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Kategorie szczegółowe BISAC

Amyloid Proteins

ISBN-13: 9781617375026 / Angielski / Miękka / 2010 / 408 str.

Einar M. Sigurdsson
Amyloid Proteins Einar M. Sigurdsson 9781617375026 Springer - książkaWidoczna okładka, to zdjęcie poglądowe, a rzeczywista szata graficzna może różnić się od prezentowanej.

Amyloid Proteins

ISBN-13: 9781617375026 / Angielski / Miękka / 2010 / 408 str.

Einar M. Sigurdsson
cena 401,43
(netto: 382,31 VAT:  5%)

Najniższa cena z 30 dni: 385,37
Termin realizacji zamówienia:
ok. 22 dni roboczych
Dostawa w 2026 r.

Darmowa dostawa!

A proven collection of readily reproducible techniques for studying amyloid proteins and their involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular Biology(TM) series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.

Kategorie:
Nauka, Biologia i przyroda
Kategorie BISAC:
Medical > Nutrition
Medical > Biochemistry
Science > Biochemia
Wydawca:
Springer
Seria wydawnicza:
Methods in Molecular Biology (Paperback)
Język:
Angielski
ISBN-13:
9781617375026
Rok wydania:
2010
Numer serii:
000203440
Ilość stron:
408
Waga:
0.57 kg
Wymiary:
23.39 x 15.6 x 2.13
Oprawa:
Miękka
Wolumenów:
01

Part I. In Vitro Assays Preparation of Aggregate-Free, Low Molecular Weight Amyloid-b for Assembly and Toxicity Assays Gal Bitan and David B. Teplow Determination of Peptide Oligomerization State Using Rapid Photochemical Crosslinking Sabrina S. Vollers, David B. Teplow, and Gal Bitan In Vitro Preparation of Prefibrillar Intermediates of Amyloid-b and a-Synuclein Hilal A. Lashuel and Dolors Grillo-Bosch Purification of Recombinant Tau Protein and Preparation of Alzheimer-Paired Helical Filaments In Vitro Stefan Barghorn, Jacek Biernat, and Eckhard Mandelkow Cyclic Amplification of Protein Misfolding and Aggregation Paula Saá, Joaquín Castilla, and Claudio Soto X-Ray Diffraction Studies of Amyloid Structure O. Sumner Makin and Louise C. Serpell Molecular Electron Microscopy Approaches to Elucidating the Mechanisms of Protein Fibrillogenesis Hilal A. Lashuel and Joseph S. Wall Time-Lapse Atomic Force Microscopy in the Characterization of Amyloid-Like Fibril Assembly and Oligomeric Intermediates Claire Goldsbury and Janelle Green Fourier Transform Infrared and Circular Dichroism Spectroscopies for Amyloid Studies Miguel Calero and María Gasset Quasielastic Light Scattering for Protein Assembly Studies Aleksey Lomakin, David B. Teplow, and George B. Benedek Intrinsic Fluorescent Detection of Tau Conformation and Aggregation Martin von Bergen, Li Li, and Eckhard Mandelkow Quantitative Measurement of Fibrillogenesis by Mass Spectrometry Andrew D. Miranker Part II. Cell Culture Assays Isolation and Culturing of Human Vascular Smooth Muscle Cells Finnbogi R. Thormodsson and Ingvar H. Olafsson Murine Cerebrovascular Cells as a Cell Culture Model for Cerebral Amyloid Angiopathy: Isolation of Smooth Muscle and Endothelial Cells From MouseBrain Sonia S. Jung and Efrat Levy Purification of Human Wild-Type or Variant Cystatin C From Conditioned Media of Transfected Cells Frances Prelli, Monika Pawlik, Blas Frangione, and Efrat Levy Prion Propagation in Cell Culture Sylvain Lehmann Part III. In Vivo-Related Assays Preparation and Propagation of Amyloid-Enhancing Factor Robert Kisilevsky Purification of Amyloid Protein AA Subspecies From Amyloid-Rich Human Tissues Gunilla T. Westermark and Per Westermark Purification of Transthyretin and Transthyretin Fragments From Amyloid-Rich Human Tissues Per Westermark and Gunilla T. Westermark Extraction and Chemical Characterization of Tissue-Deposited Proteins From Minute Diagnostic Biopsy Specimens Fernando Goñi and Gloria Gallo Tissue Processing Prior to Protein Analysis and Amyloid-b Quantitation Stephen D. Schmidt, Ying Jiang, Ralph A. Nixon, and Paul M. Mathews ELISA Method for Measurement of Amyloid-b Levels Stephen D. Schmidt, Ralph A. Nixon, and Paul M. Mathews Histological Staining of Amyloid-b in Mouse Brains Einar M. Sigurdsson The Mouse Model for Scrapie: Inoculation, Clinical Scoring, and Histopathological Techniques Harry C. Meeker, Xuemin Ye, and Richard I. Carp Radiolabeling of Amyloid-b Peptides Miguel Calero and Jorge Ghiso In Vivo Imaging of Amyloid-b Deposits in Mouse Brain With Multiphoton Microscopy Jesse Skoch, Gregory A. Hickey, Stephen T. Kajdasz, Bradley T. Hyman, and Brian J. Bacskai Magnetic Resonance Imaging of Amyloid Plaques in Transgenic Mice Youssef Zaim Wadghiri, Einar M. Sigurdsson, Thomas Wisniewski, and Daniel H. Turnbull Index

In recent years, various in vitro and in vivo techniques, transgenic technologies, and novel animal models have been developed to understand amyloid diseases-such as Alzheimer's disease and some forms of diabetes-and to screen for drugs that can block amyloid formation and/or disassemble its associated fibrils. In Amyloid Proteins: Methods and Protocols, internationally known researchers describe in step-by-step detail their best techniques for studying these types of proteins and their involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide proven methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular Biology™ series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
Authoritative and highly practical, Amyloid Proteins: Methods and Protocols offers both skilled and novice investigators a proven collection of standard and novel techniques for studying amyloid proteins and peptides, as well as their relation to amyloid diseases.



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