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Heat Shock Protein 90 Modulates the Unfolded Protein Response by Stabilizing IRE1α
The molecular chaperone HSP90 regulates stability and function of multiple protein kinases. The HSP90-binding drug geldanamycin interferes with this activity and promotes proteasome-dependent degradation of most HSP90 client proteins. Geldanamycin also binds to GRP94, the HSP90 paralog located in th...
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| Hlavní autoři: | , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology
2002
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC139892/ https://ncbi.nlm.nih.gov/pubmed/12446770 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/MCB.22.24.8506-8513.2002 |
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