The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
3D variability analysis: Resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM
Open accessOverview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Maximum Likelihood from Incomplete Data Via the EM Algorithm
Dempster, A. P., Laird, N. M., & Rubin, D. B. (1977) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1977.tb01600.x · Cited by 50,444
Golub, G. (2012) · doi:10.56021/9781421407944 · Cited by 34,505
Auto-Encoding Variational Bayes
Kingma, D. P., & Welling, M. (2013) · arXiv · doi:10.48550/arxiv.1312.6114 · Cited by 20,067
UMAP: Uniform Manifold Approximation and Projection
McInnes, L., Healy, J., Saul, N., & Großberger, L. (2018) · Journal of Open Source Software · doi:10.21105/joss.00861 · Cited by 9,826
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
A View of the Em Algorithm that Justifies Incremental, Sparse, and other Variants
Neal, R. M., & Hinton, G. E. (1998) · Learning in Graphical Models · doi:10.1007/978-94-011-5014-9_12 · Cited by 2,187
Structure and dynamics of GPCR signaling complexes
Hilger, D., Masureel, M., & Kobilka, B. K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0011-7 · Cited by 969
Cited by
Hallucinating symmetric protein assemblies
Wicky, B. I. M., Milles, L. F., Courbet, A., Ragotte, R. J., Dauparas, J., Kinfu, E., Tipps, S., Kibler, R. D., Baek, M., DiMaio, F., et al. (2022) · Science · doi:10.1126/science.add1964 · Cited by 240
Structure of the bacterial ribosome at 2 Å resolution
Watson, Z. L., Ward, F. R., Méheust, R., Ad, O., Schepartz, A., Banfield, J. F., & Cate, J. H. (2020) · eLife · doi:10.7554/elife.60482 · Cited by 263
Targeting cancer with small-molecule pan-KRAS degraders
Popow, J., Farnaby, W., Gollner, A., Kofink, C., Fischer, G., Wurm, M., Zollman, D., Wijaya, A., Mischerikow, N., Hasenoehrl, C., et al. (2024) · Science · doi:10.1126/science.adm8684 · Cited by 198
Cyclic nucleotide-induced helical structure activates a TIR immune effector
Hogrel, G., Guild, A., Graham, S., Rickman, H., Grüschow, S., Bertrand, Q., Spagnolo, L., & White, M. F. (2022) · Nature · doi:10.1038/s41586-022-05070-9 · Cited by 129
Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients
