Author

G. Hagelueken

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4 Immunology· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Organism:human· 4 Research Focus:protein folding & dynamics· 4 Assay:cryo-EM· 3 Organism:bacteria (other)· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2

Frequent Co-Authors

M. Geyer· 6 shared M. F. Peter· 4 shared G. H. Thomas· 3 shared N. Schneberger· 3 shared A. Kopp· 2 shared E. Latz· 2 shared I. V. Hochheiser· 2 shared J. Moecking· 2 shared

Activity by Year

2020-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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6 shared papersBiochemistry

M. Geyer

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Pyroptosis inhibiting nanobodies block Gasdermin D pore formation

A. Kopp, G. Hagelueken, I. Jamitzky, J. Moecking, L. D. J. Schiffelers, F. I. Schmidt, M. Geyer

This study identifies nanobodies that inhibit GSDMD pore formation without affecting caspase cleavage, providing structural insights and potential drug design frameworks.

bioRxiv · Apr 20, 2023Biochemistry

Conformational coupling of the sialic acid TRAP transporter HiSiaQM with its substrate binding protein HiSiaP

M. F. Peter, J. A. Ruland, Y. Kim, P. Hendricks, J. P. Siebrasse, G. H. Thomas, U. Kubitscheck, G. Hagelueken

The paper demonstrates conformational coupling between the TRAP transporter HiSiaQM and its substrate binding protein HiSiaP using disulfide engineering and single-molecule TIRF microscopy.

bioRxiv · Mar 4, 2023Biochemistry

A conserved isoleucine in the binding pocket of RIG-I controls immune tolerance to mitochondrial RNA

A. K. de Regt, K. Anand, K. Ciupka, K. Gatterdam, B. Putschli, D. Fusshoeller, D. Hilbig, A. Kirchhoff, C. Hunkler, S. Wolter, A. Gruenewald, C. Schuberth-Wagner, J. Ludwig, K. Paeschke, E. Bartok, , M. Schlee

This study identifies an isoleucine residue in RIG-I that prevents recognition of 5p-RNA, thereby maintaining immune tolerance to mitochondrial RNA.

bioRxiv · Aug 2, 2022Immunology

SAVED by a toxin: Structure and function of the CRISPR Lon protease.

C. Rouillon, N. Schneberger, H. Chi, M. F. Peter, M. Geyer, W. Boenigk, R. Seifert, M. F. White, G. Hagelueken

The paper reports the crystal structure of CRISPR-Lon, a protein that activates by binding cA4 and cleaves CRISPR-T to release a nuclease-like fragment.

bioRxiv · Dec 6, 2021Biochemistry

The structure of HiSiaQM defines the architecture of tripartite ATP-independent periplasmic (TRAP) transporters

M. F. Peter, P. Depping, N. Schneberger, E. Severi, K. Gatterdam, S. Tindall, A. Durand, V. Heinz, P. A. Koenig, M. Geyer, C. Ziegler, G. H. Thomas, G. Hagelueken

This paper presents the first cryo-EM structure of TRAP transporter membrane domains and identifies structural features that enable monomeric elevator architecture.

bioRxiv · Dec 3, 2021Biochemistry

Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation

I. V. Hochheiser, H. Behrmann, G. Hagelueken, J. F. Rodriguez-Alcazar, A. Kopp, E. Latz, E. Behrmann, M. Geyer

The paper determines the directionality of PYD filament growth by showing ASC elongates exclusively on the B-end of NLRP3 filaments, enabling a transition from NLRP3 nucleation to ASC elongation.

bioRxiv · Nov 25, 2021Immunology

Cryo-EM structure of the NLRP3 decamer bound to the cytokine release inhibitory drug CRID3

I. V. Hochheiser, M. Pilsl, G. Hagelueken, J. Moecking, M. Marleaux, R. Brinkschulte, E. Latz, C. Engel, M. Geyer

The paper determines the cryo-EM structure of NLRP3 bound to CRID3, revealing how the inhibitor stabilizes the protein and provides insights for drug development.

bioRxiv · Jul 22, 2021Immunology

Triggering closure of a sialic acid TRAP transporter substrate binding protein through binding of natural or artificial substrates

M. F. Peter, C. Gebhardt, J. Glaenzer, N. Schneberger, M. de Boer, G. H. Thomas, T. Cordes, G. Hagelueken

This study investigates the conformational changes in the sialic acid TRAP transporter SBP VcSiaP upon substrate binding, showing that substrate induces closure and provides structural insights for inhibitor development.

bioRxiv · Dec 2, 2020Biophysics