SerialEM: A Program for Automated Tilt Series Acquisition on Tecnai Microscopes Using Prediction of Specimen Position

Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor

Kim, K., Che, T., Panova, O., DiBerto, J. F., Lyu, J., Krumm, B. E., Wacker, D., Robertson, M. J., Seven, A. B., Nichols, D. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.024 · Cited by 481

CasX enzymes comprise a distinct family of RNA-guided genome editors

Liu, J.-J., Orlova, N., Oakes, B. L., Ma, E., Spinner, H. B., Baney, K. L. M., Chuck, J., Tan, D., Knott, G. J., Harrington, L. B., et al. (2019) · Nature · doi:10.1038/s41586-019-0908-x · Cited by 446

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

Structural basis for the docking of mTORC1 on the lysosomal surface

Rogala, K. B., Gu, X., Kedir, J. F., Abu-Remaileh, M., Bianchi, L. F., Bottino, A. M. S., Dueholm, R., Niehaus, A., Overwijn, D., Fils, A.-C. P., et al. (2019) · Science · doi:10.1126/science.aay0166 · Cited by 220

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

Boyer, D. R., Li, B., Sun, C., Fan, W., Zhou, K., Hughes, M. P., Sawaya, M. R., Jiang, L., & Eisenberg, D. S. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917914117 · Cited by 179

Protein Analysis of Purified Respiratory Syncytial Virus Particles Reveals an Important Role for Heat Shock Protein 90 in Virus Particle Assembly

Radhakrishnan, A., Yeo, D., Brown, G., Myaing, M. Z., Iyer, L. R., Fleck, R., Tan, B.-H., Aitken, J., Sanmun, D., Tang, K., et al. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.001651 · Cited by 114

Cell wall synthesis and remodelling dynamics determine division site architecture and cell shape in Escherichia coli

Navarro, P. P., Vettiger, A., Ananda, V. Y., Llopis, P. M., Allolio, C., Bernhardt, T. G., & Chao, L. H. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01210-z · Cited by 102

The molecular architecture of the nuclear basket

(2024) · doi:10.1016/j.cell.2024.07.020 · Cited by 94

In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts

Cai, S., Wu, Y., Guillén-Samander, A., Hancock-Cerutti, W., Liu, J., & De Camilli, P. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2203769119 · Cited by 93

Molecular basis of proton sensing by G protein-coupled receptors

Howard, M. K., Hoppe, N., Huang, X.-P., Mitrovic, D., Billesbølle, C. B., Macdonald, C. B., Mehrotra, E., Rockefeller Grimes, P., Trinidad, D. D., Delemotte, L., et al. (2025) · Cell · doi:10.1016/j.cell.2024.11.036 · Cited by 77

Cryo-EM Determination of Eravacycline-Bound Structures of the Ribosome and the Multidrug Efflux Pump AdeJ of Acinetobacter baumannii

Zhang, Z., Morgan, C. E., Bonomo, R. A., & Yu, E. W. (2021) · mBio · doi:10.1128/mbio.01031-21 · Cited by 58

Intermediate conformations of CD4-bound HIV-1 Env heterotrimers

Dam, K.-M. A., Fan, C., Yang, Z., & Bjorkman, P. J. (2023) · Nature · doi:10.1038/s41586-023-06639-8 · Cited by 50

Cryo-EM structures reveal high-resolution mechanism of a DNA polymerase sliding clamp loader

Gaubitz, C., Liu, X., Pajak, J., Stone, N. P., Hayes, J. A., Demo, G., & Kelch, B. A. (2022) · eLife · doi:10.7554/elife.74175 · Cited by 50

The structure of apolipoprotein B100 from human low-density lipoprotein

Berndsen, Z. T., & Cassidy, C. K. (2025) · Nature · doi:10.1038/s41586-024-08467-w · Cited by 43

Structural basis of the Integrator complex assembly and association with transcription factors

Razew, M., Fraudeau, A., Pfleiderer, M. M., Linares, R., & Galej, W. P. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.05.009 · Cited by 35

Structure and design of Langya virus glycoprotein antigens

Wang, Z., McCallum, M., Yan, L., Gibson, C. A., Sharkey, W., Park, Y.-J., Dang, H. V., Amaya, M., Person, A., Broder, C. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314990121 · Cited by 32

An amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in S. cerevisiae

(2022) · doi:10.7554/elife.78385 · Cited by 29

Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii

Li, A., You, T., Pang, X., Wang, Y., Tian, L., Li, X., & Liu, Z. (2024) · Nature Communications · doi:10.1038/s41467-024-49532-2 · Cited by 26

StableMARK-decorated microtubules in cells have expanded lattices

de Jager, L., Jansen, K. I., Hoogebeen, R., Akhmanova, A., Kapitein, L. C., Förster, F., & Howes, S. C. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202206143 · Cited by 25

Biochemical profiling and structural basis of ADAR1-mediated RNA editing

Deng, X., Sun, L., Zhang, M., Basavaraj, R., Wang, J., Weng, Y.-L., & Gao, Y. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.017 · Cited by 19

A second DNA binding site on RFC facilitates clamp loading at gapped or nicked DNA

Liu, X., Gaubitz, C., Pajak, J., & Kelch, B. A. (2022) · eLife · doi:10.7554/elife.77483 · Cited by 19

