SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields

Pore-forming activity and structural autoinhibition of the gasdermin family

Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771

Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes

Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schröder, G. F., Fitzgerald, K. A., Wu, H., & Egelman, E. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.008 · Cited by 1,353

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

A ratchet-like inter-subunit reorganization of the ribosome during translocation

Frank, J., & Agrawal, R. K. (2000) · Nature · doi:10.1038/35018597 · Cited by 799

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

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

Structural organization of authentic, mature HIV‐1 virions and cores

Briggs, J. A. G., Wilk, T., Welker, R., Kräusslich, H., & Fuller, S. D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg143 · Cited by 496

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

The mitochondrial inner membrane protein mitofilin controls cristae morphology

John, G. B., Shang, Y., Li, L., Renken, C., Mannella, C. A., Selker, J. M. L., Rangell, L., Bennett, M. J., & Zha, J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0697 · Cited by 440

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 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

Cryo-EM structures of the TMEM16A calcium-activated chloride channel

Dang, S., Feng, S., Tien, J., Peters, C. J., Bulkley, D., Lolicato, M., Zhao, J., Zuberbühler, K., Ye, W., Qi, L., et al. (2017) · Nature · doi:10.1038/nature25024 · Cited by 333

Acetylation-Mediated Proteasomal Degradation of Core Histones during DNA Repair and Spermatogenesis

Qian, M.-X., Pang, Y., Liu, C. H., Haratake, K., Du, B.-Y., Ji, D.-Y., Wang, G.-F., Zhu, Q.-Q., Song, W., Yu, Y., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.032 · Cited by 330

Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.

Frauenfeld, J., Gumbart, J., Sluis, E. O. V. D., Funes, S., Gartmann, M., Beatrix, B., Mielke, T., Berninghausen, O., Becker, T., Schulten, K., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2026 · Cited by 298

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

Structure of a 14-3-3 Coordinated Hexamer of the Plant Plasma Membrane H+-ATPase by Combining X-Ray Crystallography and Electron Cryomicroscopy

Ottmann, C., Marco, S., Jaspert, N., Marcon, C., Schauer, N., Weyand, M., Vandermeeren, C., Duby, G., Boutry, M., Wittinghofer, A., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.017 · Cited by 255

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

Quaternary Structure, Protein Dynamics, and Synaptic Function of SAP97 Controlled by L27 Domain Interactions

Nakagawa, T., Futai, K., Lashuel, H. A., Lo, I., Okamoto, K., Walz, T., Hayashi, Y., & Sheng, M. (2004) · Neuron · doi:10.1016/j.neuron.2004.10.012 · Cited by 250

The scanning electron microscope in microbiology and diagnosis of infectious disease

Golding, C. G., Lamboo, L. L., Beniac, D. R., & Booth, T. F. (2016) · Scientific Reports · doi:10.1038/srep26516 · Cited by 236

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

Three-Dimensional Analysis of Budding Sites and Released Virus Suggests a Revised Model for HIV-1 Morphogenesis

Carlson, L.-A., Briggs, J. A. G., Glass, B., Riches, J. D., Simon, M. N., Johnson, M. C., Müller, B., Grünewald, K., & Kräusslich, H.-G. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.10.013 · Cited by 230

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

Structural basis for TetM-mediated tetracycline resistance

Dönhöfer, A., Franckenberg, S., Wickles, S., Berninghausen, O., Beckmann, R., & Wilson, D. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208037109 · Cited by 217

Structures of modified eEF2·80S ribosome complexes reveal the role of GTP hydrolysis in translocation

Taylor, D. J., Nilsson, J., Merrill, A. R., Andersen, G. R., Nissen, P., & Frank, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601677 · Cited by 193

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190

Crystal structure of a soluble CD28-Fab complex

Evans, E. J., Esnouf, R. M., Manso-Sancho, R., Gilbert, R. J. C., James, J. R., Yu, C., Fennelly, J. A., Vowles, C., Hanke, T., Walse, B., et al. (2005) · Nature Immunology · doi:10.1038/ni1170 · Cited by 180

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

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

SecM-Stalled Ribosomes Adopt an Altered Geometry at the Peptidyl Transferase Center

Bhushan, S., Hoffmann, T., Seidelt, B., Frauenfeld, J., Mielke, T., Berninghausen, O., Wilson, D. N., & Beckmann, R. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000581 · Cited by 154

Relating conformation to function in integrin α 5 β 1

Su, Y., Xia, W., Li, J., Walz, T., Humphries, M. J., Vestweber, D., Cabañas, C., Lu, C., & Springer, T. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605074113 · Cited by 146

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 E. coli signal recognition particle bound to a translating ribosome.

Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I., & Ban, N. (2006) · Nature · doi:10.1038/nature05182 · Cited by 136

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

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

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

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

Selective Targeting of TGF-β Activation to Treat Fibroinflammatory Airway Disease

Minagawa, S., Lou, J., Seed, R. I., Cormier, A., Wu, S., Cheng, Y., Murray, L., Tsui, P., Connor, J., Herbst, R., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3008074 · Cited by 90

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

Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20

McCraw, D. M., O’Donnell, J. K., Taylor, K. A., Stagg, S. M., & Chapman, M. S. (2012) · Virology · doi:10.1016/j.virol.2012.05.004 · Cited by 84

Allosteric β1 Integrin Antibodies That Stabilize the Low Affinity State by Preventing the Swing-out of the Hybrid Domain

Luo, B.-H., Strokovich, K., Walz, T., Springer, T. A., & Takagi, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404354200 · Cited by 73

Implementation and performance evaluation of reconstruction algorithms on graphics processors

Castaño Díez, D., Mueller, H., & Frangakis, A. S. (2007) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.08.010 · Cited by 68

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

Molecular Organization and ATP-Induced Conformational Changes of ABCA4, the Photoreceptor-Specific ABC Transporter

Tsybovsky, Y., Orban, T., Molday, R. S., Taylor, D., & Palczewski, K. (2013) · Structure · doi:10.1016/j.str.2013.03.001 · Cited by 53

Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments

Lawrence, L. J., Kortt, A. A., Iliades, P., Tulloch, P. A., & Hudson, P. J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00292-0 · Cited by 50

Protein Synthesis in the Developing Neocortex at Near-Atomic Resolution Reveals Ebp1-Mediated Neuronal Proteostasis at the 60S Tunnel Exit

Kraushar, M. L., Krupp, F., Harnett, D., Turko, P., Ambrozkiewicz, M. C., Sprink, T., Imami, K., Günnigmann, M., Zinnall, U., Vieira-Vieira, C. H., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.11.037 · Cited by 49

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

α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography

Maheshwari, A., Obbineni, J. M., Bui, K. H., Shibata, K., Toyoshima, Y. Y., & Ishikawa, T. (2015) · Structure · doi:10.1016/j.str.2015.06.017 · Cited by 47

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

AlphaFold as a prior: experimental structure determination conditioned on a pretrained neural network

Fadini, A., Li, M., McCoy, A. J., Banjara, S., Okumura, H., Napier, E., Fontana, P., Khan, A. R., Jovine, L., Terwilliger, T. C., et al. (2026) · Nature Methods · doi:10.1038/s41592-026-03047-4 · Cited by 22

Identification of critical residues in Gap3 of Streptococcus parasanguinis involved in Fap1 glycosylation, fimbrial formation and in vitroadhesion

Peng, Z., Fives-Taylor, P., Ruiz, T., Zhou, M., Sun, B., Chen, Q., & Wu, H. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-52 · Cited by 21

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