Visualizing density maps with UCSF Chimera

Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein

Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586

UCSF ChimeraX: Meeting modern challenges in visualization and analysis

Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267

Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody

Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885

Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals

Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853

SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901

Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies

Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795

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

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

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

Billesbølle, C. B., Azumaya, C. M., Kretsch, R. C., Powers, A. S., Gonen, S., Schneider, S., Arvedson, T., Dror, R. O., Cheng, Y., & Manglik, A. (2020) · Nature · doi:10.1038/s41586-020-2668-z · Cited by 344

Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors

Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0334-7 · Cited by 260

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

Structure and conformational dynamics of the human spliceosomal Bact complex

Haselbach, D., Komarov, I., Agafonov, D. E., Hartmuth, K., Graf, B., Dybkov, O., Urlaub, H., Kastner, B., Lührmann, R., & Stark, H. (2018) · Cell · doi:10.1016/j.cell.2018.01.010 · Cited by 218

De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2

Linsky, T. W., Vergara, R., Codina, N., Nelson, J. W., Walker, M. J., Su, W., Barnes, C. O., Hsiang, T.-Y., Esser-Nobis, K., Yu, K., et al. (2020) · Science · doi:10.1126/science.abe0075 · Cited by 216

Structure Basis for Directional R-loop Formation and Substrate Handover Mechanisms in Type I CRISPR-Cas System

Xiao, Y., Luo, M., Hayes, R. P., Kim, J., Ng, S., Ding, F., Liao, M., & Ke, A. (2017) · Cell · doi:10.1016/j.cell.2017.06.012 · Cited by 208

Integrating diverse data for structure determination of macromolecular assemblies

Alber, F., Förster, F., Korkin, D., Topf, M., & Sali, A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.060407.135530 · Cited by 206

BacPROTACs mediate targeted protein degradation in bacteria

Morreale, F. E., Kleine, S., Leodolter, J., Junker, S., Hoi, D. M., Ovchinnikov, S., Okun, A., Kley, J., Kurzbauer, R., Junk, L., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.009 · Cited by 196

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

Plant-made polio type 3 stabilized VLPs-a candidate synthetic polio vaccine

Marsian, J., Fox, H., Bahar, M. W., Kotecha, A., Fry, E. E., Stuart, D. I., Macadam, A. J., Rowlands, D. J., & Lomonossoff, G. P. (2017) · Nature Communications · doi:10.1038/s41467-017-00090-w · Cited by 121

Capsid antibodies to different adeno-associated virus serotypes bind common regions

Gurda, B. L., DiMattia, M. A., Miller, E. B., Bennett, A., McKenna, R., Weichert, W. S., Nelson, C. D., Chen, W.-J., Muzyczka, N., Olson, N. H., et al. (2013) · Journal of Virology · doi:10.1128/jvi.00622-13 · Cited by 127

Structure and Function of Glycosylated Tandem Repeats from Candida albicans Als Adhesins

Frank, A. T., Ramsook, C. B., Otoo, H. N., Tan, C., Soybelman, G., Rauceo, J. M., Gaur, N. K., Klotz, S. A., & Lipke, P. N. (2010) · Eukaryotic Cell · doi:10.1128/ec.00235-09 · Cited by 63

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

Malet, H., Canellas, F., Sawa, J., Yan, J., Thalassinos, K., Ehrmann, M., Clausen, T., & Saibil, H. R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2210 · Cited by 61

Repurposing potential of FDA‐approved and investigational drugs for COVID‐19 targeting SARS‐CoV‐2 spike and main protease and validation by machine learning algorithm

Verma, A. K., & Aggarwal, R. (2021) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13812 · Cited by 54

Mammalian expression of virus-like particles as a proof of principle for next generation polio vaccines

Bahar, M. W., Porta, C., Fox, H., Macadam, A. J., Fry, E. E., & Stuart, D. I. (2021) · npj Vaccines · doi:10.1038/s41541-020-00267-3 · Cited by 42

Cryo-EM structures of HIV-1 trimer bound to CD4-mimetics BNM-III-170 and M48U1 adopt a CD4-bound open conformation

Jette, C. A., Barnes, C. O., Kirk, S. M., Melillo, B., Smith, A. B., & Bjorkman, P. J. (2021) · Nature Communications · doi:10.1038/s41467-021-21816-x · Cited by 38

In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque

(2025) · doi:10.1038/s41564-025-02012-9 · Cited by 28

Structure and host specificity of Staphylococcus epidermidis bacteriophage Andhra

Hawkins, N. C., Kizziah, J. L., Hatoum-Aslan, A., & Dokland, T. (2022) · Science Advances · doi:10.1126/sciadv.ade0459 · Cited by 25

A general computational design strategy for stabilizing viral class I fusion proteins

Gonzalez, K. J., Huang, J., Criado, M. F., Banerjee, A., Tompkins, S. M., Mousa, J. J., & Strauch, E.-M. (2024) · Nature Communications · doi:10.1038/s41467-024-45480-z · Cited by 20

Describing inhibitor specificity for the amino acid transporter LAT1 from metainference simulations

Hutchinson, K., Silva, D. B., Bohlke, J., Clausen, C., Thomas, A. A., Bonomi, M., & Schlessinger, A. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.11.001 · Cited by 18

Cryo-EM of native membranes reveals an intimate connection between the Krebs cycle and aerobic respiration in mycobacteria

Di Trani, J. M., Yu, J., Courbon, G. M., Lobez Rodriguez, A. P., Cheung, C.-Y., Liang, Y., Coupland, C. E., Bueler, S. A., Cook, G. M., Brzezinski, P., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2423761122 · Cited by 16

Cryo-EM reveals the conformational epitope of human monoclonal antibody PAM1.4 broadly reacting with polymorphic malarial protein VAR2CSA

Raghavan, S. S. R., Dagil, R., Lopez-Perez, M., Conrad, J., Bassi, M. R., Quintana, M. D. P., Choudhary, S., Gustavsson, T., Wang, Y., Gourdon, P., et al. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010924 · Cited by 14

Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein

Kizziah, J. L., Mukherjee, A., Parker, L. K., & Dokland, T. (2025) · Structure · doi:10.1016/j.str.2025.03.007 · Cited by 11

Doublet microtubule inner junction protein FAP20 recruits tubulin to the microtubule lattice

(2023) · doi:10.1016/j.str.2023.09.010 · Cited by 9

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

Walker, M. R., Underwood, A., Björnsson, K. H., Raghavan, S. S. R., Bassi, M. R., Binderup, A., Pham, L. V., Ramirez, S., Pinholt, M., Dagil, R., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06951-7 · Cited by 6

Structural basis for EtfD-mediated coupling of β-oxidation and the respiratory chain in mycobacteria

Courbon, G. M., Makarov, V., Cole, S. T., Schnapinger, D., Ehrt, S., & Rubinstein, J. L. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00726-y · Cited by 1