EMAN: Semiautomated Software for High-Resolution Single-Particle Reconstructions

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

The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis

Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222

Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus

McLellan, J. S., Chen, M., Joyce, M. G., Sastry, M., Stewart-Jones, G. B. E., Yang, Y., Zhang, B., Chen, L., Srivatsan, S., Zheng, A., et al. (2013) · Science · doi:10.1126/science.1243283 · Cited by 1,126

A 1.7-kilobase single-stranded DNA that folds into a nanoscale octahedron

Shih, W. M., Quispe, J. D., & Joyce, G. F. (2004) · Nature · doi:10.1038/nature02307 · Cited by 989

Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody

McLellan, J. S., Chen, M., Leung, S., Graepel, K. W., Du, X., Yang, Y., Zhou, T., Baxa, U., Yasuda, E., Beaumont, T., et al. (2013) · Science · doi:10.1126/science.1234914 · Cited by 883

Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy

Shahnawaz, M., Mukherjee, A., Pritzkow, S., Mendez, N., Rabadia, P., Liu, X., Hu, B., Schmeichel, A., Singer, W., Wu, G., et al. (2020) · Nature · doi:10.1038/s41586-020-1984-7 · Cited by 820

Pre-fusion structure of a human coronavirus spike protein

Kirchdoerfer, R. N., Cottrell, C. A., Wang, N., Pallesen, J., Yassine, H. M., Turner, H. L., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2016) · Nature · doi:10.1038/nature17200 · Cited by 765

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

Outcome of the first electron microscopy validation task force meeting

Henderson, R., Sali, A., Baker, M. L., Carragher, B., Devkota, B., Downing, K. H., Egelman, E. H., Feng, Z., Frank, J., Grigorieff, N., et al. (2012) · Structure · doi:10.1016/j.str.2011.12.014 · Cited by 505

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

Structure and control of the actin regulatory WAVE complex

Chen, Z., Borek, D., Padrick, S. B., Gomez, T. S., Metlagel, Z., Ismail, A. M., Umetani, J., Billadeau, D. D., Otwinowski, Z., & Rosen, M. K. (2010) · Nature · doi:10.1038/nature09623 · Cited by 500

Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

Shiau, A. K., Harris, S. F., Southworth, D. R., & Agard, D. A. (2006) · Cell · doi:10.1016/j.cell.2006.09.027 · Cited by 455

Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles

Kirschke, E., Goswami, D., Southworth, D., Griffin, P. R., & Agard, D. A. (2014) · Cell · doi:10.1016/j.cell.2014.04.038 · Cited by 399

Structural insight into autoinhibition and histone H3-induced activation of DNMT3A

Guo, X., Wang, L., Li, J., Ding, Z., Xiao, J., Yin, X., He, S., Shi, P., Dong, L., Li, G., et al. (2015) · Nature · doi:10.1038/nature13899 · Cited by 361

Architecture of human mTOR complex 1

Aylett, C. H. S., Sauer, E., Imseng, S., Boehringer, D., Hall, M. N., Ban, N., & Maier, T. (2016) · Science · doi:10.1126/science.aaa3870 · Cited by 344

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

Functional architecture of the retromer cargo-recognition complex

Hierro, A., Rojas, A. L., Rojas, R., Murthy, N., Effantin, G., Kajava, A. V., Steven, A. C., Bonifacino, J. S., & Hurley, J. H. (2007) · Nature · doi:10.1038/nature06216 · Cited by 286

Cryo-electron microscopy--a primer for the non-microscopist

Milne, J. L. S., Borgnia, M. J., Bartesaghi, A., Tran, E. E. H., Earl, L. A., Schauder, D. M., Lengyel, J., Pierson, J., Patwardhan, A., & Subramaniam, S. (2013) · The FEBS Journal · doi:10.1111/febs.12078 · Cited by 277

Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions

Volkmann, N., Amann, K. J., Stoilova-McPhie, S., Egile, C., Winter, D. C., Hazelwood, L., Heuser, J. E., Li, R., Pollard, T. D., & Hanein, D. (2001) · Science · doi:10.1126/science.1063025 · Cited by 258

Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function

Byeon, I.-J. L., Meng, X., Jung, J., Zhao, G., Yang, R., Ahn, J., Shi, J., Concel, J., Aiken, C., Zhang, P., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.010 · Cited by 253

The cyclin-dependent kinase 8 module sterically blocks Mediator interactions with RNA polymerase II

Elmlund, H., Baraznenok, V., Lindahl, M., Samuelsen, C. O., Koeck, P. J. B., Holmberg, S., Hebert, H., & Gustafsson, C. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607483103 · Cited by 230

WASH and WAVE actin regulators of the Wiskott–Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes

Jia, D., Gomez, T. S., Metlagel, Z., Umetani, J., Otwinowski, Z., Rosen, M. K., & Billadeau, D. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913293107 · Cited by 232

Functional TRIM24 degrader via conjugation of ineffectual bromodomain and VHL ligands

