Protein Amyloid Aggregation Methods and Protocols
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 techniqu...
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Format: | Elektronisch E-Book |
Sprache: | English |
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New York, NY
Springer New York
2016
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Ausgabe: | 1st ed. 2016 |
Schriftenreihe: | Methods in Molecular Biology
1345 |
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MARC
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490 | 0 | |a Methods in Molecular Biology |v 1345 | |
520 | |a 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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Datensatz im Suchindex
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DE-BY-TUM_local_url | Verlag https://doi.org/10.1007/978-1-4939-2978-8 |
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author2 | Eliezer, David |
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building | Verbundindex |
bvnumber | BV044950663 |
collection | ZDB-2-PRO |
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dewey-full | 572.6 |
dewey-hundreds | 500 - Natural sciences and mathematics |
dewey-ones | 572 - Biochemistry |
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discipline | Biologie |
doi_str_mv | 10.1007/978-1-4939-2978-8 |
edition | 1st ed. 2016 |
format | Electronic eBook |
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id | DE-604.BV044950663 |
illustrated | Not Illustrated |
indexdate | 2024-11-25T18:02:39Z |
institution | BVB |
isbn | 9781493929788 |
language | English |
oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-030343423 |
oclc_num | 941405057 |
open_access_boolean | |
owner | DE-355 DE-BY-UBR DE-91 DE-BY-TUM |
owner_facet | DE-355 DE-BY-UBR DE-91 DE-BY-TUM |
physical | 1 Online-Ressource (XIV, 314 p. 73 illus., 49 illus. in color) |
psigel | ZDB-2-PRO |
publishDate | 2016 |
publishDateSearch | 2016 |
publishDateSort | 2016 |
publisher | Springer New York |
record_format | marc |
series2 | Methods in Molecular Biology |
spellingShingle | Protein Amyloid Aggregation Methods and Protocols Life Sciences Protein Science Life sciences Proteins Amyloidose (DE-588)4142314-8 gnd Proteine (DE-588)4076388-2 gnd Labortechnik (DE-588)4123602-6 gnd Aggregation (DE-588)4000728-5 gnd Amyloid (DE-588)4129431-2 gnd |
subject_GND | (DE-588)4142314-8 (DE-588)4076388-2 (DE-588)4123602-6 (DE-588)4000728-5 (DE-588)4129431-2 |
title | Protein Amyloid Aggregation Methods and Protocols |
title_auth | Protein Amyloid Aggregation Methods and Protocols |
title_exact_search | Protein Amyloid Aggregation Methods and Protocols |
title_full | Protein Amyloid Aggregation Methods and Protocols edited by David Eliezer |
title_fullStr | Protein Amyloid Aggregation Methods and Protocols edited by David Eliezer |
title_full_unstemmed | Protein Amyloid Aggregation Methods and Protocols edited by David Eliezer |
title_short | Protein Amyloid Aggregation |
title_sort | protein amyloid aggregation methods and protocols |
title_sub | Methods and Protocols |
topic | Life Sciences Protein Science Life sciences Proteins Amyloidose (DE-588)4142314-8 gnd Proteine (DE-588)4076388-2 gnd Labortechnik (DE-588)4123602-6 gnd Aggregation (DE-588)4000728-5 gnd Amyloid (DE-588)4129431-2 gnd |
topic_facet | Life Sciences Protein Science Life sciences Proteins Amyloidose Proteine Labortechnik Aggregation Amyloid |
url | https://doi.org/10.1007/978-1-4939-2978-8 |
work_keys_str_mv | AT eliezerdavid proteinamyloidaggregationmethodsandprotocols |