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Amyloid fibrils and prefibrillar aggregates : molecular and biological properties /
Summing up almost a decade of biomedical research, this topical handbook is a reference on the topic which incorporates recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies. The second part looks at the diagnosis and b...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Weinheim :
Wiley-VCH,
[2013]
|
| Temas: | |
| Acceso en línea: | Texto completo |
MARC
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| 245 | 0 | 0 | |a Amyloid fibrils and prefibrillar aggregates : |b molecular and biological properties / |c edited by Daniel Erik Otzen. |
| 260 | |a Weinheim : |b Wiley-VCH, |c [2013] | ||
| 300 | |a 1 online resource (xxviii, 481 pages) : |b illustrations | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 504 | |a Includes bibliographical references and index. | ||
| 520 | 8 | |a Summing up almost a decade of biomedical research, this topical handbook is a reference on the topic which incorporates recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies. 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. | |
| 588 | 0 | |a Print version record. | |
| 505 | 0 | |a Amyloid 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 -- 2.1 Atomic Structures of Segments of Amyloid-Forming Proteins -- 2.1.1 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 -- 3 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 AÝ peptides of Different Length -- 3.3.2 Islet Amyloid Polypeptide (IAPP/Amylin): Parallel and Antiparallel Steric Zippers -- 3.3.3 Ü-Synuclein: Polymorphism with Flexible Terminal Regions. | |
| 505 | 8 | |a 3.3.4 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 -- 4.3.2 Transmission Electron Microscopy -- 4.4 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 -- 5.4.2 SAXS Studies of Insulin, Glucagon, and Ü-Synuclein -- 5.4.3 SDS-Induced Aggregation of Ü-Synuclein -- 5.4.4 Multi-Component Fitting and Analysis of SAXS Data -- 5.5 General Strategies for Modeling SAXS Data from Protein Complexes -- 5.6 Summary and Final Remarks -- Acknowledgments -- References -- 6 Structural and Compositional Information about Pre-Amyloid Oligomers -- 6.1 General Introduction -- 6.2 Biophysical Techniques to Study Amyloid Oligomers -- 6.2.1 Fluorescence Spectroscopy -- 6.2.1.1 Ensemble Spectroscopy -- 6.2.1.2 Single-Molecule Spectroscopy -- 6.2.2 Atomic Force Microscopy -- 6.2.3 Absorbance and Circular Dichroism Spectroscopy -- 6.2.4 Small-Angle X-Ray Scattering -- 6.2.5 Mass Spectrometry -- 6.3 The Structure and Composition of Amyloid Oligomers -- 6.3.1 Ü-Synuclein Oligomers. | |
| 505 | 8 | |a 6.3.1.1 Morphology -- 6.3.1.2 Oligomer Structure -- 6.3.1.3 Oligomer Composition -- 6.3.2 AÝ Peptide Oligomers -- 6.3.2.1 Morphology -- 6.3.2.2 Composition -- 6.4 Concluding Remarks -- Acknowledgments -- References -- 7 The Oligomer Species: Mechanistics and Biochemistry -- 7.1 Introduction -- 7.2 The Structure-Toxicity Relation of Early Amyloids -- 7.2.1 Antibodies Define Different Structural Classes of Oligomers and Fibrils -- 7.2.2 Proteins May Form Different Kinds of Oligomers with Different Structural and Biological Activities -- 7.3 The Oligomer-Membrane Complex -- 7.3.1 The Effect of Surfaces on Protein Misfolding and Aggregation -- 7.3.2 The Membrane Composition Affects Binding and Aggregation Processes -- 7.3.3 Complex Roles of Cholesterol and Gangliosides in Oligomer Cytotoxicity -- 7.4 Biochemical Modifications Underlying Amyloid Toxicity -- 7.4.1 A New View of the Amyloid Cascade Hypothesis -- 7.4.2 Amyloid Pores: a Mechanism for Cytotoxicity? -- 7.4.3 Other Mechanisms for Oligomer Cytotoxicity -- 7.4.3.1 Oxidative Stress and Amyloid Aggregates -- 7.4.3.2 Lipid Modification and Ca2+ Entry -- 7.4.3.3 The Complexity of Amyloid and Oligomer Polymorphism -- 7.5 Summary -- References -- 8 Pathways of Amyloid Formation -- 8.1 Introduction -- 8.2 Nomenclature of the Various Conformational States -- 8.3 Graphical Representations of the Mechanisms Leading to Amyloid -- 8.3.1 Time Course of Amyloid Content -- 8.3.2 Energy Landscapes of Amyloid Fibril Formation -- 8.3.3 Reaction Equilibria Involved in Amyloid Fibril Formation -- 8.4 Pathways of Amyloid Fibril Formation -- 8.5 Nucleation Growth versus Nucleated Conformational Conversion -- 8.6 Summary -- References -- 9 Sequence-Based Prediction of Protein Behavior -- 9.1 Introduction -- 9.2 The Strategy of the Zyggregator Predictions. | |
