2023

Arragain, B., Pelosse, M., Thompson, A., & Cusack, S. (2023). Structural and functional analysis of the minimal orthomyxovirus-like polymerase of Tilapia Lake Virus from the highly diverged Amnoonviridae family. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-44044-x

Azad, K., Guilligay, D., Boscheron, C., Maity, S., De Franceschi, N., Sulbaran, G., Effantin, G., Wang, H., Kleman, J.-P., Bassereau, P., Schoehn, G., Roos, W. H., Desfosses, A., & Weissenhorn, W. (2023). Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage. Nature Structural & Molecular Biology, 30(1), 81–90. https://doi.org/10.1038/s41594-022-00867-8

Betancurt-Anzola, L., Martínez-Carranza, M., Delarue, M., Zatopek, K. M., Gardner, A. F., & Sauguet, L. (2023). Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-44125-x

Chenavier, F., Estrozi, L. F., Teulon, J.-M., Zarkadas, E., Freslon, L.-L., Pellequer, J.-L., Ruigrok, R. W. H., Schoehn, G., Ballandras-Colas, A., & Crépin, T. (2023). Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation. Science Advances, 9(50). https://doi.org/10.1126/sciadv.adj9974

Cisse, A., Desfosses, A., Stainer, S., Kandiah, E., Traore, D. A. K., Bezault, A., Schachner-Nedherer, A.-L., Leitinger, G., Hoerl, G., Hinterdorfer, P., Gutsche, I., Prassl, R., Peters, J., & Kornmueller, K. (2023). Targeting structural flexibility in low density lipoprotein by integrating cryo-electron microscopy and high-speed atomic force microscopy. International Journal of Biological Macromolecules, 252, 126345. https://doi.org/10.1016/j.ijbiomac.2023.126345

D’Acapito, A., Roret, T., Zarkadas, E., Mocaër, P.-Y., Lelchat, F., Baudoux, A.-C., Schoehn, G., & Neumann, E. (2023). Structural Study of the Cobetia marina Bacteriophage 1 (Carin-1) by Cryo-EM. Journal of Virology, 97(4). https://doi.org/10.1128/jvi.00248-23

Degroux, S., Effantin, G., Linares, R., Schoehn, G., & Breyton, C. (2023). Deciphering Bacteriophage T5 Host Recognition Mechanism and Infection Trigger. Journal of Virology, 97(3). https://doi.org/10.1128/jvi.01584-22

Dolce, L. G., Nesterenko, Y., Walther, L., Weis, F., & Kowalinski, E. (2023). Structural basis for guide RNA selection by the RESC1–RESC2 complex. Nucleic Acids Research, 51(9), 4602–4612. https://doi.org/10.1093/nar/gkad217

Durieux Trouilleton, Q., Barata-García, S., Arragain, B., Reguera, J., & Malet, H. (2023). Structures of active Hantaan virus polymerase uncover the mechanisms of Hantaviridae genome replication. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-38555-w

Effantin, G., Hograindleur, M.-A., Fenel, D., Fender, P., & Vassal-Stermann, E. (2023). Toward the understanding of DSG2 and CD46 interaction with HAdV-11 fiber, a super-complex analysis. Journal of Virology, 97(11). https://doi.org/10.1128/jvi.00910-23

Fernandez-Martinez, D., Tully, M. D., Leonard, G., Mathieu, M., & Kandiah, E. (2023). Structural insights into the bi-specific cross-over dual variable antibody architecture by cryo-EM. Scientific Reports, 13(1). https://doi.org/10.1038/s41598-023-35678-4

Grinzato, A., Auguin, D., Kikuti, C., Nandwani, N., Moussaoui, D., Pathak, D., Kandiah, E., Ruppel, K. M., Spudich, J. A., Houdusse, A., & Robert-Paganin, J. (2023). Cryo-EM structure of the folded-back state of human β-cardiac myosin. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-38698-w

Jones, R., Hons, M., Rabah, N., Zamarreño, N., Arranz, R., & Reguera, J. (2023). Structural basis and dynamics of Chikungunya alphavirus RNA capping by nsP1 capping pores. Proceedings of the National Academy of Sciences, 120(12). https://doi.org/10.1073/pnas.2213934120

Khazma, T., Golan-Vaishenker, Y., Guez-Haddad, J., Grossman, A., Sain, R., Weitman, M., Plotnikov, A., Zalk, R., Yaron, A., Hons, M., & Opatowsky, Y. (2022). A duplex structure of SARM1 octamers stabilized by a new inhibitor. Cellular and Molecular Life Sciences, 80(1). https://doi.org/10.1007/s00018-022-04641-3

