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...
Gespeichert in:
| Weitere Verfasser: | |
|---|---|
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
New York, NY
Springer New York
2016
|
| Ausgabe: | 1st ed. 2016 |
| Schriftenreihe: | Methods in Molecular Biology
1345 |
| Schlagworte: | |
| Online-Zugang: | UBR01 TUM01 Volltext |
| Zusammenfassung: | 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 |
| Beschreibung: | 1 Online-Ressource (XIV, 314 p. 73 illus., 49 illus. in color) |
| ISBN: | 9781493929788 |
| DOI: | 10.1007/978-1-4939-2978-8 |
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| 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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| 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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| isbn | 9781493929788 |
| language | English |
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| physical | 1 Online-Ressource (XIV, 314 p. 73 illus., 49 illus. in color) |
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| spelling | Protein Amyloid Aggregation Methods and Protocols edited by David Eliezer 1st ed. 2016 New York, NY Springer New York 2016 1 Online-Ressource (XIV, 314 p. 73 illus., 49 illus. in color) txt rdacontent c rdamedia cr rdacarrier Methods in Molecular Biology 1345 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 Life Sciences Protein Science Life sciences Proteins Amyloidose (DE-588)4142314-8 gnd rswk-swf Proteine (DE-588)4076388-2 gnd rswk-swf Labortechnik (DE-588)4123602-6 gnd rswk-swf Aggregation (DE-588)4000728-5 gnd rswk-swf Amyloid (DE-588)4129431-2 gnd rswk-swf Aggregation (DE-588)4000728-5 s Proteine (DE-588)4076388-2 s Amyloid (DE-588)4129431-2 s Labortechnik (DE-588)4123602-6 s 1\p DE-604 Amyloidose (DE-588)4142314-8 s 2\p DE-604 Eliezer, David edt Erscheint auch als Druck-Ausgabe 9781493929771 https://doi.org/10.1007/978-1-4939-2978-8 Verlag URL des Erstveröffentlichers Volltext 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 2\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
| 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 |