ロード中...
The structure of a β(2)-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-NMR to determine the structure of an amyloid fibril formed in vitro from β(2)-microglobulin (β(2)m), the culprit...
保存先:
| 出版年: | Nat Commun |
|---|---|
| 主要な著者: | , , , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group UK
2018
|
| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6207761/ https://ncbi.nlm.nih.gov/pubmed/30375379 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-018-06761-6 |
| タグ: |
タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!
|