Amyloid, Prions, and Other Protein Aggregates
Series: Methods in Enzymology; 309;
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Product details:
- Publisher Elsevier Science
- Date of Publication 22 September 1999
- ISBN 9780121822101
- Binding Hardback
- No. of pages820 pages
- Size 229x152 mm
- Weight 1280 g
- Language English 0
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Long description:
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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Characterization of In Vivo Protein Deposition:A. Identification and Isolation of Agreggates:G.T. Westermark, K.H. Johnson, and P. Westermark, Staining Methods for Identification of Amyloid in Tissue.G.A. Tennent, Isolation and Characterization of Amyloid Fibrils from Tissue.G. Georgiou and P. Valax, Isolating Inclusion Bodies from Bacteria.A.E. Roher and Y.-M. Kuo, Isolation of Amyloid Deposits from Brain.B. Isolation and Characterization of Protein Deposit Components:B. Kaplan, R. Hrncic, C.L. Murphy, G. Gallo, D.T. Weiss, and A. Solomon, Microtechniques and Purification Techniques Application to Chemical Characterization of Amyloid Proteins in Minute Amounts of Tissue.V.M.-Y. Lee, J. Wang, and J. Trojanowski, Purification of Paired Helical Filament Tau and Normal Tau from Human Brain Tissue.J.D. Lowenson, S. Clarke, and A.E. Roher, Chemical Modifications of Deposited Amyloid-b Proteins.C. Characterization of Aggregates In Situ and In Vitro:C. Korth, P. Streit, and B. Oesch, Monoclonal Antibodies Specific for Native, Disease-Associated Isoform of Prion Protein.B. Caughey, M. Horiuchi, R. Demaimay, and G. Raymond, Assays of Protease-Resistant Prion Protein and Its Formation.L.M. Sayre, G. Perry, and M.A. Smith, In Situ Methods for Detection and Localization of Markers of Oxidative Stress: Application in Neurodegenerative Disorders.Y. Al-Abed, A. Kapurniotu, and R. Bucala, Advanced Glycation End Products: Detection and Reversal.B.J. Balin, A.G. Loewy, and D.M. Appelt, Analysis of Transglutaminase-Catalyzed Isopeptide Bonds in Paired Helical Filaments and Neurofibrillary Tangles from Alzheimer's Disease.Characterization of In Vitro Protein Deposition:A. Managing the Aggregation Process:M.G. Zagorski, J. Yang, H. Shao, K. Ma, H. Zeng, and A. Hong, Methodological and Chemical Factors Affecting Amyloid-b Peptide Amyloidogenicity.J.Wall, C.L. Murphy, and A. Solomon, In Vitro Immunoglobulin Light Chain Fibrillogenesis.E. De Bernardez Clark, E. Schwartz, and R. Rudolph, Inhibition of Aggregation Side Reactions During In Vitro Protein Folding.J.F. Carpenter, B.S. Kendrick, B.S. Chang, M.C. Manning, and T.W. Randolph, Inhibition of Stress-Induced Aggregation of Protein Therapeutics.B. Aggregation Theory:F. Ferrone, Analysis of Protein Aggregation Kinetics.C. Monitoring Aggregate Growth by Dye Binding:H. LeVine, III, Quantification of b-Sheet Amyloid Fibril Structures with Thioflavin T.W.E. Klunk, R.F. Jacob, and R.P. Mason, Quantifying Amyloid by Congo Red Spectral Shift Assay.H. Naiki and F. Gejyo, Kinetic Analysis of Amyloid Fibril Formation.D. Measurement and Characterization of Assembly Intermediates:R. Raffen and F.J. Stevens, Small-Zone, High-Speed Gel Filtration Chromatography to Detect Protein Aggregation Associated with Light Chain Pathologies.S.D. Betts, M. Speed, and J. King, Detection of Early Aggregation Intermediates by Native