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Drug Design Group,
Institute of Pharmaceutical Chemistry,
Drug Design Group, Institute of Pharmaceutical Chemistry
Molecular scientist, computational and beyond.
Hot-spot analysis to dissect the functional protein-protein interface of a tRNA-modifying enzyme.
Proteins Oct, 2014 | Pubmed ID: 24975703
Six Biophysical Screening Methods Miss a Large Proportion of Crystallographically Discovered Fragment Hits: A Case Study.
ACS chemical biology 06, 2016 | Pubmed ID: 27028906
Structures of endothiapepsin-fragment complexes from crystallographic fragment screening using a novel, diverse and affordable 96-compound fragment library.
Acta crystallographica. Section F, Structural biology communications 05, 2016 | Pubmed ID: 27139825
Soaking suggests "alternative facts": Only co-crystallization discloses major ligand-induced interface rearrangements of a homodimeric tRNA-binding protein indicating a novel mode-of-inhibition.
PloS one , 2017 | Pubmed ID: 28419165
F2X-Universal and F2X-Entry: Structurally Diverse Compound Libraries for Crystallographic Fragment Screening.
Structure (London, England : 1993) 06, 2020 | Pubmed ID: 32413289
Philipps-Universität Marburg
Jan Wollenhaupt1,
Tatjana Barthel1,2,
Gustavo M. A. Lima3,
Alexander Metz4,
Dirk Wallacher5,
Elmir Jagudin3,
Franziska U. Huschmann1,4,
Thomas Hauß1,
Christian G. Feiler1,
Martin Gerlach1,
Michael Hellmig1,
Ronald Förster1,
Michael Steffien1,
Andreas Heine4,
Gerhard Klebe4,
Uwe Mueller1,
Manfred S. Weiss1
1Macromolecular Crystallography, Helmholtz-Zentrum Berlin,
2Structural Biochemistry Group, Institute for Chemistry and Biochemistry, Freie Universität Berlin,
3BioMAX, MAX IV Laboratory,
4Drug Design Group, Institute of Pharmaceutical Chemistry, Philipps-Universität Marburg,
5Department Sample Environment, Helmholtz-Zentrum Berlin
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