Daniel Roderer
@daniel_roderer
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Structural biologist and protein biochemist. Interested in bacterial pathogenesis and host-microbiome interactions. Junior Group Leader at @LeibnizFMP.
Berlin, Germany
Joined April 2018
RT @HanSun_lab: We are very grateful for this exciting opportunity provided by Leibniz Cooperative Excellence. Looking forward to new colla….
leibniz-fmp.softgarden.io
We're looking for: PhD student or postdoctoral fellow (f/m/d) (Full or Part Time) • Berlin, Deutschland
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RT @LeibnizFMP: 🎉 Herzlichen Glückwunsch! Prof. Volker Haucke @VolkerHaucke erhält den #LeibnizPreis 2025 der @dfg_public für seine bahnbr….
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RT @mpimoph: Sebastian Tacke has been honored with the Paper of the Year Award by the Journal of Structural Biology @ElsevierConnect for h….
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RT @HasnainKazim: Ich möchte nur kurz daran erinnern, dass dieser Zug in meiner Kindheit aus politischen Gründen unmöglich gewesen wäre, un….
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RT @MillesSigrid: I am happy our new manuscript on intrinsically disordered proteins in #endocytosis is now out on BioRxiv #NMR.@LeibnizFMP.
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RT @martingommel: 🚬 An die Raucher:innen, die kommentieren, dass ich mich ja woanders hin bewegen soll, wenn ihr an der Haltestelle qualmt:….
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RT @MishaKudryashev: We have a new paper for you: “Structure of tetrameric forms of the serotonin-gated 5-HT3A receptor ion channel”. Here….
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Are you interested in the structural background of the host-microbiome interaction and searching for a PhD position in an exciting scientific community? Then look no further and apply at the @LeibnizFMP! Please find details here:
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RT @LeibnizFMP: Happy to start working with new 1,2 GHz NMR spectrometer - perfect for precise analysis of complex biological systems like….
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RT @FiedlerLab: Follow up to our discovery of endogenous protein pyrophosphorylation, Arif Celik, a PhD student from our lab, decided to se….
pubs.acs.org
While the function of protein phosphorylation in eukaryotic cell signaling is well established, the role of a closely related modification, protein pyrophosphorylation, is just starting to surface. A...
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RT @FiedlerLab: Happy to share our latest paper on protein pyrophosphorylation - yes, it exists! It has been a long journey with many wonde….
nature.com
Nature Chemical Biology - A tailored proteomics workflow to identify endogenous protein pyrophosphorylation in human cells was developed, revealing the dependence of the modification on inositol...
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RT @LeibnizFMP: FMP Retreat 2024! 🎉A big thank you to everyone who joined us. It was fantastic to see all of you presenting your science, e….
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RT @GBM_eV: 📢Time to voice our concerns about the #WissZeitVG once again!.➡️17 scientific societies, which together represent more than 55,….
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RT @theliulab: Finally published! Delighted to introduce CLASP: a novel framework for spatial proteomics. Using XLMS we unveiled intricate….
nature.com
Nature Communications - The spatial mapping of proteins can give important functional insights. Here, Zhu et al. develop a cross-linking mass spectrometry-based spatial proteomics method that does...
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RT @Glockshuber_lab: Check out our new paper on a previously unknown function of the type 1 pilus assembly platform FimD! Many thanks to ev….
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RT @HanSun_lab: The 1.2 GHz NMR spectrometer has arrived at FMP Berlin. 😀 (Photo copyright: Adam Lange)
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. TIGIT and Gal-GalNAc on two sides of the matchstick head. From this, we can deduce a model on how F. nucleatum applies Fap2 both as a molecular spear against immune cells and a molecular grappling that attached it to tumors.
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This groove is closed by the unstructured N-terminus. At the membrane-distal end, the b-helix ends in a matchstick-like thickening. By combining cryo-EM, structure prediction, molecular docking, and MD simulation, we identify the binding sites of the two Fap2 receptors . .
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Here we show a strategy to recombinantly produce the extracellular part of Fap2 and present the first structural analysis of the protein using #cryoEM. Fap2 has a 45 nm long rod-shaped b-helix with a unique triangular cross-section that opens up a hydrophobic groove.
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A thread: F. nucleatum has been shown to drive the progression of colorectal cancer by downregulating the immune system and stimulating tumor cell growth. A key protein for this is the adhesin Fap2, which binds to natural killer cells via TIGIT and to tumor cells via Gal-GalNAc.
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