Gel Electrophoresis and Native Western Blotting.E. Monitoring Aggregate Growth by Measuring Solid-Phase Accumulation:W.P. Esler, E.R. Stimson, P.W. Mantyh, and J.E. Maggio, Deposition of Soluble Amyloid-b onto Amyloid Templates: Identification of Amyloid Fibril Extension Inhibitors.E.E. Wanker, E. Scherzinger, V. Heiser, A. Sittler, H. Eickhof, and H. Lehrach, Membrane Filter Assay for Detection of Amyloid-like Polyglutamine-Containing Protein Aggregates.D.G. Myszka, S.J. Wood, and A.L. Biere, Analysis of Fibril Elongation Using Surface Plasmon Resonance Biosensors.V. Hlady, J. Buijs, and H.P. Jennissen, Methods for Studying Protein Adsorption.F. Monitoring Aggregate Growth and Structure Using Light Scattering:A. Lomakin, G.B. Benedek, and D.B. Teplow, Monitoring Protein Assembly Using Quasielastic Light Scattering Spectroscopy.J. Wall and A. Solomon, Flow Cytometric Characterization of Amyloid Fibrils.G. Aggregation Inhibitors:H. LeVine, III, and J.D. Scholten, Screening for Pharmacologic Inhibitors of Amyloid Fibril Formation.M.A. Findeis and S. Molineaux, Design and Testing of Inhibitors of Fibril Formation.Aggregate and Precursor Protein Structure:Aggregate Morphology:E.H. Nielsen, M. Nybo, and S.-E. Svehag, Electron Mircoscopy of Prefibrillar Structures and Amyloid Fibrils.S. Inoue and R. Kisilevsky, In Situ Electron Microscopy of Amyloid Deposits in Tissues.T.T. Ding and J.D. Harper, Analysis of Amyloid-b Assemblies Using Tapping Mode Atomic Force Microscopy Under Ambient Conditions.B. Molecular Level Aggregate Structure:L.C. Serpell, P.E. Fraser, and M. Sunde, X-Ray Diffraction of Amyloid Fibrils.D. Wemmer, Solid State NMR of Protein Deposits.S. Seshadri, R. Khurana, and A.L. Fink, FTIR in Analysis of Protein Deposits.M.A. Baldwin, Stable Isotope-Labeled Peptides in the Study of Protein Aggregation.E. Lundgren, K. Andersson, A. Olofsson, I. Dacklin, and G. Goldsteins, Mapping Protein Conformations in Fibril Structures Using Monoclonal Antibodies.C. Characterization of Precursor Protein Structure:W. Colï¿1⁄2n, Analysis of Protein Structure by Solution Optical Spectroscopy.E.J. Nettleton and C.V. Robinson, Probing Conformations of Amyloidogenic Proteins by Hydrogen Exchange and Mass Spectroscopy.Cellular and Organismic Consequences of Protein Deposition:A. Microbial Model Systems:T.R. Srio, A.G. Cashikar, J.J. Moslehi, A.S. Kowal, and S.L. Lindquist, Yeast Prion [X+] and its Determinant, Sup35p.B. Animal Models of Protein Deposition Diseases:K. Higuchi, M. Hosokawa, and T. Takeda, The Senescence-Accelerated Mouse.S.W. Davies, K. Sathasivam, C. Hobbs, P. Doherty, L. Mangiarini, E. Scherzinger, E.E. Wanker, and G.P. Bates, Detection of Polyglutamine Aggregation in Mouse Models.M.S. Kindy and F.C. De Beer, A Mouse Model for Serum Amyloid A Amyloidosis.C. Cell Studies on Protein Aggregate Cytotoxicity:M.S. Shearman, Toxicity of Protein Aggregates in PC12 Cells: 3-(4,5-Dimethylthiazol-2-yl)-2,5-Diphenyltetrazolium Bromide Assay.S.L. Yates, J. Kocsis-Angle, P. Embury, and K.R. Brunden, Inflammatory Repsonses to Amyloid Fibrils.M.P. Mattson, Impairment of Membrane Transport and Signal Transduction Systems by Amyloidogenic Proteins.D.A. Butterfield, S.M. Yatin, S. Varadarajan, and T. Koppal, Amyloid b-Peptide-Associated Free Radical Oxidative Stress, Neurotoxicity, and Alzheimer's Disease.
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