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An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin
Considerable mechanistic insight has been gained into amyloid aggregation; however, a large number of non-amyloid protein aggregates are considered “amorphous,” and in most cases, little is known about their mechanisms. Amorphous aggregation of γ-crystallins in the eye lens causes cataract, a widesp...
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| I publikationen: | J Biol Chem |
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| Huvudupphovsmän: | , , , , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
American Society for Biochemistry and Molecular Biology
2016
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5009285/ https://ncbi.nlm.nih.gov/pubmed/27417136 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M116.735977 |
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