Molecular chaperones in cellular protein folding Journal Article
| Author: | Hartl, F. U. |
| Article Title: | Molecular chaperones in cellular protein folding |
| Abstract: | The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains. |
| Keywords: | review; nonhuman; protein conformation; animals; protein protein interaction; cell protein; protein binding; protein transport; rna translation; heat shock protein 70; protein folding; adenosine triphosphatase; membrane transport; heat shock; hsp70 heat-shock proteins; chaperone; chaperonins; humans; priority journal; chaperonin |
| Journal Title: | Nature |
| Volume: | 381 |
| Issue: | 6583 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1996-06-13 |
| Start Page: | 571 |
| End Page: | 580 |
| Language: | English |
| DOI: | 10.1038/381571a0 |
| PUBMED: | 8637592 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Review -- Export Date: 22 November 2017 -- Source: Scopus |
