Publications using BECM data

Monté, D., Lens, Z., Dewitte, F., et al., Nature Communications volume 16, 3772 (2025),  Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1, https://www.nature.com/articles/s41467-025-59014-8 

Lambert, F., Felix, J., Wautier, S., et al, Cell Reports 44(8) (2025), Antibody-mediated TGF-β1 activation for the treatment of diseases caused by deleterious T cell activity, https://www.sciencedirect.com/science/article/pii/S2211124725008320?via%3Dihub

Schenck, S., Laeremans, T., Steyaert, J. & Brunner, J.D., Nature Communications volume 16, 4172 (2025), Structures of native SV2A reveal the binding mode for tetanus neurotoxin and anti-epileptic racetams, https://www.nature.com/articles/s41467-025-59545-0

Matthys, A., Felix, J., Catani, J.P.C., et al., Nature Communications volume 16, 5831 (2025), Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses, https://www.nature.com/articles/s41467-025-60232-3

Sogues, A., Sleutel, M., Petit, J. et al., Proc. Natl. Acad. Sci. U.S.A. 122 (31) e2426928122 (2025), Cryo-EM structure and polar assembly of the PS2 S-layer of Corynebacterium glutamicum, , https://doi.org/10.1073/pnas.2426928122

Sleutel, M., Sogues, A., Van Gerven, N. et al., Nat Commun 16, 7652 (2025), Cryo-EM identifies F-ENA of Bacillus thuringiensis as a widespread family of endospore appendages across Firmicutes.  https://doi.org/10.1038/s41467-025-62896-3

Maes, L., Mares-Mejia, I., Martin, E., et al., Nucleic Acids Research, Volume 53, Issue 16 (2025), Cryo-EM structures of the MnmE–MnmG complex reveal large conformational changes and provide new insights into the mechanism of tRNA modification, https://doi.org/10.1093/nar/gkaf824

Gautam, J., Wu, J., Lally, J. S. V., et al., Nature volume 645, 507–517 (2025), ACLY inhibition promotes tumour immunity and suppresses liver cancer, https://www.nature.com/articles/s41586-025-09297-0

Ancia, M., Wahni, K., Chakrowf, J., et al., Protein Science volume 34, e70116 (2025), Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7, https://onlinelibrary.wiley.com/doi/10.1002/pro.70116

Gennaris, A., Nguyen, V. S., Thouvenel, L., et al., Cell Reports volume 44, 115446 (2025), Optimal functioning of the Lpt bridge depends on a ternary complex between the lipocalin YedD and the LptDE translocon, https://www.sciencedirect.com/science/article/pii/S2211124725002177?via%3Dihub

Sogues, A., Leigh, K., Halingstad, E.V., et al., Proc Natl Acad Sci U S A 121(51):e2415351121, Architecture of the Sap S-layer of Bacillus anthracis revealed by integrative structural biology, https://www.pnas.org/doi/10.1073/pnas.2415351121

Sogues, A., Sleutel, M., Petit, J., et al., bioRxiv, 2024.09. 05.611363, Cryo-EM structure and polar assembly of the PS2 S-layer of Corynebacterium glutamicum, https://www.biorxiv.org/content/10.1101/2024.09.05.611363v1

Sleutel, M., Zegeye, E.D., Llarena, A-K., et al., Nature Commun 15 (1), 7514, Helical ultrastructure of the L-ENA spore aggregation factor of a Bacillus paranthracis foodborne outbreak strain, https://www.nature.com/articles/s41467-024-51804-w

Santin, Y.G., Sogues, A., Bourigault, Y., et al., Nature Commun 15 (1), 3590, Lifecycle of a predatory bacterium vampirizing its prey through the cell envelope and S-layer, https://www.nature.com/articles/s41467-024-48042-5

Acar, D.D., Witkowski, W., Wejda, M.,et al., EBioMedicine 100, Integrating artificial intelligence-based epitope prediction in a SARS-CoV-2 antibody discovery pipeline: caution is warranted, https://www.thelancet.com/journals/ebiom/article/PIIS2352-3964(23)00526-1/fulltext

Janssens, A., Nguyen, V.S., Cecil, A.J., et al., Nature 626, 617-625, SlyB encapsulates outer membrane proteins in stress-induced lipid nanodomains, https://www.nature.com/articles/s41586-023-06925-5

Sleutel, M., Sonani, R.R., Miller, J.G., et al.,  BioRxiv doi: 10.1101/2024.12.30.630787, Donor Strand Complementation and Calcium Ion Coordination Drive the Chaperone-free Polymerization of Archaeal Cannulae, https://www.biorxiv.org/content/10.1101/2024.12.30.630787v1

Li, C., Willegems, K., Uchański, et al., Journal of Biological Chemistry 300 (10), 107734, Rapid small-scale nanobody-assisted purification of ryanodine receptors for cryo-EM, https://www.sciencedirect.com/science/article/pii/S002192582402235X

Baes R., Stroobants, A., Jonckheere K. et al., EMBO: Molecular biology of Archaea, Structural RNA-mediated regulation of the major heat shock protein in the thermophilic archaeon Sulfolobus acidocaldarius (MBoA 2024), https://scholar.google.com/citations?view_op=view_citation&hl=en&user=1-biKDEAAAAJ&sortby=pubdate&citation_for_view=1-biKDEAAAAJ:H7nrzBkawXsC

Odorčić, I., Hamed, M.B., Lismont, S., et al., Nature Communications 15 (1), 4479, Apo and Aβ46-bound γ-secretase structures provide insights into amyloid-β processing by the APH-1B isoform, https://www.nature.com/articles/s41467-024-48776-2

C Li & RG Efremov, bioRxiv, 2024.12. 20.629683, Lipids modulate open probability of RyR1 under cryo-EM conditions, https://www.biorxiv.org/content/10.1101/2024.12.20.629683v1.abstract

Kraus, J.M., Neubergerová, M., Cuadrado, A.F. et al., The structural scaffold of the TPLATE complex deforms the membrane during plant endocytosis, BioRxiv 2024.10.07.616965, https://www.biorxiv.org/content/10.1101/2024.10.07.616965v1

Galicia, C., Guaitoli, G., Fislage, M., et al., eLife 13:RP94503.(2024), Structural insights in the GTP-driven monomerization and activation of a bacterial LRRK2 homologue using allosteric nanobodies. eLife 13:RP94503, https://elifesciences.org/articles/94503

Maes, L., Martin, E., Bickel, D., et al., BioRxiv 2024, Cryo-EM structures of the MnmE-MnmG complex reveal large conformational changes and provide new insights into the mechanism of tRNA modification, https://www.biorxiv.org/content/10.1101/2024.11.29.625835v1

Ye, T., Chen, Y., Zhong, Z., et al., J. Am. Chem. Soc. 2025, 147, 1, 1307–1318 Rapid small-scale nanobody-assisted purification of ryanodine receptors for cryo-EM, https://pubs.acs.org/doi/full/10.1021/jacs.4c15688 

Hamouda, A.E.I., Filtjens, J., Brabants, E., et al., Nat Commun 15, 10635 (2024), Intratumoral delivery of lipid nanoparticle-formulated mRNA encoding IL-21, IL-7, and 4-1BBL induces systemic anti-tumor immunity, https://www.nature.com/articles/s41467-024-54877-9 

Ye T., Zhong Z., Cappellesso, F., et al., Biomaterials Volume 311, December 2024, 122693, CO-DELIVERY of glutamic acid-extended peptide antigen and imidazoquinoline TLR7/8 agonist via ionizable lipid nanoparticles induces protective anti-tumor immunity, https://www.sciencedirect.com/science/article/pii/S0142961224002278 

Zhong, Z., Deventer, M.H., Chen, Y. et al., Angew. Chem. Int. Ed. 2024, e202419031, A Fentanyl Hapten-Displaying Lipid Nanoparticle Vaccine that NonCovalently Encapsulates a TLR7/8 Agonist and T-Helper Epitope Induces Protective Anti-Fentanyl Immunity, https://onlinelibrary.wiley.com/doi/pdf/10.1002/ange.202419031

