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- W2150595189 endingPage "498" @default.
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- W2150595189 abstract "Hop is a tetratricopeptide repeat domain (TPR)-containing co-chaperone that is able to directly associate with both Hsp70 and Hsp90. Previous data showed that the TPR2A-domain is the primary site for dimerization and that the TPR2B-domain may also play a role in dimerization. We present Hop-D456G, a mutant within the TPR2B-domain, that is a mixture of monomeric and dimeric species. Keywords: Heat shock protein, Hop, TPR domain, Protein folding, protein-protein interaction, Hsp90" @default.
- W2150595189 created "2016-06-24" @default.
- W2150595189 creator A5008587231 @default.
- W2150595189 creator A5012791886 @default.
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- W2150595189 date "2010-05-01" @default.
- W2150595189 modified "2023-10-01" @default.
- W2150595189 title "Human Hsp70/Hsp90 Organizing Protein (Hop) D456G Is a Mixture of Monomeric and Dimeric Species" @default.
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- W2150595189 doi "https://doi.org/10.2174/092986610790963708" @default.
- W2150595189 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19961430" @default.
- W2150595189 hasPublicationYear "2010" @default.
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