SPARX, a new environment for Cryo-EM image processing

Structures of Cas9 endonucleases reveal RNA-mediated conformational activation

Jinek, M., Jiang, F., Taylor, D. W., Sternberg, S. H., Kaya, E., Ma, E., Anders, C., Hauer, M., Zhou, K., Lin, S., et al. (2014) · Science · doi:10.1126/science.1247997 · Cited by 1,230

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

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

Pejchal, R., Doores, K. J., Walker, L. M., Khayat, R., Huang, P.-S., Wang, S.-K., Stanfield, R. L., Julien, J.-P., Ramos, A., Crispin, M., et al. (2011) · Science · doi:10.1126/science.1213256 · Cited by 694

Complete subunit architecture of the proteasome regulatory particle

Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608

A soluble α-synuclein construct forms a dynamic tetramer

Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L. T. T., Liao, J., Auclair, J. R., Johnson, D., Landeru, A., Simorellis, A. K., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113260108 · Cited by 478

Structural Basis of Substrate Recognition by the Multidrug Resistance Protein MRP1

Johnson, Z. L., & Chen, J. (2017) · Cell · doi:10.1016/j.cell.2017.01.041 · Cited by 375

Structural Basis for the RNA-Guided Ribonuclease Activity of CRISPR-Cas13d

Zhang, C., Konermann, S., Brideau, N. J., Lotfy, P., Wu, X., Novick, S. J., Strutzenberg, T., Griffin, P. R., Hsu, P. D., & Lyumkis, D. (2018) · Cell · doi:10.1016/j.cell.2018.09.001 · Cited by 276

NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly

Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L.-M., von Gronau, S., Kleiger, G., & Schulman, B. A. (2020) · Nature · doi:10.1038/s41586-020-2000-y · Cited by 270

A conserved Mediator–CDK8 kinase module association regulates Mediator–RNA polymerase II interaction

Tsai, K.-L., Sato, S., Tomomori-Sato, C., Conaway, R. C., Conaway, J. W., & Asturias, F. J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2549 · Cited by 219

Subunit Architecture and Functional Modular Rearrangements of the Transcriptional Mediator Complex

Tsai, K.-L., Tomomori-Sato, C., Sato, S., Conaway, R. C., Conaway, J. W., & Asturias, F. J. (2014) · Cell · doi:10.1016/j.cell.2014.05.015 · Cited by 218

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

Rac1 GTPase activates the WAVE regulatory complex through two distinct binding sites

Chen, B., Chou, H.-T., Brautigam, C. A., Xing, W., Yang, S., Henry, L., Doolittle, L. K., Walz, T., & Rosen, M. K. (2017) · eLife · doi:10.7554/elife.29795 · Cited by 173

Structural basis for retroviral integration into nucleosomes

Maskell, D. P., Renault, L., Serrao, E., Lesbats, P., Matadeen, R., Hare, S., Lindemann, D., Engelman, A. N., Costa, A., & Cherepanov, P. (2015) · Nature · doi:10.1038/nature14495 · Cited by 138

Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site

Strauch, E.-M., Bernard, S. M., La, D., Bohn, A. J., Lee, P. S., Anderson, C. E., Nieusma, T., Holstein, C. A., Garcia, N. K., Hooper, K. A., et al. (2017) · Nature Biotechnology · doi:10.1038/nbt.3907 · Cited by 119

Structural basis for strand-transfer inhibitor binding to HIV intasomes

Passos, D. O., Li, M., Jóźwik, I. K., Zhao, X. Z., Santos-Martins, D., Yang, R., Smith, S. J., Jeon, Y., Forli, S., Hughes, S. H., et al. (2020) · Science · doi:10.1126/science.aay8015 · Cited by 106

Visualization of the HIV-1 Env glycan shield across scales

Berndsen, Z. T., Chakraborty, S., Wang, X., Cottrell, C. A., Torres, J. L., Diedrich, J. K., López, C. A., Yates, J. R., van Gils, M. J., Paulson, J. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000260117 · Cited by 86

CATCHR, HOPS and CORVET tethering complexes share a similar architecture

Chou, H.-T., Dukovski, D., Chambers, M. G., Reinisch, K. M., & Walz, T. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3264 · Cited by 83

Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface

Jenni, S., & Harrison, S. C. (2018) · Science · doi:10.1126/science.aar6436 · Cited by 72

An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex

Bush, M., Alhanshali, B. M., Qian, S., Stanley, C. B., Heller, W. T., Matsui, T., Weiss, T. M., Nicholl, I. D., Walz, T., Callaway, D. J. E., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911489116 · Cited by 42

An epitope tag alters phosphoglycerate dehydrogenase structure and impairs ability to support cell proliferation

Mattaini, K. R., Brignole, E. J., Kini, M., Davidson, S. M., Fiske, B. P., Drennan, C. L., & Vander Heiden, M. G. (2015) · Cancer & Metabolism · doi:10.1186/s40170-015-0131-7 · Cited by 38

Cryo-EM structure of the HIV-1 Pol polyprotein provides insights into virion maturation

Harrison, J. J. E. K., Passos, D. O., Bruhn, J. F., Bauman, J. D., Tuberty, L., DeStefano, J. J., Ruiz, F. X., Lyumkis, D., & Arnold, E. (2022) · Science Advances · doi:10.1126/sciadv.abn9874 · Cited by 31

Microfibril-associated glycoprotein 4 forms octamers that mediate interactions with elastogenic proteins and cells

Wozny, M. R., Nelea, V., Siddiqui, I. F. S., Wanga, S., de Waard, V., Strauss, M., & Reinhardt, D. P. (2024) · Nature Communications · doi:10.1038/s41467-024-48377-z · Cited by 9