Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Johannes Hermann"'
Autor:
Johannes Hermann Kilz, Marie Angela Sidoti Abate, Victoria Luise Simone Wieland, Luisa Egen, Caelan Max Haney, Aleksander Antoniewicz, Alexander Studier-Fischer, Thomas Stefan Worst, Maurice Stephan Michel, Patrick Honeck, Niklas Westhoff, Maximilian Christian Kriegmair, Karl-Friedrich Kowalewski
Publikováno v:
European Urology Open Science, Vol 71, Iss , Pp 78-86 (2025)
Externí odkaz:
https://doaj.org/article/3fda932686d74255937f73d44251ffc9
Controlling Protein Crystallization by Free Energy Guided Design of Interactions at Crystal Contacts
Autor:
Johannes Hermann, Daniel Bischoff, Phillip Grob, Robert Janowski, Dariusch Hekmat, Dierk Niessing, Martin Zacharias, Dirk Weuster-Botz
Publikováno v:
Crystals, Vol 11, Iss 6, p 588 (2021)
Protein crystallization can function as an effective method for protein purification or formulation. Such an application requires a comprehensive understanding of the intermolecular protein–protein interactions that drive and stabilize protein crys
Externí odkaz:
https://doaj.org/article/a0918a409a384a0492b47a34f5408640
Autor:
Reich, Barbara, Schmidbauer, Kathrin, Rodriguez Gomez, Manuel, Johannes Hermann, Fabian, Göbel, Nicole, Brühl, Hilke, Ketelsen, Isabel, Talke, Yvonne, Mack, Matthias *
Publikováno v:
In Kidney International July 2013 84(1):78-89
Verschwörungsgläubigkeit ist ein zunehmend relevantes Thema im aktuellen gesellschaftlichen Diskurs mit gefährlichen Konsequenzen auf persönlicher und politischer Ebene, weshalb in der Wissenschaft viele Modelle zur Erklärung dieses Phänomens e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4193::9fdb3d74a5a7d8b75d1220712cf92aee
https://resolver.obvsg.at/urn:nbn:at:at-ubk:1-47017
https://resolver.obvsg.at/urn:nbn:at:at-ubk:1-47017
Autor:
Phillip Nowotny, Dariusch Hekmat, Angela Krautenbacher, Johannes Hermann, Dirk Weuster-Botz, Kai Klöpfer, Jianing Li
Publikováno v:
Crystal Growth & Design. 19:2380-2387
Technical protein crystallization is an alternative to preparative chromatography for purification of proteins. However, only a few proteins are satisfactorily crystallizable for this technical pur...
Controlling protein crystallization by free energy guided design of interactions at crystal contacts
Autor:
Dariusch Hekmat, Robert Janowski, Dierk Niessing, Johannes Hermann, Daniel Bischoff, Martin Zacharias, Dirk Weuster-Botz, Phillip Grob
Publikováno v:
Crystals 11:588 (2021)
Crystals
Volume 11
Issue 6
Crystals, Vol 11, Iss 588, p 588 (2021)
Crystals
Volume 11
Issue 6
Crystals, Vol 11, Iss 588, p 588 (2021)
Protein crystallization can function as an effective method for protein purification or formulation. Such an application requires a comprehensive understanding of the intermolecular protein–protein interactions that drive and stabilize protein crys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a71e5b213a598d886751420c8ccf612
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=62255
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=62255
Autor:
Philamer Calses, Sam Clark, Jacob Corpuz, Susan Fong, Phil Gerkin, Mohammad Hekmatnejad, Evan McMahon, Megan Murray, Truc Nguyen, Tony Phan, Allison Roberts, Phillip Schwartz, Mikayla Shanafelt, Hiroko Tanaka, Jennifer Tomczyk, John Widen, Monika Williams, John Eksterowicz, Daniel Erlanson, Marie Evangelista, Johannes Hermann, Richard M. Neve, Snahel Patel, Kevin R. Webster
Publikováno v:
Cancer Research. 82:3601-3601
KRAS is one of the most frequently mutated genes in cancer with alterations occurring in > 14% of all tumors. Recent advances have led to the discovery and development of inhibitors that bind the inactive (GDP-bound) form of KRASG12C. The most advanc
Autor:
Dierk Niessing, Robert Janowski, Dariusch Hekmat, Dirk Weuster-Botz, Johannes Hermann, Phillip Grob, Brigitte Walla, Max Huber
Publikováno v:
Biotechnol. J. 15:2000010 (2020)
Technical crystallization is an attractive method to purify recombinant proteins. However, it is rarely applied due to the limited crystallizability of many proteins. To overcome this limitation, single amino acid exchanges are rationally introduced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2f31868ee07cfc16b2e807f4836dc49
https://mediatum.ub.tum.de/1546783
https://mediatum.ub.tum.de/1546783