| MAP7 family proteins regulate kinesin-1 recruitment and activation
Hooikaas, P. J., Martin, M., Mühlethaler, T., Kuijntjes, G. J., Peeters, C. A. E., Katrukha, E. A., … Akhmanova, A. (2019). MAP7 family proteins regulate kinesin-1 recruitment and activation. Journal of Cell Biology, 218(4), 1298-1318. https://doi.org/10.1083/jcb.201808065 |
| GEF-H1 signaling upon microtubule destabilization is required for dendritic cell activation and specific anti-tumor responses
Kashyap, A. S., Fernandez-Rodriguez, L., Zhao, Y., Monaco, G., Trefny, M. P., Yoshida, N., … Zippelius, A. (2019). GEF-H1 signaling upon microtubule destabilization is required for dendritic cell activation and specific anti-tumor responses. Cell Reports, 28(13), 3367-3380.e1. https://doi.org/10.1016/j.celrep.2019.08.057 |
| Structure, thermodynamics, and kinetics of plinabulin binding to two tubulin isotypes
La Sala, G., Olieric, N., Sharma, A., Viti, F., de Asis Balaguer Perez, F., Huang, L., … Cavalli, A. (2019). Structure, thermodynamics, and kinetics of plinabulin binding to two tubulin isotypes. Chem, 5(11), 2969-2986. https://doi.org/10.1016/j.chempr.2019.08.022 |
| VISAGE reveals a targetable mitotic spindle vulnerability in cancer cells
Patterson, J. C., Joughin, B. A., Prota, A. E., Mühlethaler, T., Jonas, O. H., Whitman, M. A., … Yaffe, M. B. (2019). VISAGE reveals a targetable mitotic spindle vulnerability in cancer cells. Cell Systems, 9(1), 74-92.e8. https://doi.org/10.1016/j.cels.2019.05.009 |
| Taxanes convert regions of perturbed microtubule growth into rescue sites
Rai, A., Liu, T., Glauser, S., Katrukha, E. A., Estévez-Gallego, J., Rodríguez-García, R., … Akhmanova, A. (2019). Taxanes convert regions of perturbed microtubule growth into rescue sites. Nature Materials, 19, 355-365. https://doi.org/10.1038/s41563-019-0546-6 |
| Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex
Wang, N., Bosc, C., Ryul Choi, S., Boulan, B., Peris, L., Olieric, N., … Huang, H. (2019). Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex. Nature Structural and Molecular Biology, 26(7), 571-582. https://doi.org/10.1038/s41594-019-0241-y |
| Crystal structure of the cyclostreptin-tubulin adduct: implications for tubulin activation by taxane-site ligands
de Asís Balaguer, F., Mühlethaler, T., Estévez-Gallego, J., Calvo, E., Giménez-Abián, J., Risinger, A. L., … Díaz, J. F. (2019). Crystal structure of the cyclostreptin-tubulin adduct: implications for tubulin activation by taxane-site ligands. International Journal of Molecular Sciences, 20(6), 1392 (17 pp.). https://doi.org/10.3390/ijms20061392 |
| CLASP suppresses microtubule catastrophes through a single TOG domain
Aher, A., Kok, M., Sharma, A., Rai, A., Olieric, N., Rodriguez-Garcia, R., … Akhmanova, A. (2018). CLASP suppresses microtubule catastrophes through a single TOG domain. Developmental Cell, 46(1), 40-58.e8. https://doi.org/10.1016/j.devcel.2018.05.032 |
| Interaction between the <em>Caenorhabditis elegans</em> centriolar protein SAS-5 and microtubules facilitates organelle assembly
Bianchi, S., Rogala, K. B., Dynes, N. J., Hilbert, M., Leidel, S. A., Steinmetz, M. O., … Vakonakis, I. (2018). Interaction between the Caenorhabditis elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly. Molecular Biology of the Cell, 29(6), 722-735. https://doi.org/10.1091/mbc.E17-06-0412 |
| High-affinity ligands of the colchicine domain in tubulin based on a structure-guided design
Bueno, O., Estévez Gallego, J., Martins, S., Prota, A. E., Gago, F., Gómez-SanJuan, A., … Priego, E. M. (2018). High-affinity ligands of the colchicine domain in tubulin based on a structure-guided design. Scientific Reports, 8(1), 4242 (17 pp.). https://doi.org/10.1038/s41598-018-22382-x |
