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/https://libri-media.knygos-static.lt/59613600-05f4-4a0c-9a9b-ff179239cfe5/1)
- Leidėjas: Elsevier Science
- Metai: 2026
- Puslapiai: 400
- ISBN-10: 0323956386
- ISBN-13: 9780323956383
- Formatas: 15.2 x 22.9 x cm, minkšti viršeliai
- Kalba: Anglų
Structural Biology of Amyloid Fibrils (el. knyga) (skaityta knyga) | knygos.lt
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Aprašymas
Structural Biology of Amyloid Fibrils provides a comprehensive reference on the structure of protein aggregates in different neurodegenerative diseases, along with their molecular bases. Chapters describe these structures in detail, highlighting their similarities and differences across different disease states along with an unprecedented overview of current developments and new hypotheses emerging in amyloid fibril structure, stability and mechanisms of formation. The book also discusses how amyloid structure may affect the ability of fibrils to spread to different sites in a prion-like manner, as well as their role in disease.
Featuring chapters on NMR, X-ray crystallography, and Cryo-EM methods, and discussing the structure of amyloid fibrils obtained directly from patients, the book allows readers to understand how polymorphism is associated with disease phenotype and how fibril structure affects and influences the cellular environment. Understanding the molecular architecture of amyloid fibrils and oligomers will be an important step towards developing therapeutic interventions based on targeting the fibrils and oligomers themselves and the processes that generate them.
- Leidėjas: Elsevier Science
- Metai: 2026
- Puslapiai: 400
- ISBN-10: 0323956386
- ISBN-13: 9780323956383
- Formatas: 15.2 x 22.9 x cm, minkšti viršeliai
- Kalba: Anglų
Structural Biology of Amyloid Fibrils provides a comprehensive reference on the structure of protein aggregates in different neurodegenerative diseases, along with their molecular bases. Chapters describe these structures in detail, highlighting their similarities and differences across different disease states along with an unprecedented overview of current developments and new hypotheses emerging in amyloid fibril structure, stability and mechanisms of formation. The book also discusses how amyloid structure may affect the ability of fibrils to spread to different sites in a prion-like manner, as well as their role in disease.
Featuring chapters on NMR, X-ray crystallography, and Cryo-EM methods, and discussing the structure of amyloid fibrils obtained directly from patients, the book allows readers to understand how polymorphism is associated with disease phenotype and how fibril structure affects and influences the cellular environment. Understanding the molecular architecture of amyloid fibrils and oligomers will be an important step towards developing therapeutic interventions based on targeting the fibrils and oligomers themselves and the processes that generate them.
Atsiliepimai