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Prof. Dr. Matthias Geyer

Member, Steering-Committee Member

Institute of Structural Biology

University Bonn, Department of Structural Immunology, Sigmund-Freud-Str. 25, D-53127 Bonn

matthias.geyer@uni-bonn.de

+49 228 28751400

Website

The Geyer lab is interested in the regulation of transcription and the molecular mechanisms that govern immune receptor activation. We use a variety of techniques from molecular biology and biochemistry to structural biology to analyze interaction between proteins, RNA, lipids, and ligands. The transcription cycle is regulated by cyclin-dependent kinases that phosphorylate the RNA polymerase II. We analyze the transition from transcription initiation to productive elongation in eukaryotic cells. We study the molecular and structural mechanisms that determine the activity and regulation of transcription-controlling kinases, as well as their inhibition by small molecular compounds. We recently also focused on the analysis of receptor activation of NLRP3 and forma-tion of the NLRP3/ASC/caspase inflammasome. Besides NACHT-domain containing proteins, Toll-like receptors, RIG-I and the cGAS-STING pathway mediate the immune-recogni-tion of pathogens. We aim at identifying target sites in these immune regulators that allow for the specific interference with the immune system, e.g., by small molecular compounds.

Recent publications

  • Quantitative modelling of P-TEFb mediated CTD phosphorylation identifies local cooperativity.

    PLoS computational biology

    Authors: Aaron Callenbach, Domagoj Dorešić, Robert Düster, Vanessa Nakonecnij, Erika Dudkin, Matthias Geyer, Jan Hasenauer

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  • Membrane-Active Peptide Protects Against Inflammation by Targeting NLRP3 Activation at the Trans-Golgi Network.

    Advanced science (Weinheim, Baden-Wurttemberg, Germany)

    Authors: Jonas Engelhardt, Nico Kirsch, Aileen Kerfin, Lars P Lunding, Dominic Ferber, Hannes Buthmann, Ilka Schreier, Carlotta Bosio, Ann-Kathrin Dobbelstein, Anna Klawonn, Rebecca C Coll, Lena Bauernhofer, Sandro Keller, Matthias Geyer, Michael Wegmann, Andra B Schromm, Günther Weindl

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  • C-terminal lysine residues localise NLRP10 at lipid droplets and govern NLRP10 oligomer formation.

    EMBO reports

    Authors: Timo-Daniel Voss, Christoph Winterberg, Adrian Beck, Clarissa Gottschild, Leonie Mueller, Selina M Enayat, Matthias Geyer, Thomas A Kufer

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