| 505 | 8 | |a 9.2.1 Prediction of the Effects of Amino Acid Substitutions on Protein Aggregation Rates -- 9.2.2 Prediction of the Overall Aggregation Rates of Peptides and Proteins -- 9.2.3 Prediction of Aggregation-Prone Regions in Amino Acid Sequences -- 9.3 Aggregation Under Other Conditions -- 9.3.1 Prediction of Protein Aggregation-Prone Regions in the Presence of Denaturants -- 9.3.2 Prediction of Aggregation-Prone Regions in Native States of Proteins -- 9.4 Prediction of the Cellular Toxicity of Protein Aggregates -- 9.5 Relationship to Other Methods of Predicting Protein Aggregation Propensities -- 9.6 Competition between Folding and Aggregation of Proteins -- 9.7 Prediction of Protein Solubility from the Competition between Folding and Aggregation -- 9.7.1 Sequence-Based Prediction of Protein Solubility -- 9.7.2 Prediction of the Solubility of Proteins Based on Their Cellular Abundance -- 9.8 Sequence-Based Prediction of Protein Interactions with Molecular Chaperones -- 9.9 Summary -- References -- 10 The Kinetics and Mechanisms of Amyloid Formation -- 10.1 Introduction -- 10.2 Classical Theory of Nucleated Polymerization -- 10.2.1 From Microscopic Processes to a Master Equation -- 10.2.2 Kinetic Equations for Experimental Observables -- 10.2.3 Characteristics of Oosawa-Type Growth -- 10.2.3.1 Nucleation and Growth Occur Simultaneously -- 10.2.3.2 The Early Stages of the Reaction Time Course Are Described by Polynomial Growth -- 10.2.3.3 The Late Stages of the Reaction Time Course are Described by Simple First-Order Kinetics -- 10.2.3.4 The Integrated Rate Laws Exhibit Scaling Behavior -- 10.2.4 Global Analysis of Experimental Data Using the Oosawa Theory -- 10.3 The Theory of Filamentous Growth with Secondary Pathways -- 10.3.1 Extending the Oosawa Framework to Include Fragmentation and Secondary Nucleation -- 10.3.2 Early Time Perturbative Solutions. | |
| 505 | 8 | |a 10.3.3 Characteristics of Exponential-Type Growth -- 10.3.3.1 The Early Stages of the Reaction Time Course Are Exponential -- 10.3.3.2 The Solution Exhibits Scaling Behavior -- 10.3.4 Global Analysis of Experimental Data Using Linearized Solutions -- 10.4 Self-Consistent Solutions for the Complete Reaction Time Course -- 10.4.1 The Key Phenomenological Parameters Depend on Combinations of the Microscopic Rate Constants -- 10.4.2 Reaction Time Course with Depleted Monomer Concentration -- 10.4.3 Global Analysis of Amyloid Reaction Kinetics Using Self-Consistent Solutions -- 10.5 Summary -- References -- 11 Fluorescence Spectroscopy as a Tool to Characterize Amyloid Oligomers and Fibrils -- 11.1 Introduction -- 11.2 Fluorescence Spectroscopy for Studies of Amyloid Reactions In vitro -- 11.2.1 Fluorescence Output Formats -- 11.2.2 Fluorescence Anisotropy -- 11.2.3 Single Molecule Detection -- 11.2.4 Conformational Probes -- 11.3 Cysteine-Reactive Fluorescent Probes -- 11.3.1 Environmentally Sensitive Probes -- Spectrochromic Stokes Shift Assay -- 11.3.2 Fluorescence Anisotropy Probes for Amyloid Oligomerization -- 11.3.3 Pyrene Excimer Formation Probes for amyloid Oligomer and Fibril Topology -- 11.3.4 Bifunctional Cysteine Reagents as Probes for Amyloid Oligomers and Fibrils -- 11.4 Amyloidotropic Probes for Amyloid Fibrils and Oligomeric States -- 11.4.1 Are There Selective Probes for Prefibrillar Oligomeric States? -- 11.4.2 Fluorescence Anisotropy of Small Molecule Probes for Capturing the Intermediate Oligomeric State -- 11.4.3 In vivo Fluorescent Probes for Amyloid Fibrils -- 11.5 Luminescent Conjugated Poly and Oligothiophenes LCPs and LCOs -- 11.5.1 Optical Properties of Chemically Defined LCOs -- 11.5.2 Bridging the Imaging and Spectroscopy Gap -- Microspectroscopy of In vivo Formed Amyloids. | |
| 546 | |a English. | ||
| 590 | |a ProQuest Ebook Central |b Ebook Central Academic Complete | ||
| 650 | 0 | |a Amyloid. | |
| 650 | 1 | 2 | |a Amyloid |x chemistry |
| 650 | 1 | 2 | |a Amyloid |x pharmacokinetics |
| 650 | 2 | |a Amyloid | |
| 650 | 6 | |a Amyloïde. | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Amyloid |2 fast | |
| 650 | 7 | |a Bioquímica. |2 lemac | |
| 655 | 4 | |a Llibres electrònics. | |
| 700 | 1 | |a Otzen, Daniel Erik, |d 1969- |1 https://id.oclc.org/worldcat/entity/E39PCjvmw9rmgGQ39FcbPVmq8K | |
| 758 | |i has work: |a Amyloid fibrils and prefibrillar aggregates (Text) |1 https://id.oclc.org/worldcat/entity/E39PCFKWW3htJKGCpbgRFWCKHP |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |t Amyloid fibrils and prefibrillar aggregates. |d Weinheim : Wiley-VCH, [2013] |z 9783527332007 |w (OCoLC)829054952 |
| 856 | 4 | 0 | |u https://ebookcentral.uam.elogim.com/lib/uam-ebooks/detail.action?docID=1205604 |z Texto completo |
| 880 | 8 | |6 505-00/(S |a 3 What Does Solid-State NMR Tell Us about Amyloid Structures3.1 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 Aβ peptides of Different Length; 3.3.2 Islet Amyloid Polypeptide (IAPP/Amylin): Parallel and Antiparallel Steric Zippers. | |
| 880 | 8 | |6 505-00/(S |a 3.3.3 α-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. | |
| 880 | 8 | |6 505-00/(S |a 4.3.2 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 α-Synuclein; 5.4.3SDS-Induced Aggregation of α-Synuclein. | |
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