M
Michael Kolbe
Researcher at University of Hamburg
Publications - 48
Citations - 2619
Michael Kolbe is an academic researcher from University of Hamburg. The author has contributed to research in topics: Shigella flexneri & Secretion. The author has an hindex of 21, co-authored 40 publications receiving 2282 citations. Previous affiliations of Michael Kolbe include Max Planck Society.
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Journal ArticleDOI
Structure of the Light-Driven Chloride Pump Halorhodopsin at 1.8 Å Resolution
TL;DR: A combination of ion-ion and ion-dipole interactions for stabilizing the anion 18 angstroms below the membrane surface explains why chloride and proton translocation modes are mechanistically equivalent in archaeal rhodopsins.
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Atomic model of the type III secretion system needle
Antoine Loquet,Nikolaos G. Sgourakis,Rashmi Gupta,Karin Giller,Dietmar Riedel,Christian Goosmann,Christian Griesinger,Michael Kolbe,David Baker,Stefan Becker,Adam Lange +10 more
TL;DR: An alternative approach combining recombinant wild-type needle production, solid-state NMR, electron microscopy and Rosetta modelling is reported to reveal the supramolecular interfaces and ultimately the complete atomic structure of the Salmonella typhimurium T3SS needle.
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AhR sensing of bacterial pigments regulates antibacterial defence
Pedro Moura-Alves,Kellen C. Faé,Erica Houthuys,Anca Dorhoi,Annika Kreuchwig,Jens Furkert,Nicola Barison,Anne Diehl,Antje Munder,Patricia Constant,Tatsiana Skrahina,Ute Guhlich-Bornhof,Marion Klemm,Anne-Britta Koehler,Silke Bandermann,Christian Goosmann,Hans-Joachim Mollenkopf,Robert Hurwitz,Volker Brinkmann,Simon Fillatreau,Mamadou Daffé,Burkhard Tümmler,Michael Kolbe,Hartmut Oschkinat,Gerd Krause,Stefan H. E. Kaufmann +25 more
TL;DR: It is demonstrated that AhR senses distinct bacterial virulence factors and controls antibacterial responses, supporting a previously unidentified role for AhR as an intracellular pattern recognition receptor, and identifying bacterial pigments as a new class of pathogen-associated molecular patterns.
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Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit.
TL;DR: Results show that the interaction of Gt with an activated rhodopsin monomer is sufficient for fully functional Gt activation, and the activation rate in solution is at the physically possible limit, but the rate in the native membrane is still 10-fold higher.
Journal ArticleDOI
On the self-association potential of transmembrane tight junction proteins
Ingolf E. Blasig,Lars Winkler,B. Lassowski,Sebastian L. Mueller,Nikolaj Zuleger,Eberhard Krause,Gerd Krause,Klaus Gast,Michael Kolbe,Jörg Piontek +9 more
TL;DR: The assumption that homodimerization of transmembrane tight junction proteins may serve as a common structural feature in tight junction assembly is supported.