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An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.
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- Nature Communications, 2017, v. 8, n. 5, p. 15328, doi. 10.1038/ncomms15328
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- Article
Combined HSP90 and kinase inhibitor therapy: Insights from The Cancer Genome Atlas.
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- Cell Stress & Chaperones, 2015, v. 20, n. 5, p. 729, doi. 10.1007/s12192-015-0604-1
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- Article
Chaperoning the Chaperone: A Role for the Co-chaperone Cpr7 in Modulating Hsp90 Function in Saccharomyces cerevisiae.
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- Genetics, 2012, v. 191, n. 3, p. 805, doi. 10.1534/genetics.112.140319
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- Article
Analysis of the health economics portfolio funded by the National Institutes of Health in response to published guidance.
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- PLoS ONE, 2024, v. 19, n. 2, p. 1, doi. 10.1371/journal.pone.0284235
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- Article
Hsp90 and co-chaperones twist the functions of diverse client proteins.
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- Biopolymers, 2010, v. 93, n. 3, p. 211, doi. 10.1002/bip.21292
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- Article
Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands.
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- Chemistry - A European Journal, 2015, v. 21, n. 39, p. 13598, doi. 10.1002/chem.201502211
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- Article
Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.
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- Current Genetics, 2014, v. 60, n. 4, p. 265, doi. 10.1007/s00294-014-0432-3
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- Article
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1.
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- Nature Communications, 2019, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41467-019-10463-y
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- Article