B. Zierer

发表

The Cochaperone SGTA (Small Glutamine-rich Tetratricopeptide Repeat-containing Protein Alpha) Demonstrates Regulatory Specificity for the Androgen, Glucocorticoid, and Progesterone Receptors*

J. Buchner, Z. Hildenbrand, Atanu Paul, 2014, The Journal of Biological Chemistry.

Cdc37 (Cell Division Cycle 37) Restricts Hsp90 (Heat Shock Protein 90) Motility by Interaction with N-terminal and Middle Domain Binding Sites*

J. Reinstein, D. Rutz, K. Richter, 2013, The Journal of Biological Chemistry.

Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90.

G. Colombo, E. Moroni, J. Buchner, 2016, Journal of molecular biology.

Post-translational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors

D. Bolon, L. Neckers, Tony Taldone, 2013, Oncotarget.

Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors.

D. Bolon, L. Neckers, Tony Taldone, 2013 .

Importance of cycle timing for the function of the molecular chaperone Hsp90

J. Buchner, T. Madl, M. Sattler, 2016, Nature Structural &Molecular Biology.

Modulation of the Hsp90 chaperone cycle by a stringent client protein.

J. Buchner, T. Madl, M. Sattler, 2014, Molecular cell.

Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions.

J. Buchner, M. Sattler, G. Fischer, 2014, Angewandte Chemie.

Elimination of a cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding.

R. Jakob, F. Schmid, H. Dobbek, 2010, Journal of molecular biology.

Modulation of the Hsp90 chaperone cycle by a stringent client protein.

J. Buchner, T. Madl, M. Sattler, 2014, Molecular cell.