𝔖 Scriptorium
✦   LIBER   ✦

πŸ“

Amyloid Proteins: Methods and Protocols

✍ Scribed by Adam P. Gunn, Blaine R. Roberts, Ashley I. Bush (auth.), Einar M. Sigurdsson, Miguel Calero, María Gasset (eds.)


Publisher
Humana Press
Year
2012
Tongue
English
Leaves
541
Series
Methods in Molecular Biology 849
Edition
2
Category
Library

⬇  Acquire This Volume

No coin nor oath required. For personal study only.

✦ Synopsis


Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word β€œamyloid” 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.

✦ 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

✦ Subjects


Protein Science


πŸ“œ SIMILAR VOLUMES


Amyloid Proteins: Methods and Protocols
✍ Gal Bitan, David B. Teplow (auth.), Einar M. Sigurdsson (eds.) πŸ“‚ Library πŸ“… 2005 πŸ› Humana Press 🌐 English

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 Proteins: Methods and Protocols
✍ Einar M. Sigurdsson, Miguel Calero, MarΓ­a Gasset πŸ“‚ Library πŸ“… 2012 πŸ› Humana Press 🌐 English

Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word β€œamyloid” 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 Proteins: Methods and Protocols
✍ Einar M. Sigurdsson, Miguel Calero, MarΓ­a Gasset πŸ“‚ Library πŸ“… 2012 πŸ› Humana Press 🌐 English

Amyloid diseases are characterized by the deposition of insoluble fibrous amyloid proteins. The word β€œamyloid” 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

Protein Amyloid Aggregation: Methods and
✍ David Eliezer πŸ“‚ Library πŸ“… 2015 πŸ› Humana Press 🌐 English

<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

Protein Amyloid Aggregation: Methods and
✍ David Eliezer (eds.) πŸ“‚ Library πŸ“… 2016 πŸ› Humana Press 🌐 English

<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