Article ; Online: Preserving protein function through reversible aggregation.
2017 Volume 19, Issue 10, Page(s) 1142–1144
Abstract: It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase ... ...
| Abstract | It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase triggers reversible aggregation to preserve protein function under stress. |
|---|---|
| Language | English |
| Publishing date | 2017-09-29 |
| Publishing country | England |
| Document type | Journal Article |
| ZDB-ID | 1474722-4 |
| ISSN | 1476-4679 ; 1465-7392 |
| ISSN (online) | 1476-4679 |
| ISSN | 1465-7392 |
| DOI | 10.1038/ncb3620 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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