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EMAN2: An extensible image processing suite for electron microscopy
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Cites
Structure of the human transferrin receptor-transferrin complex
Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571
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
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RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
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
Khalifa, A. A. Z., Ichikawa, M., Dai, D., Kubo, S., Black, C. S., Peri, K., McAlear, T. S., Veyron, S., Yang, S. K., Vargas, J., et al. (2020) · eLife · doi:10.7554/elife.52760 · Cited by 1,676
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
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
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
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
Self-citationThe Molecular Architecture for RNA-Guided RNA Cleavage by Cas13a
Liu, L., Li, X., Ma, J., Li, Z., You, L., Wang, J., Wang, M., Zhang, X., & Wang, Y. (2017) · Cell · doi:10.1016/j.cell.2017.06.050 · Cited by 538
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
The crystal structure of Cpf1 in complex with CRISPR RNA
Dong, D., Ren, K., Qiu, X., Zheng, J., Guo, M., Guan, X., Liu, H., Li, N., Zhang, B., Yang, D., et al. (2016) · Nature · doi:10.1038/nature17944 · Cited by 430
Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
Verba, K. A., Wang, R. Y.-R., Arakawa, A., Liu, Y., Shirouzu, M., Yokoyama, S., & Agard, D. A. (2016) · Science · doi:10.1126/science.aaf5023 · Cited by 424
The structure of the dynactin complex and its interaction with dynein
Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., Patel, N. A., Robinson, C. V., & Carter, A. P. (2015) · Science · doi:10.1126/science.aaa4080 · Cited by 421
Near-atomic model of microtubule-tau interactions
Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416
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
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
In-cell architecture of an actively transcribing-translating expressome
O’Reilly, F. J., Xue, L., Graziadei, A., Sinn, L., Lenz, S., Tegunov, D., Blötz, C., Singh, N., Hagen, W. J. H., Cramer, P., et al. (2020) · Science · doi:10.1126/science.abb3758 · Cited by 284
Covalently circularized nanodiscs for studying membrane proteins and viral entry
Nasr, M. L., Baptista, D., Strauss, M., Sun, Z.-Y. J., Grigoriu, S., Huser, S., Plückthun, A., Hagn, F., Walz, T., Hogle, J. M., et al. (2017) · Nature Methods · doi:10.1038/nmeth.4079 · Cited by 262
Proteins evolve on the edge of supramolecular self-assembly
Garcia-Seisdedos, H., Empereur-Mot, C., Elad, N., & Levy, E. D. (2017) · Nature · doi:10.1038/nature23320 · Cited by 253
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
Structural basis for regulation of human acetyl-CoA carboxylase
Hunkeler, M., Hagmann, A., Stuttfeld, E., Chami, M., Guri, Y., Stahlberg, H., & Maier, T. (2018) · Nature · doi:10.1038/s41586-018-0201-4 · Cited by 229
The guidance receptor plexin D1 is a mechanosensor in endothelial cells
Mehta, V., Pang, K.-L., Rozbesky, D., Nather, K., Keen, A., Lachowski, D., Kong, Y., Karia, D., Ameismeier, M., Huang, J., et al. (2020) · Nature · doi:10.1038/s41586-020-1979-4 · Cited by 221
Structural basis for the recognition of Sonic Hedgehog by human Patched1
Gong, X., Qian, H., Cao, P., Zhao, X., Zhou, Q., Lei, J., & Yan, N. (2018) · Science · doi:10.1126/science.aas8935 · Cited by 216
Zhang, K., Zheludev, I. N., Hagey, R. J., Haslecker, R., Hou, Y. J., Kretsch, R., Pintilie, G. D., Rangan, R., Kladwang, W., Li, S., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00653-y · Cited by 189
Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
Howes, S. C., Alushin, G. M., Shida, T., Nachury, M. V., & Nogales, E. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0387 · Cited by 183
Comprehensive structure and functional adaptations of the yeast nuclear pore complex
Akey, C. W., Singh, D., Ouch, C., Echeverria, I., Nudelman, I., Varberg, J. M., Yu, Z., Fang, F., Shi, Y., Wang, J., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.015 · Cited by 180
Self-citationThe 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
Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation
Lü, W., Du, J., Goehring, A., & Gouaux, E. (2017) · Science · doi:10.1126/science.aal3729 · Cited by 176
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
Structure of a CLC chloride ion channel by cryo-electron microscopy
Park, E., Campbell, E. B., & MacKinnon, R. (2017) · Nature · doi:10.1038/nature20812 · Cited by 164
Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes
Yu, X., Yi, P., Hamilton, R. A., Shen, H., Chen, M., Foulds, C. E., Mancini, M. A., Ludtke, S. J., Wang, Z., & O’Malley, B. W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.031 · Cited by 154
Self-citationCryo-EM structure of the exocyst complex
Mei, K., Li, Y., Wang, S., Shao, G., Wang, J., Ding, Y., Luo, G., Yue, P., Liu, J.-J., Wang, X., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0016-2 · Cited by 156
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
Self-citationStructure of the STRA6 receptor for retinol uptake
Chen, Y., Clarke, O. B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, M., Godoy-Ruiz, R., von Alpen, D. C., Manzini, C., et al. (2016) · Science · doi:10.1126/science.aad8266 · Cited by 148
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
Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex
Wieczorek, M., Urnavicius, L., Ti, S.-C., Molloy, K. R., Chait, B. T., & Kapoor, T. M. (2020) · Cell · doi:10.1016/j.cell.2019.12.007 · Cited by 136
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 of second-generation HIV integrase inhibitor action and viral resistance
Cook, N. J., Li, W., Berta, D., Badaoui, M., Ballandras-Colas, A., Nans, A., Kotecha, A., Rosta, E., Engelman, A. N., & Cherepanov, P. (2020) · Science · doi:10.1126/science.aay4919 · Cited by 108
Beckham, K. S. H., Ciccarelli, L., Bunduc, C. M., Mertens, H. D. T., Ummels, R., Lugmayr, W., Mayr, J., Rettel, M., Savitski, M. M., Svergun, D. I., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.47 · Cited by 112
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
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
Structural differences between yeast and mammalian microtubules revealed by cryo-EM
Howes, S. C., Geyer, E. A., LaFrance, B., Zhang, R., Kellogg, E. H., Westermann, S., Rice, L. M., & Nogales, E. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612195 · Cited by 89
Young, L. N., Cho, K., Lawrence, R., Zoncu, R., & Hurley, J. H. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603650113 · 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
Structural Definition of a Neutralization-sensitive Epitope on the MERS-CoV S1-NTD
Wang, N., Rosen, O., Wang, L., Turner, H. L., Stevens, L. J., Corbett, K. S., Bowman, C. A., Pallesen, J., Shi, W., Zhang, Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.052 · Cited by 86
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
Structural basis of BRCC36 function in DNA repair and immune regulation
Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84
De novo modeling in cryo-EM density maps with Pathwalking
Chen, M., Baldwin, P. R., Ludtke, S. J., & Baker, M. L. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.06.004 · Cited by 82
The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth
Chaaban, S., Jariwala, S., Hsu, C.-T., Redemann, S., Kollman, J. M., Müller-Reichert, T., Sept, D., Bui, K. H., & Brouhard, G. J. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.08.023 · Cited by 83
DeepCryoPicker: fully automated deep neural network for single protein particle picking in cryo-EM
Al-Azzawi, A., Ouadou, A., Max, H., Duan, Y., Tanner, J. J., & Cheng, J. (2020) · BMC Bioinformatics · doi:10.1186/s12859-020-03809-7 · Cited by 74
Progressive assembly of multi-domain protein structures from cryo-EM density maps
Zhou, X., Li, Y., Zhang, C., Zheng, W., Zhang, G., & Zhang, Y. (2022) · Nature Computational Science · doi:10.1038/s43588-022-00232-1 · Cited by 75
Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation
Linares, R., Arnaud, C.-A., Effantin, G., Darnault, C., Epalle, N. H., Boeri Erba, E., Schoehn, G., & Breyton, C. (2023) · Science Advances · doi:10.1126/sciadv.ade9674 · Cited by 75
Structural insights into the mechanism of human NPC1L1-mediated cholesterol uptake
Hu, M., Yang, F., Huang, Y., You, X., Liu, D., Sun, S., & Sui, S.-F. (2021) · Science Advances · doi:10.1126/sciadv.abg3188 · Cited by 72
Architecture of an HIV-1 reverse transcriptase initiation complex
Larsen, K. P., Mathiharan, Y. K., Kappel, K., Coey, A. T., Chen, D.-H., Barrero, D., Madigan, L., Puglisi, J. D., Skiniotis, G., & Puglisi, E. V. (2018) · Nature · doi:10.1038/s41586-018-0055-9 · Cited by 66
Kalluri, V. S., Smaglo, B. G., Mahadevan, K. K., Kirtley, M. L., McAndrews, K. M., Mendt, M., Yang, S., Maldonado, A. S., Sugimoto, H., Salvatierra, M. E., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63718-2 · Cited by 70
Self-citationRhodopsin–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
“selected using the auto-boxing feature of EMAN2 (Tang et al., 2007) for particle size statistics and manually for 3D reconstruction.”
InfluentialTsybovsky, Y., Orban, T., Molday, R. S., Taylor, D., & Palczewski, K. (2013) · Structure · doi:10.1016/j.str.2013.03.001 · Cited by 53
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis.
Alvira, S., Watkins, D. W., Troman, L. A., Allen, W. J., Lorriman, J. S., Degliesposti, G., Cohen, E. J., Beeby, M., Daum, B., Gold, V. A., et al. (2020) · eLife · doi:10.7554/elife.60669 · Cited by 51
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(2024) · doi:10.1038/s41586-024-07508-8 · Cited by 51
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
Jose, A., Mietzsch, M., Smith, J. K., Kurian, J., Chipman, P., McKenna, R., Chiorini, J., & Agbandje-McKenna, M. (2019) · Journal of Virology · doi:10.1128/jvi.01394-18 · Cited by 44
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Leisico, F., Omeiri, J., Le Narvor, C., Beaudouin, J., Hons, M., Fenel, D., Schoehn, G., Couté, Y., Bonnaffé, D., Sadir, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34882-6 · Cited by 45
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Zinder, J. C., Olinares, P. D. B., Svetlov, V., Bush, M. W., Nudler, E., Chait, B. T., Walz, T., & de Lange, T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201662119 · Cited by 44
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Jastrzebska, B., Ringler, P., Palczewski, K., & Engel, A. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.02.014 · Cited by 42
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Wang, A., Zhou, F., Liu, C., Gao, D., Qi, R., Yin, Y., Liu, S., Gao, Y., Fu, L., Xia, Y., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00374-6 · Cited by 41
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Subramanian, S., Maurer, A. C., Bator, C. M., Makhov, A. M., Conway, J. F., Turner, K. B., Marden, J. H., Vandenberghe, L. H., & Hafenstein, S. L. (2019) · Human Gene Therapy · doi:10.1089/hum.2019.041 · Cited by 40
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
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Sun, W. W., Michalak, D. J., Sochacki, K. A., Kunamaneni, P., Alfonzo-Méndez, M. A., Arnold, A. M., Strub, M.-P., Hinshaw, J. E., & Taraska, J. W. (2025) · Nature Communications · doi:10.1038/s41467-025-56045-z · Cited by 35
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Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., & Jiang, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059817 · Cited by 34
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“[PubMed: 30194371] Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, Ludtke SJ, 2007 EMAN2: an extensible image processing suite for electron microscopy.”
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Levy, A., Raghu, R., Feathers, J. R., Grzadkowski, M., Poitevin, F., Johnston, J. D., Vallese, F., Clarke, O. B., Wetzstein, G., & Zhong, E. D. (2025) · Nature Methods · doi:10.1038/s41592-025-02720-4 · Cited by 25
Vahedi-Faridi, A., Jastrzebska, B., Palczewski, K., & Engel, A. (2013) · Microscopy · doi:10.1093/jmicro/dfs091 · Cited by 24
De Nardis, C., Lössl, P., van den Biggelaar, M., Madoori, P. K., Leloup, N., Mertens, K., Heck, A. J. R., & Gros, P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.758862 · Cited by 24
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Anton, L., Cheng, W., Haile, M. T., Dziekan, J. M., Cobb, D. W., Zhu, X., Han, L., Li, E., Nair, A., Lee, C. L., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01632-3 · Cited by 21
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Metadata
- Authors
- Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., & Ludtke, S. J.
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2007-01
- Volume
- 157
- Issue
- 1
- Pages
- 38-46
- ISSN
- 1047-8477 (ISSN-L)
- OpenAlex
- W2100455255
- Cited by
- 2,994
- References
- 2
- FWCI
- 3.98
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.