Amyloid Proteins: Methods and Protocols
β Scribed by Adam P. Gunn, Blaine R. Roberts, Ashley I. Bush (auth.), Einar M. Sigurdsson, Miguel Calero, MarΓa Gasset (eds.)
- Publisher
- Humana Press
- Year
- 2012
- Tongue
- English
- Leaves
- 541
- Series
- Methods in Molecular Biology 849
- Edition
- 2
- Category
- Library
No coin nor oath required. For personal study only.
β¦ Synopsis
Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word βamyloidβ 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 analyticalmethods for studying these proteins, cell culture models andassays for production of amyloid proteins, and protocols foramyloid extraction from tissue, its detection in vitro and in vivo, as well asnontransgenic methods for developing amyloid mouse models. Written in the highly successful Methods in Molecular Biologyβ’ 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.
β¦ Table of Contents
Front Matter....Pages i-xv
Front Matter....Pages 1-1
Front Matter....Pages 3-10
Front Matter....Pages 11-21
Front Matter....Pages 23-31
Back Matter....Pages 33-52
....Pages 53-68
β¦ Subjects
Protein Science
π SIMILAR VOLUMES
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 v
Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word βamyloidβ indicates a starch-like compound, and though a misnomer, continues to be the accepted term for this group of protein conformational disorders. The second editionΒ of Amyloid Proteins expand
Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word βamyloidβ indicates a starch-like compound, and though a misnomer, continues to be the accepted term for this group of protein conformational disorders. The second editionΒ of Amyloid Proteins expand
<p>This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techn
<p><p>This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes te