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Alexandra Rehn
Alexandra Rehn
Technische Universität München
Hsp90
Chaperone (protein)
ATPase
Biology
Chemistry
6
Papers
138
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Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
2021
Nature Communications
Maximilian M. Biebl
Abraham Lopez
Alexandra Rehn
Lee Freiburger
Jannis Lawatscheck
Birgit Blank
Michael Sattler
Johannes Buchner
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Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.
2020
Nature Communications
Alexandra Rehn
Jannis Lawatscheck
Marie-Lena Jokisch
Sophie L. Mader
Qi Luo
Franziska Tippel
Birgit Blank
Klaus Richter
Kathrin Lang
Ville R. I. Kaila
Johannes Buchner
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A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
2020
Nature Communications
Alexandra Rehn
Jannis Lawatscheck
Marie-Lena Jokisch
Sophie L. Mader
Qi Luo
Franziska Tippel
Birgit Blank
Klaus Richter
Kathrin Lang
Ville R. I. Kaila
Johannes Buchner
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Citations (11)
Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90
2016
Journal of Molecular Biology
Alexandra Rehn
Elisabetta Moroni
Bettina K. Zierer
Franziska Tippel
Giulia Morra
Christine John
Klaus Richter
Giorgio Colombo
Johannes Buchner
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Citations (41)
p23 and Aha1
2015
Sub-cellular biochemistry
Alexandra Rehn
Johannes Buchner
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Citations (20)
1