The palisade layer of the poxvirus core is composed of flexible A10 trimers

(2024) · doi:10.1038/s41594-024-01218-5 · Cited by 18

Mapping the ultrastructural topology of the corynebacterial cell surface

Isbilir, B., Yeates, A., Alva, V., & Bharat, T. A. M. (2025) · PLOS Biology · doi:10.1371/journal.pbio.3003130 · Cited by 18

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

Anger, R., Pieulle, L., Shahin, M., Valette, O., Le Guenno, H., Kosta, A., Pelicic, V., & Fronzes, R. (2023) · Nature Communications · doi:10.1038/s41467-023-42872-5 · Cited by 17

Structural basis for flagellin-induced NAIP5 activation

Paidimuddala, B., Cao, J., & Zhang, L. (2023) · Science Advances · doi:10.1126/sciadv.adi8539 · Cited by 17

Structures of 9-1-1 DNA checkpoint clamp loading at gaps from start to finish and ramification on biology

Zheng, F., Georgescu, R. E., Yao, N. Y., O’Donnell, M. E., & Li, H. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112694 · Cited by 15

Spatial constraints drive amylosome-mediated resistant starch degradation by Ruminococcus bromii in the human colon

Wimmer, B. H., Moraïs, S., Amit, I., Tovar-Herrera, O., Tatli, M., Trautwein-Schult, A., Pfister, B., Zalk, R., Tödtli, P., Simoni, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65800-1 · Cited by 15

Structural mechanisms for VMAT2 inhibition by tetrabenazine

Dalton, M. P., Cheng, M. H., Bahar, I., & Coleman, J. A. (2024) · eLife · doi:10.7554/elife.91973.4 · Cited by 14

Molecular mechanism of PP2A/B55α phosphatase inhibition by IER5

Cao, R., Jones, D. T. D., Pan, L., Yang, A., Wang, S., Padi, S. K. R., Rawson, S., Aster, J. C., & Blacklow, S. C. (2025) · Cell Chemical Biology · doi:10.1016/j.chembiol.2025.03.004 · Cited by 7

Structural and Biochemical Characterization of a Widespread Enterobacterial Peroxidase Encapsulin

(2025) · doi:10.1002/advs.202415827 · Cited by 7

Structural mechanisms for VMAT2 inhibition by tetrabenazine

Dalton, M. P., Cheng, M. H., Bahar, I., & Coleman, J. A. (2023) · doi:10.1101/2023.09.05.556211 · Cited by 6

Assembly and glycosylation of Helicobacter pylori sheathed flagella

Kumar, R., Tachiyama, S., Yu, H., Heydari, S., Guo, J., Botting, J. M., Guo, W., Hoover, T. R., & Liu, J. (2026) · PNAS Nexus · doi:10.1093/pnasnexus/pgag011 · Cited by 6

Roles of multiple TEF30-associated intermediate complexes in the repair and reassembly of photosystem II in Chlamydomonas reinhardtii

Wang, Y., Wang, C., Li, A., & Liu, Z. (2025) · Nature Plants · doi:10.1038/s41477-025-02036-3 · Cited by 5

THE PALISADE LAYER OF THE POXVIRUS CORE IS COMPOSED OF FLEXIBLE A10-TRIMERS

Liu, J., Corroyer-Dulmont, S., Pražák, V., Khusainov, I., Bahrami, K., Welsch, S., Vasishtan, D., Obarska-Kosińska, A., Thorkelsson, S. R., Grunewald, K., et al. (2023) · doi:10.1101/2023.05.24.542031 · Cited by 4

Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins

Stevens, A., Kashyap, S., Crofut, E. H., Wang, S. E., Muratore, K. A., Johnson, P. J., & Zhou, Z. H. (2025) · Nature Communications · doi:10.1038/s41467-025-59369-y · Cited by 4

MagIC-Cryo-EM, structural determination on magnetic beads for scarce macromolecules in heterogeneous samples

Arimura, Y., Konishi, H. A., & Funabiki, H. (2025) · eLife · doi:10.7554/elife.103486.3 · Cited by 4

In situ architecture of the Tad pilus machine in Caulobacter crescentus

Iarocci, J., Whitfield, G. B., Williston, R. F., Wozny, M. R., Basu, K., Presley, J. F., Ellison, C. K., Brun, Y. V., & Guo, S. (2026) · mBio · doi:10.1128/mbio.00111-26 · Cited by 3

Segmented filamentous bacteria undergo a structural transition at their adhesive tip during unicellular to filament development

Cruz, A. R., Wimmer, B. H., Teo, T. H., Pehau-Arnaudet, G., Winter, J.-M., Gazi, A. D., Lafaye, P., Brier, S., Legrand, A., Dubrovsky-Gaupp, A., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66892-5 · Cited by 3

The bile acid-sensitive ion channel is gated by Ca2+-dependent conformational changes in the transmembrane domain

(2025) · doi:10.1038/s41467-025-62038-9 · Cited by 3

Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape

(2026) · doi:10.1126/science.aea6343 · Cited by 3

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

(2023) · doi:10.1101/2023.06.15.545089

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

(2023) · doi:10.21203/rs.3.rs-3068972/v1

Structural mechanisms for VMAT2 inhibition by tetrabenazine

Dalton, M. P., Cheng, M. H., Bahar, I., & Coleman, J. A. (2024) · doi:10.7554/elife.91973.3