FREALIGN: High-resolution refinement of single particle structures

Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy

Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416

Structure of the human transferrin receptor-transferrin complex

Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571

Molecular model for a complete clathrin lattice from electron cryomicroscopy

Fotin, A., Cheng, Y., Sliz, P., Grigorieff, N., Harrison, S. C., Kirchhausen, T., & Walz, T. (2004) · Nature · doi:10.1038/nature03079 · Cited by 541

cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination

Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626

High-Resolution Microtubule Structures Reveal the Structural Transitions in αβ-Tubulin upon GTP Hydrolysis

Alushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D., & Nogales, E. (2014) · Cell · doi:10.1016/j.cell.2014.03.053 · Cited by 696

Near-atomic model of microtubule-tau interactions

Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416

Structure of the Decorated Ciliary Doublet Microtubule

Ma, M., Stoyanova, M., Rademacher, G., Dutcher, S. K., Brown, A., & Zhang, R. (2019) · Cell · doi:10.1016/j.cell.2019.09.030 · Cited by 290

Conformational switching of the 26S proteasome enables substrate degradation

Matyskiela, M. E., Lander, G. C., & Martin, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2616 · Cited by 251

Cryo-EM structures and atomic model of the HIV-1 strand transfer complex intasome

Passos, D. O., Li, M., Yang, R., Rebensburg, S. V., Ghirlando, R., Jeon, Y., Shkriabai, N., Kvaratskhelia, M., Craigie, R., & Lyumkis, D. (2017) · Science · doi:10.1126/science.aah5163 · Cited by 202

Separating the effects of nucleotide and EB binding on microtubule structure

Zhang, R., LaFrance, B., & Nogales, E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1802637115 · Cited by 160

The role of tubulin–tubulin lattice contacts in the mechanism of microtubule dynamic instability

Manka, S. W., & Moores, C. A. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0087-8 · Cited by 159

Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion

Rosenberg, O. S., Dovala, D., Li, X., Connolly, L., Bendebury, A., Finer-Moore, J., Holton, J., Cheng, Y., Stroud, R. M., & Cox, J. S. (2015) · Cell · doi:10.1016/j.cell.2015.03.040 · Cited by 134

Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport

Shima, T., Morikawa, M., Kaneshiro, J., Kambara, T., Kamimura, S., Yagi, T., Iwamoto, H., Uemura, S., Shigematsu, H., Shirouzu, M., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711178 · Cited by 125

Structural transitions in the GTP cap visualized by cryo-electron microscopy of catalytically inactive microtubules

LaFrance, B. J., Roostalu, J., Henkin, G., Greber, B. J., Zhang, R., Normanno, D., McCollum, C. O., Surrey, T., & Nogales, E. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114994119 · Cited by 100

Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function

Ballandras-Colas, A., Brown, M., Cook, N. J., Dewdney, T. G., Demeler, B., Cherepanov, P., Lyumkis, D., & Engelman, A. N. (2016) · Nature · doi:10.1038/nature16955 · Cited by 98

Native doublet microtubules from Tetrahymena thermophila reveal the importance of outer junction proteins

Kubo, S., Black, C. S., Joachimiak, E., Yang, S. K., Legal, T., Peri, K., Khalifa, A. A. Z., Ghanaeian, A., McCafferty, C. L., Valente-Paterno, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37868-0 · Cited by 93

The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth

Chaaban, S., Jariwala, S., Hsu, C.-T., Redemann, S., Kollman, J. M., Müller-Reichert, T., Sept, D., Bui, K. H., & Brouhard, G. J. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.08.023 · Cited by 83

A microtubule RELION-based pipeline for cryo-EM image processing

Cook, A. D., Manka, S. W., Wang, S., Moores, C. A., & Atherton, J. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2019.10.004 · Cited by 63

Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs

Shigematsu, H., Imasaki, T., Doki, C., Sumi, T., Aoki, M., Uchikubo-Kamo, T., Sakamoto, A., Tokuraku, K., Shirouzu, M., & Nitta, R. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711182 · Cited by 54

Structural determinants of microtubule minus end preference in CAMSAP CKK domains

Atherton, J., Luo, Y., Xiang, S., Yang, C., Rai, A., Jiang, K., Stangier, M., Vemu, A., Cook, A. D., Wang, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13247-6 · Cited by 48

GPU-enabled FREALIGN: Accelerating single particle 3D reconstruction and refinement in Fourier space on graphics processors

Li, X., Grigorieff, N., & Cheng, Y. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.06.010 · Cited by 45

Dimerization of GAS2 mediates crosslinking of microtubules and F-actin

An, J., Imasaki, T., Narita, A., Niwa, S., Sasaki, R., Makino, T., Nitta, R., & Kikkawa, M. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00415-2 · Cited by 5