Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.
Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, o...
| Main Authors: | , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1997
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| _version_ | 1797075926734864384 |
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| author | Booth, DR Sunde, M Bellotti, V Robinson, C Hutchinson, W Fraser, P Hawkins, P Dobson, C Radford, SE Blake, C Pepys, M |
| author_facet | Booth, DR Sunde, M Bellotti, V Robinson, C Hutchinson, W Fraser, P Hawkins, P Dobson, C Radford, SE Blake, C Pepys, M |
| author_sort | Booth, DR |
| collection | OXFORD |
| description | Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally. |
| first_indexed | 2024-03-06T23:57:06Z |
| format | Journal article |
| id | oxford-uuid:749cd3d2-a987-4109-b15b-88f8fead4e2c |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:57:06Z |
| publishDate | 1997 |
| record_format | dspace |
| spelling | oxford-uuid:749cd3d2-a987-4109-b15b-88f8fead4e2c2022-03-26T20:04:06ZInstability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:749cd3d2-a987-4109-b15b-88f8fead4e2cEnglishSymplectic Elements at Oxford1997Booth, DRSunde, MBellotti, VRobinson, CHutchinson, WFraser, PHawkins, PDobson, CRadford, SEBlake, CPepys, MTissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally. |
| spellingShingle | Booth, DR Sunde, M Bellotti, V Robinson, C Hutchinson, W Fraser, P Hawkins, P Dobson, C Radford, SE Blake, C Pepys, M Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. |
| title | Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. |
| title_full | Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. |
| title_fullStr | Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. |
| title_full_unstemmed | Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. |
| title_short | Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. |
| title_sort | instability unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis |
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