Amyloid Proteins
Humana Press Inc. (Verlag)
978-1-61779-550-3 (ISBN)
Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word “amyloid” indicates a starch-like compound, and though a misnomer, continues to be the accepted term for this group of protein conformational disorders. The second edition of Amyloid Proteins expands upon the previous edition with current, detailed protocols for the preparation of amyloid and its precursors, specific analytical methods for studying these proteins, cell culture models and assays for production of amyloid proteins, and protocols for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.
Authoritative and practical, Amyloid Proteins, Second Edition seeks to aid scientists in the amyloid field to establish new techniques in their laboratories.
Authoritative and practical, Amyloid Proteins, Second Edition seeks to aid scientists in the amyloid field to establish new techniques in their laboratories.
Rapid Generation of Dityrosine Cross-linked Aβ Oligomers via Cu-redox Cycling.-Application of Photochemical Cross-linking to the Study of Oligomerization of Amyloidogenic Proteins.-PREPARATION OF STABLE AMYLOID β-PROTEIN OLIGOMERS OF DEFINED ASSEMBLY ORDER.-Purification and Fibrillation of full-Length Recombinant PrP.-Featuring Amyloids with Fourier Transform Infrared and Circular Dichroism Spectroscopies .-Quasielastic Light Scattering Study of Amyloid b -Protein Fibrillogenesis.-Conformations of Microtubule-Associated Protein Tau Mapped by Fluorescence Resonance Energy Transfer (FRET).-Measuring the Kinetics of Amyloid Fibril Elongation using Quartz Crystal Microbalances (QCM).-X-ray Fibre Diffraction Studies of Amyloid Fibrils.-Structural Characterization of Pre-fibrillar Intermediates and Amyloid Fibrils by Small-angle X-ray Scattering.-Atomic Force Fluorescence Microscopy in the Characterization of Amyloid Fibril Assembly and Oligomeric Intermediates.Investigating Fibrillar Aggregates of Tau Protein by Atomic Force Microscopy.-Structural Studies of Amyloids by Quenched Hydrogen-Deuterium Exchange by NMR.-Cyclic Amplification of Prion Protein Misfolding .-Search for Amyloid Binding Proteins by Affinity Chromatography.-Using Biophysical Approaches for Establishing the Links Between Aβ Aggregation and Cytotoxicity in Vitro.-Preparation of Cultured Human Vascular Cells.-Murine Cerebrovascular Cells as a Cell Culture Model for Cerebral Amyloid Angiopathy: Isolation of Smooth Muscle and Endothelial Cells from Mouse Brain.-IN VITROASSAYS MEASURING PROTECTION BY PROTEINS SUCH AS CYSTATIN C OF PRIMARY CORTICAL NEURONAL AND SMOOTH MUSCLE CELLS.-Study of Neurotoxic Intracellular Calcium Signalling Triggered by Amyloids.-Bacterial Amyloids.-Study of Amyloids using Yeast.-Cell-to-cell Transmission of a-synuclein Aggregate.-Subcutaneous Adipose Tissue Biopsy for Amyloid Protein Studies.-Analysis of S100 Oligomers and Amyloids.-S100A8/A9 Amyloidosis in the Ageing Prostate: Relating ex vivo and in vitro Studies.-Isolation of Amyloid by Solubilization in Water.-Histological Staining of Amyloid and Pre-Amyloid Peptides and Proteins in Mouse Tissue.-A Pentameric Luminescent Conjugated Oligothiophene for Optical Imaging of in vitro Formed Amyloid Fibrils and Protein Aggregates in Tissue Sections.-In Vivo Magnetic Resonance Imaging of Amyloid-β Plaques in Mice.-The Mouse Model for Scrapie: Inoculation, Clinical Scoring and Histopathological Techniques.-Biochemical Isolation of Insoluble Tau in Transgenic Mouse Models of Tauopathies.-Tissue Processing Prior to Analysis of Alzheimer’s Disease Associated Proteins and Metabolites, Including Ab.-Ab Measurement by Enzyme-linked Immunosorbent Assay (ELISA).-Cognitive and Sensorimotor Tasks for Assessing Functional Impairments in Mouse Models of Alzheimer’s Disease and Related Disorders.
| Reihe/Serie | Methods in Molecular Biology ; 849 |
|---|---|
| Zusatzinfo | 46 Illustrations, color; 69 Illustrations, black and white; XV, 548 p. 115 illus., 46 illus. in color. |
| Verlagsort | Totowa, NJ |
| Sprache | englisch |
| Maße | 178 x 254 mm |
| Themenwelt | Naturwissenschaften ► Biologie ► Biochemie |
| Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie | |
| Schlagworte | aggregates • Amyloid • Cell Culture Models • Diseases • in vitro • In vivo • nontransgenic methods • pathogenesis • protein polymers • transgenic technology |
| ISBN-10 | 1-61779-550-X / 161779550X |
| ISBN-13 | 978-1-61779-550-3 / 9781617795503 |
| Zustand | Neuware |
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