| Quinazolinone-based anticancer agents: synthesis, antiproliferative SAR, antitubulin activity, and tubulin Co-crystal structure
Dohle, W., Jourdan, F. L., Menchon, G., Prota, A. E., Foster, P. A., Mannion, P., … Potter, B. V. L. (2018). Quinazolinone-based anticancer agents: synthesis, antiproliferative SAR, antitubulin activity, and tubulin Co-crystal structure. Journal of Medicinal Chemistry, 61(3), 1031-1044. https://doi.org/10.1021/acs.jmedchem.7b01474 |
| Structural basis of formation of the microtubule minus-end-regulating CAMSAP-katanin complex
Jiang, K., Faltova, L., Hua, S., Capitani, G., Prota, A. E., Landgraf, C., … Akhmanova, A. (2018). Structural basis of formation of the microtubule minus-end-regulating CAMSAP-katanin complex. Structure, 26(3), 375-382. https://doi.org/10.1016/j.str.2017.12.017 |
| Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils
Kraatz, S. H. W., Bianchi, S., & Steinmetz, M. O. (2018). Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils. Bioscience Reports, 38(5), BSR20181073 (11 pp.). https://doi.org/10.1042/BSR20181073 |
| A fluorescence anisotropy assay to discover and characterize ligands targeting the maytansine site of tubulin
Menchon, G., Prota, A. E., Lucena-Agell, D., Bucher, P., Jansen, R., Irschik, H., … Steinmetz, M. O. (2018). A fluorescence anisotropy assay to discover and characterize ligands targeting the maytansine site of tubulin. Nature Communications, 9(1), 2106 (9 pp.). https://doi.org/10.1038/s41467-018-04535-8 |
| Cep120 promotes microtubule formation through a unique tubulin binding C2 domain
Sharma, A., Gerard, S. F., Olieric, N., & Steinmetz, M. O. (2018). Cep120 promotes microtubule formation through a unique tubulin binding C2 domain. Journal of Structural Biology, 203(1), 62-70. https://doi.org/10.1016/j.jsb.2018.01.009 |
| Sustainable syntheses of (-)-jerantinines A & E and structural characterisation of the jerantinine-tubulin complex at the colchicine binding site
Smedley, C. J., Stanley, P. A., Qazzaz, M. E., Prota, A. E., Olieric, N., Collins, H., … Moses, J. E. (2018). Sustainable syntheses of (-)-jerantinines A & E and structural characterisation of the jerantinine-tubulin complex at the colchicine binding site. Scientific Reports, 8(1), 10617 (7 pp.). https://doi.org/10.1038/s41598-018-28880-2 |
| Structure-function relationship of the Bik1-Bim1 complex
Stangier, M. M., Kumar, A., Chen, X., Farcas, A. M., Barral, Y., & Steinmetz, M. O. (2018). Structure-function relationship of the Bik1-Bim1 complex. Structure, 26(4), 607-618.e4. https://doi.org/10.1016/j.str.2018.03.003 |
| Microtubule-targeting agents: strategies to hijack the cytoskeleton
Steinmetz, M. O., & Prota, A. E. (2018). Microtubule-targeting agents: strategies to hijack the cytoskeleton. Trends in Cell Biology, 28(10), 776-792. https://doi.org/10.1016/j.tcb.2018.05.001 |
| A structural model for microtubule minus-end recognition and protection by CAMSAP proteins
Atherton, J., Jiang, K., Stangier, M. M., Luo, Y., Hua, S., Houben, K., … Akhmanova, A. (2017). A structural model for microtubule minus-end recognition and protection by CAMSAP proteins. Nature Structural and Molecular Biology, 24(11), 931-943. https://doi.org/10.1038/nsmb.3483 |
| Deconvolution of buparlisib's mechanism of action defines specific PI3K and tubulin inhibitors for therapeutic intervention
Bohnacker, T., Prota, A. E., Beaufils, F., Burke, J. E., Melone, A., Inglis, A. J., … Wymann, M. P. (2017). Deconvolution of buparlisib's mechanism of action defines specific PI3K and tubulin inhibitors for therapeutic intervention. Nature Communications, 8, 14683 (13 pp.). https://doi.org/10.1038/ncomms14683 |