| 書目名稱 | Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases | | 編輯 | Farid Rahimi,Gal Bitan | | 視頻video | http://file.papertrans.cn/668/667106/667106.mp4 | | 概述 | An up-to-date review of protein-misfolding diseases which will serve as a complete reference point for readers.Up-to-date chapters that discuss different diseases associated with protein misfolding an | | 圖書封面 |  | | 描述 | Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates. The non-fibrillar protein assemblies range from small, low-order oligomers to spherical, annular, and protofibrillar species. Oligomeric species are believed to mediate various pathogenic mechanisms that lead to cellular dysfunction, cytotoxicity, and cell loss, eventuating in disease-specific degeneration and systemic morbidity. The particular pathologies thus are determined by the afflicted cell types, organs, systems, and the proteins involved. Evidence suggests that the oligomeric species may share structural features and possibly common mechanisms of action. In many cases, the structure–function interrelationships amongst the various protein assemblies | | 出版日期 | Book 2012 | | 關(guān)鍵詞 | Amyloidogenic proteins; Degenerative/neurodegenerative diseases; Mechanisms of disease; Non-fibrillar o | | 版次 | 1 | | doi | https://doi.org/10.1007/978-94-007-2774-8 | | isbn_softcover | 978-94-007-9895-3 | | isbn_ebook | 978-94-007-2774-8 | | copyright | Springer Science+Business Media B.V. 2012 |
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