The Carboxy-Terminal Domain of Hsc70 Provides Binding Sites for a Distinct Set of Chaperone Cofactors
The modulation of the chaperone activity of the heat shock cognate Hsc70 protein in mammalian cells involves cooperation with chaperone cofactors, such as Hsp40; BAG-1; the Hsc70-interacting protein, Hip; and the Hsc70-Hsp90-organizing protein, Hop. By employing the yeast two-hybrid system and in vi...
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| Published in: | Mol Cell Biol |
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| Main Authors: | , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
Taylor & Francis
1998
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC121432/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9528774/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.18.4.2023 |
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