Khazma, T., Grossman, A., Guez-Haddad, J., Feng, C., Dabas, H., Sain, R., Weitman, M., Zalk, R., Isupov, M. N., Hammarlund, M., Hons, M., & Opatowsky, Y. (2023). Structure-function analysis of ceTIR-1/hSARM1 explains the lack of Wallerian axonal degeneration in C. elegans. Cell Reports, 42(9), 113026. https://doi.org/10.1016/j.celrep.2023.113026

Kišonaitė, M., Wild, K., Lapouge, K. et al. Structural inventory of cotranslational protein folding by the eukaryotic RAC complex. Nat Struct Mol Biol 30, 670–677 (2023). https://doi.org/10.1038/s41594-023-00973-1

Kouba, T., Dubankova, A., Drncova, P., Donati, E., Vidossich, P., Speranzini, V., Pflug, A., Huchting, J., Meier, C., De Vivo, M., & Cusack, S. (2023). Direct observation of backtracking by influenza A and B polymerases upon consecutive incorporation of the nucleoside analog T1106. Cell Reports, 42(1), 111901. https://doi.org/10.1016/j.celrep.2022.111901

Lethier, M., Huard, K., Hons, M., Favier, A., Brutscher, B., Boeri Erba, E., Abbott, D. W., Cusack, S., & Pellegrini, E. (2023). Structure shows that the BIR2 domain of E3 ligase XIAP binds across the RIPK2 kinase dimer interface. Life Science Alliance, 6(11), e202201784. https://doi.org/10.26508/lsa.202201784

Linares, R., Arnaud, C.-A., Effantin, G., Darnault, C., Epalle, N. H., Boeri Erba, E., Schoehn, G., & Breyton, C. (2023). Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation. Science Advances, 9(12). https://doi.org/10.1126/sciadv.ade9674

McGregor, L., Acajjaoui, S., Desfosses, A., Saïdi, M., Bacia-Verloop, M., Schwarz, J. J., Juyoux, P., von Velsen, J., Bowler, M. W., McCarthy, A. A., Kandiah, E., Gutsche, I., & Soler-Lopez, M. (2023). The assembly of the Mitochondrial Complex I Assembly complex uncovers a redox pathway coordination. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-43865-0

Petukhova, V. Z., Aboagye, S. Y., Ardini, M., Lullo, R. P., Fata, F., Byrne, M. E., Gabriele, F., Martin, L. M., Harding, L. N. M., Gone, V., Dangi, B., Lantvit, D. D., Nikolic, D., Ippoliti, R., Effantin, G., Ling, W. L., Johnson, J. J., Thatcher, G. R. J., Angelucci, F., … Petukhov, P. A. (2023). Non-covalent inhibitors of thioredoxin glutathione reductase with schistosomicidal activity in vivo. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-39444-y

Sharma, R., Adams, M., Griffith-Jones, S., Sahr, T., Gomez-Valero, L., Weis, F., Hons, M., Gharbi, S., Berkane, R., Stolz, A., Buchrieser, C., & Bhogaraju, S. (2023). Structural basis for the toxicity of Legionella pneumophila effector SidH. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-42683-8

Schwartz, T., Fadeeva, M., Klaiman, D., & Nelson, N. (2023). Structure of Photosystem I Supercomplex Isolated from a Chlamydomonas reinhardtii Cytochrome b6f Temperature-Sensitive Mutant. Biomolecules, 13(3), 537. https://doi.org/10.3390/biom13030537

Torres-Sánchez, L., Géry Sana, T., Decossas, M., Hashem, Y., & Krasteva, P. V. (2023). Structures of theP. aeruginosaFleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control. Proceedings of the National Academy of Sciences, 120(50). https://doi.org/10.1073/pnas.2312276120

Trastoy, B., Du, J. J., Cifuente, J. O., Rudolph, L., García-Alija, M., Klontz, E. H., Deredge, D., Sultana, N., Huynh, C. G., Flowers, M. W., Li, C., Sastre, D. E., Wang, L.-X., Corzana, F., Mallagaray, A., Sundberg, E. J., & Guerin, M. E. (2023). Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-37215-3

Velasco-Carneros, L., Cuéllar, J., Dublang, L., Santiago, C., Maréchal, J.-D., Martín-Benito, J., Maestro, M., Fernández-Higuero, J. Á., Orozco, N., Moro, F., Valpuesta, J. M., & Muga, A. (2023). The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-41150-8

Vu, H. H., Behrmann, H., Hanić, M., Jeyasankar, G., Krishnan, S., Dannecker, D., Hammer, C., Gunkel, M., Solov’yov, I. A., Wolf, E., & Behrmann, E. (2023). A marine cryptochrome with an inverse photo-oligomerization mechanism. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-42708-2

Yang, L., Wagner, T., Mechaly, A., Boyko, A., Bruch, E. M., Megrian, D., Gubellini, F., Alzari, P. M., & Bellinzoni, M. (2023). High resolution cryo-EM and crystallographic snapshots of the actinobacterial two-in-one 2-oxoglutarate dehydrogenase. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-40253-6