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A switch point in the molecular chaperone Hsp90 responding to client interaction
Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switc...
Autores principales: | Rutz, Daniel Andreas, Luo, Qi, Freiburger, Lee, Madl, Tobias, Kaila, Ville R. I., Sattler, Michael, Buchner, Johannes |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5902578/ https://www.ncbi.nlm.nih.gov/pubmed/29662162 http://dx.doi.org/10.1038/s41467-018-03946-x |
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