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Franziska Tippel

Showing results (1-10 of 9) with videos related to

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EMBO Reports|December 16, 2014
Hop/Sti1 phosphorylation inhibits its co-chaperone functionAlina Röhl, Franziska Tippel, Evelyn Bender, et al.
Iscience|December 28, 2020
High-throughput determination of protein affinities using unmodified peptide libraries in nanomolar scaleClemens Schulte, Vladimir Khayenko, Noah Frieder Nordblom, et al.
Journal of Molecular Biology|September 25, 2016
Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90Alexandra Rehn, Elisabetta Moroni, Bettina K Zierer, et al.
Nature Structural & Molecular Biology|November 5, 2016
Importance of cycle timing for the function of the molecular chaperone Hsp90Bettina K Zierer, Martin Rübbelke, Franziska Tippel, et al.
Nature Communications|August 11, 2019
The Hsp90 isoforms from S. cerevisiae differ in structure, function and client rangeHannah Girstmair, Franziska Tippel, Abraham Lopez, et al.
Nature Communications|March 7, 2020
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90Alexandra Rehn, Jannis Lawatscheck, Marie-Lena Jokisch, et al.
Nature Communications|July 23, 2020
Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90Alexandra Rehn, Jannis Lawatscheck, Marie-Lena Jokisch, et al.
Nature Communications|April 9, 2015
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modulesAlina Röhl, Daniela Wengler, Tobias Madl, et al.
Scientific Reports|April 6, 2017
The Hsp90 machinery facilitates the transport of diphtheria toxin into human cellsManuel Schuster, Leonie Schnell, Peter Feigl, et al.
Pageof 1

Showing results (1-10 of 9) with videos related to

Sort By:
Pageof 1
EMBO Reports|December 16, 2014
Hop/Sti1 phosphorylation inhibits its co-chaperone functionAlina Röhl, Franziska Tippel, Evelyn Bender, et al.
Iscience|December 28, 2020
High-throughput determination of protein affinities using unmodified peptide libraries in nanomolar scaleClemens Schulte, Vladimir Khayenko, Noah Frieder Nordblom, et al.
Journal of Molecular Biology|September 25, 2016
Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90Alexandra Rehn, Elisabetta Moroni, Bettina K Zierer, et al.
Nature Structural & Molecular Biology|November 5, 2016
Importance of cycle timing for the function of the molecular chaperone Hsp90Bettina K Zierer, Martin Rübbelke, Franziska Tippel, et al.
Nature Communications|August 11, 2019
The Hsp90 isoforms from S. cerevisiae differ in structure, function and client rangeHannah Girstmair, Franziska Tippel, Abraham Lopez, et al.
Nature Communications|March 7, 2020
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90Alexandra Rehn, Jannis Lawatscheck, Marie-Lena Jokisch, et al.
Nature Communications|July 23, 2020
Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90Alexandra Rehn, Jannis Lawatscheck, Marie-Lena Jokisch, et al.
Nature Communications|April 9, 2015
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modulesAlina Röhl, Daniela Wengler, Tobias Madl, et al.
Scientific Reports|April 6, 2017
The Hsp90 machinery facilitates the transport of diphtheria toxin into human cellsManuel Schuster, Leonie Schnell, Peter Feigl, et al.
Pageof 1