Bloch, Y., Felix, J., Merceron, R., et al.; Structures of complete extracellular receptor assemblies mediated by IL-12 and IL-23, (2024), Nat Struct Mol Biol 2024 Apr;31(4):591-597, https://www.nature.com/articles/s41594-023-01190-6

Torino, S., Dhurandhar, M., Stroobants, A., et al.; Time-resolved cryo-EM using a combination of droplet microfluidics with on-demand jetting, Nat Methods. 2023 Sep;20(9):1400-1408. doi: 10.1038/s41592-023-01967-z, https://www.nature.com/articles/s41592-023-01967-z

De Gieter, S., Gallagher, C.I., Wijckmans, E., et al.; Sterol derivative binding to the orthosteric site causes conformational changes in an invertebrate Cys-loop receptor, Elife. 2023 Jul 3;12:e86029. doi: 10.7554/eLife.86029, https://elifesciences.org/articles/86029

Fernandez, M., Shkumatov, A.V., Liu, Y., et al.; AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements, Nucleic Acids Res. 2023 Jun 9;51(10):4929-4941. doi: 10.1093/nar/gkad241, https://academic.oup.com/nar/article/51/10/4929/7110757

Claridge, J.K., Martens, C., Pradhan, B., et al.; The folding-limited nucleation of curli hints at an evolved safety mechanism for functional amyloid production, bioRxiv, 2023.05. 26.542396, https://www.biorxiv.org/content/10.1101/2023.05.26.542396v1

Sleutel, M., Pradhan, B., Volkov, A.N., Remaut, H.; Structural analysis and architectural principles of the bacterial amyloid curli, Nature Communications 14 (1), 2822, https://www.nature.com/articles/s41467-023-38204-2

Tsirigotaki, A., Dansercoer, A., Verschueren, K.H.G., et al.; Mechanism of receptor assembly via the pleiotropic adipokine Leptin, Nature Structural & Molecular Biology 30 (4), 551-563, https://www.nature.com/articles/s41594-023-00941-9

Dupuy, E., Van der Verren, S.E., Lin, J. et al.; A molecular device for the redox quality control of GroEL/ES substrates, Cell 186 (5), 1039-1049. e17, https://www.sciencedirect.com/science/article/pii/S0092867423000430

Fioravanti, A., Mathelie-Guinlet, M., Dufrêne, Y.F., Remaut, H.; The Bacillus anthracis S-layer is an exoskeleton-like structure that imparts mechanical and osmotic stabilization to the cell wall, PNAS nexus 1 (4), September 2022,  pgac121, https://academic.oup.com/pnasnexus/article/1/4/pgac121/6655932

Shkumatov, A.V., Aryanpour, N., Oger, C.A., et al.; Structural insight into Tn3 family transposition mechanism,  Nature Communications,  13, Article number: 6155 (2022), https://www.nature.com/articles/s41467-022-33871-z

Kolata, P. & Efremov, R.G.; Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation,  eLife 2021;10:e68710 DOI: 10.7554/eLife.68710

Pradhan, B., Liedtke, J. Sleutel, M., et al; Endospore Appendages: a novel pilus superfamily from the endospores of pathogenic Bacilli, EMBO J 2021:e106887 https://doi.org/10.15252/embj.2020106887

Efremov, R.G. & Stroobants, A.; Coma-corrected rapid single-particle cryo-EM data collection on the CRYO ARM 300, Acta Cryst. 2021, D77, 555-564
https://doi.org/10.1107/S2059798321002151

Fislage, M., Shkumatov, A.V., Stroobants, A. & Efremov, R.G.; Assessing the JEOL CRYO ARM 300 for high-throughput automated single-particle cryo-EM in a multiuser environment; IUCrJ, Volume 7, Part 4, 2020, pp. 707-718,https://doi.org/10.1107/S2052252520006065