Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
Aggregation of eye lens proteins leads to cataracts, a major cause of blindness. Here the authors use solid state NMR to probe the structure of γD-crystallin eye lens proteins aggregates, which are found to retain a native-like conformation.
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms15137 |
| _version_ | 1818400507492827136 |
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| author | Jennifer C. Boatz Matthew J. Whitley Mingyue Li Angela M. Gronenborn Patrick C. A. van der Wel |
| author_facet | Jennifer C. Boatz Matthew J. Whitley Mingyue Li Angela M. Gronenborn Patrick C. A. van der Wel |
| author_sort | Jennifer C. Boatz |
| collection | DOAJ |
| description | Aggregation of eye lens proteins leads to cataracts, a major cause of blindness. Here the authors use solid state NMR to probe the structure of γD-crystallin eye lens proteins aggregates, which are found to retain a native-like conformation. |
| first_indexed | 2024-12-14T07:37:40Z |
| format | Article |
| id | doaj.art-194e190adbbb4cf7b1a9b3aaf854fa91 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T07:37:40Z |
| publishDate | 2017-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-194e190adbbb4cf7b1a9b3aaf854fa912022-12-21T23:11:08ZengNature PortfolioNature Communications2041-17232017-05-018111010.1038/ncomms15137Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pHJennifer C. Boatz0Matthew J. Whitley1Mingyue Li2Angela M. Gronenborn3Patrick C. A. van der Wel4Department of Structural Biology, University of Pittsburgh School of MedicineDepartment of Structural Biology, University of Pittsburgh School of MedicineDepartment of Structural Biology, University of Pittsburgh School of MedicineDepartment of Structural Biology, University of Pittsburgh School of MedicineDepartment of Structural Biology, University of Pittsburgh School of MedicineAggregation of eye lens proteins leads to cataracts, a major cause of blindness. Here the authors use solid state NMR to probe the structure of γD-crystallin eye lens proteins aggregates, which are found to retain a native-like conformation.https://doi.org/10.1038/ncomms15137 |
| spellingShingle | Jennifer C. Boatz Matthew J. Whitley Mingyue Li Angela M. Gronenborn Patrick C. A. van der Wel Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH Nature Communications |
| title | Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH |
| title_full | Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH |
| title_fullStr | Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH |
| title_full_unstemmed | Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH |
| title_short | Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH |
| title_sort | cataract associated p23t γd crystallin retains a native like fold in amorphous looking aggregates formed at physiological ph |
| url | https://doi.org/10.1038/ncomms15137 |
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