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Hsp90-Mediated Folding of the Lymphoid Cell Kinase p56 lck

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Mutational analysis of Hsp90α dimerization and subcellular localization: dimer disruption does not impede ‘in vivo’ interaction with estrogen receptor

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Hsp90 chaperone complexes are required for the activity and stability of yeast protein kinases Mik1, Wee1 and Swe1

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The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast.

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The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo

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14-3-3 ζ Protein Binds to the Carboxyl Half of Mouse Wee1 Kinase

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Molecular chaperones and protein folding in plants

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A multicopy suppressor of a cell cycle defect in S. pombe encodes a heat shock‐inducible 40 kDa cyclophilin‐like protein.

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Hsp90 phosphorylation, Wee1 and the cell cycle

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Hsp90 chaperone complexes are required for the activity and stability of yeast protein kinases Mik1, Wee1 and Swe1

Goes, F. S., & Martin, J. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02105.x · Cited by 64 · see citing works

Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function

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Genetic interactions between Hsp90 and the Cdc2 mitotic machineryin the fission yeast Schizosaccharomyces pombe

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Summary

Mollapour, M., Tsutsumi, S., Donnelly, A. C., Beebe, K. E., Mari, J., Colombo, G., Blagg, B. S. J., Panaretou, B., Stetler, W. G., Trepel, J. B., et al. (2015)