Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action
(2014)
Journal Article
Karagöz, G. E., Duarte, A. M., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., Dickey, C. A., Mandelkow, E., Zweckstetter, M., Boelens, R., Madl, T., & Rüdiger, S. G. (2014). Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action. Cell, 156(5), 963-974. https://doi.org/10.1016/j.cell.2014.01.037
Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly... Read More about Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action.