M
Michael Hennig
Researcher at Hoffmann-La Roche
Publications - 106
Citations - 5957
Michael Hennig is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Binding site & Carnitine. The author has an hindex of 39, co-authored 102 publications receiving 5451 citations. Previous affiliations of Michael Hennig include University of Cologne & University of Göttingen.
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Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose
Claudia Ferrara,Sandra Grau,Christiane Jäger,Peter Sondermann,Peter Brünker,Inja Waldhauer,Michael Hennig,Armin Ruf,Arne C. Rufer,Martine Stihle,Pablo Umana,Jörg Benz +11 more
TL;DR: A detailed, molecular understanding of the regulatory role of Fc-oligosaccharide core fucosylation in improving ADCC is obtained and a unique mechanism by which the immune system can regulate antibody-mediated effector functions is suggested.
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Radiometal-Labelled Macrocyclic Chelator-Derivatised Somatostatin Analogue with Superb Tumour-Targeting Properties and Potential for Receptor-Mediated Internal Radiotherapy
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Insight into steroid scaffold formation from the structure of human oxidosqualene cyclase
Ralf Thoma,Tanja Schulz-Gasch,Brigitte D'Arcy,Jörg Benz,Johannes Aebi,Henrietta Dehmlow,Michael Hennig,Martine Stihle,Armin Ruf +8 more
TL;DR: The target protein with an inhibitor that showed cholesterol lowering in vivo opens the way for the structure-based design of new OSC inhibitors, and the complex with the reaction product lanosterol gives a clear picture of the way in which the enzyme achieves product specificity in this highly exothermic cyclization reaction.
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Biophysics in drug discovery: impact, challenges and opportunities
Jean-Paul Renaud,Chun-wa Chung,U. Helena Danielson,Ursula Egner,Michael Hennig,Roderick E. Hubbard,Herbert Nar +6 more
TL;DR: This Review provides a framework to understand this evolution of biophysical technologies by describing the key biophysical methods, the information they can provide and the ways in which they can be applied at different stages of the drug discovery process.
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Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon.
TL;DR: The crystal structure of the extracellular domain of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon is described and reveals two multiply connected folding domains which embrace a large central cavity containing the active site.