Gechijian, L. N., Buckley, D. L., Lawlor, M. A., Reyes, J. M., Paulk, J., Ott, C. J., Winter, G. E., Erb, M. A., Scott, T. G., Xu, M., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0010-y · Cited by 222

Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies

Garces, F., Sok, D., Kong, L., McBride, R., Kim, H. J., Saye-Francisco, K. F., Julien, J.-P., Hua, Y., Cupo, A., Moore, J. P., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.009 · Cited by 178

Structure of the CRISPR Interference Complex CSM Reveals Key Similarities with Cascade

Rouillon, C., Zhou, M., Zhang, J., Politis, A., Beilsten-Edmands, V., Cannone, G., Graham, S., Robinson, C. V., Spagnolo, L., & White, M. F. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.020 · Cited by 188

The Assembly-Activating Protein Promotes Capsid Assembly of Different Adeno-Associated Virus Serotypes

Sonntag, F., Köther, K., Schmidt, K., Weghofer, M., Raupp, C., Nieto, K., Kuck, A., Gerlach, B., Böttcher, B., Müller, O. J., et al. (2011) · Journal of Virology · doi:10.1128/jvi.05359-11 · Cited by 184

Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion

Diao, J., Grob, P., Cipriano, D. J., Kyoung, M., Zhang, Y., Shah, S., Nguyen, A., Padolina, M., Srivastava, A., Vrljic, M., et al. (2012) · eLife · doi:10.7554/elife.00109 · Cited by 170

3‐D structural and functional characterization of the purified KATP channel complex Kir6.2–SUR1

Mikhailov, M. V., Campbell, J. D., de Wet, H., Shimomura, K., Zadek, B., Collins, R. F., Sansom, M. S., Ford, R. C., & Ashcroft, F. M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600877 · Cited by 168

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

Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1

Chen, Q., Plasencia, M., Li, Z., Mukherjee, S., Patra, D., Chen, C.-L., Klose, T., Yao, X.-Q., Kossiakoff, A. A., Chang, L., et al. (2021) · Nature · doi:10.1038/s41586-021-03721-x · Cited by 152

Structural and Functional Analysis of a β2-Adrenergic Receptor Complex with GRK5

Komolov, K. E., Du, Y., Duc, N. M., Betz, R. M., Rodrigues, J. P. G. L. M., Leib, R. D., Patra, D., Skiniotis, G., Adams, C. M., Dror, R. O., et al. (2017) · Cell · doi:10.1016/j.cell.2017.03.047 · Cited by 152

Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex

Southworth, D. R., & Agard, D. A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.023 · Cited by 143

Structure of the SecY channel during initiation of protein translocation

Park, E., Ménétret, J.-F., Gumbart, J. C., Ludtke, S. J., Li, W., Whynot, A., Rapoport, T. A., & Akey, C. W. (2014) · Nature · doi:10.1038/nature12720 · Cited by 148

The beginning of kinesin's force-generating cycle visualized at 9-Å resolution

Sindelar, C. V., & Downing, K. H. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612090 · Cited by 139

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

Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity

Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., et al. (2013) · Nature Communications · doi:10.1038/ncomms3416 · Cited by 119

Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon

Jomaa, A., Boehringer, D., Leibundgut, M., & Ban, N. (2016) · Nature Communications · doi:10.1038/ncomms10471 · Cited by 115

An Endoplasmic Reticulum (ER) Membrane Complex Composed of SPFH1 and SPFH2 Mediates the ER-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

Pearce, M. M. P., Wormer, D. B., Wilkens, S., & Wojcikiewicz, R. J. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809801200 · Cited by 114

Leucine-Rich Repeat Kinase 2 Binds to Neuronal Vesicles through Protein Interactions Mediated by Its C-Terminal WD40 Domain

Piccoli, G., Onofri, F., Cirnaru, M. D., Kaiser, C. J. O., Jagtap, P., Kastenmüller, A., Pischedda, F., Marte, A., von Zweydorf, F., Vogt, A., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00914-13 · Cited by 113

Ribosome binding of a single copy of the SecY complex: implications for protein translocation.

Ménétret, J.-F., Schaletzky, J., Clemons, W. M., Osborne, A. R., Skånland, S. S., Denison, C., Gygi, S. P., Kirkpatrick, D. S., Park, E., Ludtke, S. J., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.034 · Cited by 108

The 3.2-Å resolution structure of human mTORC2

Scaiola, A., Mangia, F., Imseng, S., Boehringer, D., Berneiser, K., Shimobayashi, M., Stuttfeld, E., Hall, M. N., Ban, N., & Maier, T. (2020) · Science Advances · doi:10.1126/sciadv.abc1251 · Cited by 105

FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella in Chlamydomonas

Yanagisawa, H.-A., Mathis, G., Oda, T., Hirono, M., Richey, E. A., Ishikawa, H., Marshall, W. F., Kikkawa, M., & Qin, H. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-08-0464 · Cited by 89

Structural and functional characterization of the Spo11 core complex

Claeys Bouuaert, C., Tischfield, S. E., Pu, S., Mimitou, E. P., Arias-Palomo, E., Berger, J. M., & Keeney, S. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00534-w · Cited by 87

Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements

Toropova, K., Mladenov, M., & Roberts, A. J. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3391 · Cited by 85

The Structures of Frataxin Oligomers Reveal the Mechanism for the Delivery and Detoxification of Iron

Karlberg, T., Schagerlöf, U., Gakh, O., Park, S., Ryde, U., Lindahl, M., Leath, K., Garman, E., Isaya, G., & Al-Karadaghi, S. (2006) · Structure · doi:10.1016/j.str.2006.08.010 · Cited by 85

Cryo‐EM model validation using independent map reconstructions

DiMaio, F., Zhang, J., Chiu, W., & Baker, D. (2013) · Protein Science · doi:10.1002/pro.2267 · Cited by 72

High-Resolution Cryo-Electron Microscopy Structures of Murine Norovirus 1 and Rabbit Hemorrhagic Disease Virus Reveal Marked Flexibility in the Receptor Binding Domains

Katpally, U., Voss, N. R., Cavazza, T., Taube, S., Rubin, J. R., Young, V. L., Stuckey, J., Ward, V. K., Virgin, H. W., Wobus, C. E., et al. (2010) · Journal of Virology · doi:10.1128/jvi.00314-10 · Cited by 77

Albumin-binding adenoviruses circumvent pre-existing neutralizing antibodies upon systemic delivery

Rojas, L. A., Condezo, G. N., Moreno, R., Fajardo, C. A., Arias-Badia, M., San Martín, C., & Alemany, R. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.07.004 · Cited by 66

Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.

Jomaa, A., Fu, Y.-H. H., Boehringer, D., Leibundgut, M., Shan, S.-O., & Ban, N. (2017) · Nature Communications · doi:10.1038/ncomms15470 · Cited by 66

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

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

Rhodopsin–transducin heteropentamer: Three-dimensional structure and biochemical characterization

Jastrzebska, B., Ringler, P., Lodowski, D. T., Moiseenkova-Bell, V., Golczak, M., Müller, S. A., Palczewski, K., & Engel, A. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.08.016 · Cited by 57

The Cryo-Electron Microscopy Structure of Feline Calicivirus Bound to Junctional Adhesion Molecule A at 9-Angstrom Resolution Reveals Receptor-Induced Flexibility and Two Distinct Conformational Changes in the Capsid Protein VP1

Bhella, D., & Goodfellow, I. G. (2011) · Journal of Virology · doi:10.1128/jvi.05621-11 · Cited by 55

Origin of the Reflectin Gene and Hierarchical Assembly of Its Protein

Guan, Z., Cai, T., Liu, Z., Dou, Y., Hu, X., Zhang, P., Sun, X., Li, H., Kuang, Y., Zhai, Q., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.07.061 · Cited by 52

Lipidated apolipoprotein E4 structure and its receptor binding mechanism determined by a combined cross-linking coupled to mass spectrometry and molecular dynamics approach

Henry, N., Krammer, E.-M., Stengel, F., Adams, Q., Van Liefferinge, F., Hubin, E., Chaves, R., Efremov, R., Aebersold, R., Vandenbussche, G., et al. (2018) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1006165 · Cited by 42

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

Hildenbrand, Z. L., Molugu, S. K., Herrera, N., Ramirez, C., Xiao, C., & Bernal, R. A. (2011) · Oncotarget · doi:10.18632/oncotarget.225 · Cited by 38

Cryo-EM Structure of a Novel Calicivirus, Tulane Virus

Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., & Jiang, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059817 · Cited by 34

Complex structure of the fission yeast SREBP-SCAP binding domains reveals an oligomeric organization

Gong, X., Qian, H., Shao, W., Li, J., Wu, J., Liu, J.-J., Li, W., Wang, H.-W., Espenshade, P., & Yan, N. (2016) · Cell Research · doi:10.1038/cr.2016.123 · Cited by 31

In Vitro Assembly of Virus-Like Particles of a Gammaretrovirus, the Murine Leukemia Virus XMRV

Hadravová, R., de Marco, A., Ulbrich, P., Štokrová, J., Doležal, M., Pichová, I., Ruml, T., Briggs, J. A. G., & Rumlová, M. (2012) · Journal of Virology · doi:10.1128/jvi.05564-11 · Cited by 26

Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores

Datler, J., Hansen, J. M., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V., & Schur, F. K. M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01201-6 · Cited by 23

Antibodies from dengue patients with prior exposure to Japanese encephalitis virus are broadly neutralizing against Zika virus

Salem, G. M., Galula, J. U., Wu, S.-R., Liu, J.-H., Chen, Y.-H., Wang, W.-H., Wang, S.-F., Song, C.-S., Chen, F.-C., Abarientos, A. B., et al. (2024) · Communications Biology · doi:10.1038/s42003-023-05661-w · Cited by 14

Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures

Conley, M., Emmott, E., Orton, R., Taylor, D., Carneiro, D. G., Murata, K., Goodfellow, I. G., Hansman, G. S., & Bhella, D. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000658 · Cited by 8