Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

por Biebl, Maximilian M., Lopez, Abraham, Rehn, Alexandra, Freiburger, Lee, Lawatscheck, Jannis, Blank, Birgit, Sattler, Michael, Buchner, Johannes
Publicado 2021

Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins

por Jores, Tobias, Lawatscheck, Jannis, Beke, Viktor, Franz-Wachtel, Mirita, Yunoki, Kaori, Fitzgerald, Julia C., Macek, Boris, Endo, Toshiya, Kalbacher, Hubert, Buchner, Johannes, Rapaport, Doron
Publicado 2018

Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90

por Mader, Sophie L., Lopez, Abraham, Lawatscheck, Jannis, Luo, Qi, Rutz, Daniel A., Gamiz-Hernandez, Ana P., Sattler, Michael, Buchner, Johannes, Kaila, Ville R. I.
Publicado 2020

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

por Rehn, Alexandra, Lawatscheck, Jannis, Jokisch, Marie-Lena, Mader, Sophie L., Luo, Qi, Tippel, Franziska, Blank, Birgit, Richter, Klaus, Lang, Kathrin, Kaila, Ville R. I., Buchner, Johannes
Publicado 2020

Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

por Rehn, Alexandra, Lawatscheck, Jannis, Jokisch, Marie-Lena, Mader, Sophie L., Luo, Qi, Tippel, Franziska, Blank, Birgit, Richter, Klaus, Lang, Kathrin, Kaila, Ville R. I., Buchner, Johannes
Publicado 2020

The IMiD target CRBN determines HSP90 activity toward transmembrane proteins essential in multiple myeloma

por Heider, Michael, Eichner, Ruth, Stroh, Jacob, Morath, Volker, Kuisl, Anna, Zecha, Jana, Lawatscheck, Jannis, Baek, Kheewoong, Garz, Anne-Kathrin, Rudelius, Martina, Deuschle, Friedrich-Christian, Keller, Ulrich, Lemeer, Simone, Verbeek, Mareike, Götze, Katharina S., Skerra, Arne, Weber, Wolfgang A., Buchner, Johannes, Schulman, Brenda A., Kuster, Bernhard, Fernández-Sáiz, Vanesa, Bassermann, Florian
Publicado 2021