus Tolnay, and Michel Goedert).- Accumulating Evidence Suggests that Parkinson´s Disease is a Prion-like Disorder -- Nolwen L. Rey, Elodie Angot, Christopher Dunning, Jennifer A. Steiner, Patrik Brundin).- Propagation and Replication of Misfolded SOD1: Implications for Amyotrophic Lateral Sclerosis (Anne Bertolotti) -- Development of Drugs that Target Proteopathic Seeds Will Require Measurement of Drug Mechanism in Human Brain (Peter T. Lansbury).- The Role of Functional Prions in the Persistence of Memory Storage (Eric R. Kandel, Irina Derkatch, Elias Pavlopoulos) -- Subject Index.
Additional Edition:
ISBN 9783642354908
Additional Edition:
Buchausg. u.d.T. Proteopathic seeds and neurodegenerative diseases Berlin : Springer, 2013 ISBN 9783642354908
Additional Edition:
ISBN 3642354904
Language:
English
Keywords:
Nervendegeneration
;
Proteinfaltung
;
Konferenzschrift
DOI:
10.1007/978-3-642-35491-5
URL:
Volltext
(lizenzpflichtig)
Author information:
Christen, Yves 1948-
Author information:
Jucker, Mathias 1961-
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