Elsevier S & T

Amyloid, Prions, and Other Protein Aggregates

Abelson, John N.; Simon, Melvin I.

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Table of contents

Table of Contentsv
Contributors to Volume 309xi
Prefacexvii
Volumes in Seriesxxi
Section I: Characterization of in Vivo Protein Deposition1
A. Identification and Isolation of Aggregates1
Chapter 1. Staining Methods for Identification of Amyloid in Tissue3
Chapter 2. Isolation and Characterization of Amyloid Fibrils from Tissue26
Chapter 3. Isolating Inclusion Bodies from Bacteria48
Chapter 4. Isolation of Amyloid Deposits from Brain58
B. Isolation and Characterization of Protein Deposit Components1
Chapter 5. Microextraction and Purification Techniques Applicable to Chemical Characterization of Am67
Chapter 6. Purification of Paired Helical Filament Tau and Normal Tau from Human Brain Tissue81
Chapter 7. Chemical Modifications of Deposited Amyloid-B Peptides89
C. Characterization of Aggregates in Situ and in Vitro1
Chapter 8. Monoclonal Antibodies Specific for the Native, Disease-Associated Isoform of Prion Protei106
Chapter 9. Assays of Protease-Resistant Prion Protein and Its Formation122
Chapter 10. In Situ Methods for Detection and Localization of Markers of Oxidative Stress: Applicati133
Chapter 11. Advanced Glycation End Products: Detection and Reversal152
Chapter 12. Analysis of Transglutaminase-Catalyzed Isopeptide Bonds in Paired Helical Filaments and172
Section II: Characterization of in Vitro Protein Deposition187
A. Managing the Aggregation Process187
Chapter 13. Methodological and Chemical Factors Affecting Amyloid-B Peptide Amyloidogenicity189
Chapter 14. In Vitro Immunoglobulin Light Chain Fibrillo- genesis204
Chapter 15. Inhibition of Aggregation Side Reactions during in Vitro Protein Folding217
Chapter 16. Inhibition of Stress-Induced Aggregation of Protein Therapeutics236
B. Aggregation Theory187
Chapter 17. Analysis of Protein Aggregation Kinetics256
C. Monitoring Aggregate Growth by Dye Binding187
Chapter 18. Quantification of B-Sheet Amyloid Fibril Structures with Thioflavin T274
Chapter 19. Quantifying Amyloid by Congo Red Spectral Assay285
Chapter 20. Kinetic Analysis of Amyloid Fibril Formation305
D. Measurement and Characterization of Assembly Intermediates187
Chapter 21. Small-Zone, High-Speed Gel Filtration Chromatog- raphy to Detect Protein Aggregation Ass318
Chapter 22. Detection of Early Aggregation Intermediates by Native Gel Electrophoresis and Native We333
E. Monitoring Aggregate Growth by Measuring Solid-Phase Accumulation187
Chapter 23. Deposition of Soluble Amyloid-B onto Amyloid Templates: Identification of Amyloid Fibri350
Chapter 24. Membrane Filter Assay for Detection of Amyloid- like Polyglutamine-Containing Protein Ag375
Chapter 25. Analysis of Fibril Elongation Using Surface Plas- mon Resonance Biosensors386
Chapter 26. Methods for Studying Protein Adsorption402
F. Monitoring Aggregate Growth and Structure Using Light Scattering187
Chapter 27. Monitoring Protein Assembly Using Quasielastic Light Scattering Spectroscopy429
Chapter 28. Flow Cytometric Characterization of Amyloid Fibrils460
G. Aggregation Inhibitors187
Chapter 29. Screening for Pharmacologic Inhibitors of Amyloid Fibril Formation467
Chapter 30. Design and Testing of Inhibitors of Fibril Formation476
Section III: Aggregate and Precursor Protein Structure489
A. Aggregate Morphology489
Chapter 31. Electron Microscopy of Prefibrillar Structures and Amyloid Fibrils491
Chapter 32. In Situ Electron Microscopy of Amyloid Deposits in Tissues496
Chapter 33. Analysis of Amyloid- Assemblies Using Tapping Mode Atomic Force Microscopy under Ambien510
B. Molecular Level Aggregate Structure489
Chapter 34. X-Ray Fiber Diffraction of Amyloid Fibrils526
Chapter 35. Solid State Nuclear Magnetic Resonance of Protein Deposits536
Chapter 36. Fourier Transform Infrared Spectroscopy in Analysis of Protein Deposits559
Chapter 37. Stable Isotope-Labeled Peptides in Study of Protein Aggregation576
Chapter 38. Mapping Protein Conformations in Fibril Structures Using Monoclonal Antibodies591
C. Characterization of Precursor Protein Structure489
Chapter 39. Analysis of Protein Structure by Solution Optical Spectroscopy605
Chapter 40. Probing Conformations of Amyloidogenic Proteins by Hydrogen Exchange and Mass Spectrosco633
Section IV: Cellular and Organismic Consequences of Protein Deposition647
A. Microbial Model Systems647
Chapter 41. Yeast Prion [Y+ ] and Its Determinant, Sup35p649
B. Animal Models of Protein Deposition Diseases647
Chapter 42. The Senescence-Accelerated Mouse674
Chapter 43. Detection of Polyglutamine Aggregation in Mouse Models687
Chapter 44. A Mouse Model for Serum Amyloid A Amyloidosis701
C. Cell Studies on Protein Aggregate Cytotoxicity647
Chapter 45. Toxicity of Protein Aggregates in PC12 Cells: 3-(4,5-Dimethylthiazol-2-yl)-2,5- diphenyl716
Chapter 46. Inflammatory Responses to Amyloid Fibrils723
Chapter 47. Impairment of Membrane Transport and Signal Transduction Systems by Amyloidogenic Protei733
Chapter 48. Amyloid B-Peptide-Associated Free Radical Oxidative Stress, Neurotoxicity, and Alzheime746
Author Index769
Subject Index797

Book details

Vendor Elsevier S & T
SKU 9780121822101
ISBN-13 9780080496672
Author Abelson, John N.; Simon, Melvin I.
Category Medical
Subject Biochemistry

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This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates.
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.

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