The Nature and Origin of Amyloid Fibrils (eBook)

Gregory R. Bock, Jamie A. Goode (Herausgeber)

eBook Download: PDF

2008
John Wiley & Sons (Verlag)
978-0-470-51493-1 (ISBN)

Infos

Amyloid fibrils are associated with a range of pathological disorders including Alzheimer's Disease, Down's syndrome, diabetes, cardiomyopathies, and transmissible spongiform encephalopathies. This volume is a comprehensive account of recent developments in the understanding of the process of amyloid fibrils. Contains up-to-date data on all of the clinical problems which, despite their pathological significance, are still largely unsolved.

The Novartis Foundation is an international scientific and educational charity which promotes the study and general knowledge of science and in particular encourages international co-operation in scientific research.

Inhalt

THE NATURE AND ORIGIN OF AMYLOID FIBRILS 5
Contents 7
Participants 10
Preface 13
Introduction 15
In memoriam 19
A molecular model of the amyloid fibril 20
Refined fibril structures: the hydrophobic core in Alzheimer's amyloid b-protein and prion as revealed by X-ray diffraction 36
General discussion I 54
Modulating conformational factors in transthyretin amyloid 61
Proteoglycans and amyloid fibrillogenesis 72
Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy 87
General discussion II 104
Metabolism of amyloid proteins 118
Alzheimer’s disease: genesis of amyloid 133
Apolipoprotein E and amyloidogenesis 146
Interaction of transthyretin with amyloid B-protein: binding and inhibition of amyloid formation 160
General discussion III 179
B-amyloid precursor protein and early-o nset Alzheimer’s disease 184
Prion protein amyloid: separation of scrapie infectivity from PrP polymers 195
General discussion IV 216
Ageing and amyloid fibrillogenesis: lessons from apolipoprotein Al, transthyretin and islet amyloid polypeptide 219
General discussion V 237
FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation 242
Index of contributors 257
Subject index 259

Produkt-Details

• Erscheint lt. Verlag: 30.4.2008
• Reihe/Serie: Novartis Foundation Symposia
• Reihe/Serie: Novartis Foundation Symposium
• Sprache: englisch
• Themenwelt: Medizin / Pharmazie ► Medizinische Fachgebiete ► Neurologie
• Themenwelt: Studium ► 1. Studienabschnitt (Vorklinik) ► Histologie / Embryologie
• Themenwelt: Studium ► 1. Studienabschnitt (Vorklinik) ► Physiologie
• Themenwelt: Studium ► 2. Studienabschnitt (Klinik) ► Pathologie
• Themenwelt: Naturwissenschaften ► Biologie ► Humanbiologie
• Themenwelt: Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie
• Schlagworte: Amyloid • Amyloidogenesis • antiparallel • Basis • Biowissenschaften • Cell & Molecular Biology • Characteristics • combination • components • Entity • Fibrils • insoluble • known • Life Sciences • nonprotein • Plaques • Process • Protein • Quaternary • recently • selfassembled • Sheet • Single • Structure • years • Zell- u. Molekularbiologie
• ISBN-10: 0-470-51493-0 / 0470514930
• ISBN-13: 978-0-470-51493-1 / 9780470514931