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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:
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. Colón, 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.
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.
Biochemists, molecular biologists, biomedical researchers, cell biologists, developmental biologists, and neuroscientists.
- No. of pages:
- © Academic Press 1999
- 14th September 1999
- Academic Press
- Hardcover ISBN:
- eBook ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
University of Tennessee Medical Center, Knoxville, U.S.A.
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