LEADER 05281nam 2200649Ia 450 001 9910133857203321 005 20240313225341.0 010 $a3-527-65420-8 010 $a3-527-65418-6 010 $a3-527-65421-6 035 $a(CKB)3360000000455834 035 $a(EBL)1205604 035 $a(OCoLC)846495244 035 $a(SSID)ssj0000904699 035 $a(PQKBManifestationID)11943847 035 $a(PQKBTitleCode)TC0000904699 035 $a(PQKBWorkID)10925119 035 $a(PQKB)10920435 035 $a(MiAaPQ)EBC1205604 035 $a(Au-PeEL)EBL1205604 035 $a(CaPaEBR)ebr10716610 035 $a(CaONFJC)MIL494627 035 $a(PPN)183720210 035 $a(EXLCZ)993360000000455834 100 $a20121015d2013 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aAmyloid fibrils and prefibrillar aggregates $emolecular and biological properties /$fedited by Daniel Erik Otzen 205 $a1st ed. 210 $aWeinheim $cWiley-VCH$dc2013 215 $a1 online resource (440 p.) 300 $aDescription based upon print version of record. 311 $a3-527-33200-6 320 $aIncludes bibliographical references and index. 327 $aAmyloid Fibrils and Prefibrillar Aggregates; Contents; Preface; List of Contributors; 1 The Amyloid Phenomenon and Its Significance; 1.1 Introduction; 1.2 The Nature of the Amyloid State of Proteins; 1.3 The Structure and Properties of Amyloid Species; 1.4 The Kinetics and Mechanism of Amyloid Formation; 1.5 The Link between Amyloid Formation and Disease; 1.6 Strategies for Therapeutic Intervention; 1.7 Looking to the Future; 1.8 Summary; Acknowledgments; References; 2 Amyloid Structures at the Atomic Level: Insights from Crystallography 327 $a2.1 Atomic Structures of Segments of Amyloid-Forming Proteins2.1.1 Protein Segments That Form Amyloid-Related Crystals; 2.1.2 Atomic Structures of Fiber-Like Microcrystals; 2.2 Stability of Amyloid Fibers; 2.3 Which Proteins Enter the Amyloid State?; 2.4 Molecular Basis of Amyloid Polymorphism and Prion Strains; 2.5 Atomic Structures of Steric Zippers Suggest Models for Amyloid Fibers of Parent Proteins; 2.6 Atomic Structures of Steric Zippers Offer Approaches for Chemical Interventions against Amyloid Formation; 2.7 Summary; Acknowledgments; References 327 $a3 What Does Solid-State NMR Tell Us about Amyloid Structures?3.1 Introduction; 3.2 Principles of Solid-State NMR Spectroscopy and Experiments for Structural Constraints; 3.2.1 Isotope Labeling, Magic Angle Spinning, Dipolar Coupling, and Resonance Assignment; 3.2.2 De.ning the Amyloid Core by Magnetization Transfer from Water; 3.2.3 Determining the Fibril Registry; 3.2.4 Seeded versus Unseeded Fibrils; 3.3 Amyloid Fibrils Investigated by Solid-State NMR Spectroscopy; 3.3.1 A? peptides of Different Length; 3.3.2 Islet Amyloid Polypeptide (IAPP/Amylin): Parallel and Antiparallel Steric Zippers 327 $a3.3.3 ?-Synuclein: Polymorphism with Flexible Terminal Regions3.3.4 PrP: Rearrangements to Maintain a Fibrillar Core Region; 3.3.5 Yeast Prions with Glutamine/Asparagine-Rich Prion Domains: Sup35p, Ure2p, and Rnq1p; 3.3.6 Functional Amyloid: the Yeast Prion HET-s; 3.4 Summary; References; 4 From Molecular to Supramolecular Amyloid Structures: Contributions from Fiber Diffraction and Electron Microscopy; 4.1 Introduction; 4.2 History; 4.2.1 The Historical Use of X-ray Fiber Diffraction; 4.2.2 The Historical Use of Transmission Electron Microscopy; 4.3 Methodology; 4.3.1 X-Ray Fiber Diffraction 327 $a4.3.2 Transmission Electron Microscopy4.4 Recent Advances in Amyloid Structure Determination; 4.4.1 X-ray Fiber Diffraction; 4.4.2 Transmission Electron Microscopy; 4.5 Summary; Acknowledgments; References; 5 Structures of Aggregating Species by Small-Angle X-Ray Scattering; 5.1 Introduction; 5.2 Theoretical and Experimental Aspects; 5.3 Data Analysis and Modeling Methods; 5.4 Studying Protein Aggregation and Fibrillation Using SAXS; 5.4.1 Some General Considerations; 5.4.2SAXS Studies of Insulin, Glucagon, and ?-Synuclein; 5.4.3SDS-Induced Aggregation of ?-Synuclein 327 $a5.4.4 Multi-Component Fitting and Analysis of SAXS Data 330 $aSumming up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher o 606 $aAmyloid 606 $aGlycoproteins 615 0$aAmyloid. 615 0$aGlycoproteins. 676 $a572.68 701 $aOtzen$b Daniel Erik$f1969-$0958665 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910133857203321 996 $aAmyloid fibrils and prefibrillar aggregates$92172262 997 $aUNINA