Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils
Abstract Many proteins self-assemble to form amyloid fibrils, which are highly organized structures stabilized by a characteristic cross-β network of hydrogen bonds. This process underlies a variety of human diseases and can be exploited to develop versatile functional biomaterials. Thus, protein se...
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| Hlavní autoři: | , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Portfolio
2024-02-01
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| Edice: | Communications Biology |
| On-line přístup: | https://doi.org/10.1038/s42003-024-05858-7 |
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