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Chaperone-client interactions: Non-specificity engenders multifunctionality
| Content Provider | Scilit |
|---|---|
| Author | Koldewey, Philipp Horowitz, Scott Bardwell, James C. A. |
| Copyright Year | 2017 |
| Description | Journal: Journal of Biological Chemistry Here, we provide an overview of the different mechanisms whereby three different chaperones, Spy, Hsp70, and Hsp60, interact with folding proteins, and we discuss how these chaperones may guide the folding process. Available evidence suggests that even a single chaperone can use many mechanisms to aid in protein folding, most likely due to the need for most chaperones to bind clients promiscuously. Chaperone mechanism may be better understood by always considering it in the context of the client's folding pathway and biological function. |
| Related Links | http://www.jbc.org/content/292/29/12010.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5519353/pdf http://www.jbc.org/article/S0021925820429734/pdf |
| Ending Page | 12017 |
| Page Count | 8 |
| Starting Page | 12010 |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| DOI | 10.1074/jbc.r117.796862 |
| Journal | Journal of Biological Chemistry |
| Issue Number | 29 |
| Volume Number | 292 |
| Language | English |
| Publisher | Elsevier BV |
| Publisher Date | 2017-07-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Chemistry Biochemistry and Molecular Biology 70-kilodalton Heat Shock Protein (hsp70) Molecular Chaperone Protein-protein Interaction |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
