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" Protein amyloid aggregation "
edited by David Eliezer, Weill Cornell Medical College, New York, NY, USA.
Document Type
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BL
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Record Number
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569128
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Doc. No
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b398347
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Title & Author
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Protein amyloid aggregation : methods and protocols /\ edited by David Eliezer, Weill Cornell Medical College, New York, NY, USA.
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Publication Statement
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New York :: Humana Press ;Springer,, [2015]
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Series Statement
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Methods in molecular biology,; volume 1345
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Springer protocols,
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ISBN
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9781493929771
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: 1493929771
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9781493929788
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Bibliographies/Indexes
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Includes bibliographical references and index.
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Abstract
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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 techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils, and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists, and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.
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Subject
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Life sciences, Laboratory manuals.
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Subject
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Proteins, Laboratory manuals.
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Subject
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Protein Aggregates.
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Subject
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Protein Aggregation, Pathological.
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Subject
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Amyloid.
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Added Entry
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Eliezer, David.
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