Zobrazeno 1 - 10
of 478
pro vyhledávání: '"Gerhard, Klebe"'
Autor:
Anke-Dorothee Werner, Nils Krapoth, Michael J. Norris, Andreas Heine, Gerhard Klebe, Erica Ollmann Saphire, Stephan Becker
Publikováno v:
ACS Omega, Vol 9, Iss 30, Pp 33193-33203 (2024)
Externí odkaz:
https://doaj.org/article/35426d60ad6248b28f7e4aa3aa389ab4
Autor:
Marina Gárdonyi, Christian Hasewinkel, Johanna Wallbaum, Jan Wollenhaupt, Manfred S. Weiss, Gerhard Klebe, Klaus Reuter, Andreas Heine
Publikováno v:
ACS Omega, Vol 8, Iss 48, Pp 46051-46065 (2023)
Externí odkaz:
https://doaj.org/article/5bde61bba2284f389909af2957a03088
Autor:
Franziska U. Huschmann, Janis Mueller, Alexander Metz, Moritz Ruf, Johanna Senst, Serghei Glinca, Johannes Schiebel, Andreas Heine, Gerhard Klebe
Publikováno v:
Crystals, Vol 14, Iss 9, p 755 (2024)
Fragment screening directly on protein crystals has been applied using AnalytiCon’s collection of intermediates that have been utilized to generate libraries of larger synthetic natural product-like molecules. The fragments with well-balanced physi
Externí odkaz:
https://doaj.org/article/4e95b53a82e24820bf05c4f364b32dbd
Publikováno v:
ACS Omega, Vol 4, Iss 1, Pp 775-784 (2019)
Externí odkaz:
https://doaj.org/article/bcb58fa64ded431691ce5d044db1370f
Autor:
Johannes Schiebel, Roberto Gaspari, Tobias Wulsdorf, Khang Ngo, Christian Sohn, Tobias E. Schrader, Andrea Cavalli, Andreas Ostermann, Andreas Heine, Gerhard Klebe
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Trypsin is a serine protease. Here the authors present the high resolution X-ray and neutron diffraction structures of uncomplexed and inhibitor bound trypsin that provide insights into the geometry of H-bonds in the active site of the enzyme and mol
Externí odkaz:
https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b1
Autor:
Anna Sandner, Khang Ngo, Christoph P. Sager, Frithjof Scheer, Michael Daude, Wibke E. Diederich, Andreas Heine, Gerhard Klebe
Publikováno v:
Biomolecules, Vol 11, Iss 12, p 1837 (2021)
The transient specificity pocket of aldose reductase only opens in response to specific ligands. This pocket may offer an advantage for the development of novel, more selective ligands for proteins with similar topology that lack such an adaptive poc
Externí odkaz:
https://doaj.org/article/d281860ce9d74c0db718c7b1b1b9ce96
Autor:
Janis Müller, Raphael Klein, Olga Tarkhanova, Anastasiia Gryniukova, Petro Borysko, Stefan Merkl, Moritz Ruf, Alexander Neumann, Marcus Gastreich, Yurii S. Moroz, Gerhard Klebe, Serghei Glinca
Publikováno v:
Journal of Medicinal Chemistry. 65:15663-15678
Fragment-based drug discovery (FBDD) has successfully led to approved therapeutics for challenging and "undruggable" targets. In the context of FBDD, we introduce a novel, multidisciplinary method to identify active molecules from purchasable chemica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abe624a2c3a417198233b05e985dc866
https://doi.org/10.1021/acs.jmedchem.2c00813
https://doi.org/10.1021/acs.jmedchem.2c00813
Autor:
Florian Funk, Annette Kronenbitter, Katarzyna Hackert, Matthias Oebbeke, Gerhard Klebe, Mareike Barth, Daniel Koch, Joachim P Schmitt
Publikováno v:
Cardiovascular Research
Cardiovascular research 119(7), 1568-1582 (2023). doi:10.1093/cvr/cvad037
Cardiovascular research 119(7), 1568-1582 (2023). doi:10.1093/cvr/cvad037
Cardiovascular research (2023). doi:10.1093/cvr/cvad037
Published by Oxford University Press, Oxford
Published by Oxford University Press, Oxford
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22f61f5c2d92da896dd421fb8963ebf4
https://hdl.handle.net/21.11116/0000-000D-6B09-2
https://hdl.handle.net/21.11116/0000-000D-6B09-2
Autor:
Maurice Sebastiani, Christina Behrens, Stefanie Dörr, Hans-Dieter Gerber, Rania Benazza, Oscar Hernandez-Alba, Sarah Cianférani, Gerhard Klebe, Andreas Heine, Klaus Reuter
Publikováno v:
ACS Chemical Biology. 17:2229-2247
In tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f71ab9cd3de511f3f5feba57768aaeb
https://doi.org/10.1021/acschembio.2c00368
https://doi.org/10.1021/acschembio.2c00368
Publikováno v:
Biomolecules, Vol 10, Iss 4, p 518 (2020)
Fragment screening is a powerful tool to identify and characterize binding pockets in proteins. We herein present the results of a proof-of-concept screening campaign of a versatile 96-entry fragment library from our laboratory against the drug targe
Externí odkaz:
https://doaj.org/article/cae3a9517b134e9fa02761b04bb94cb1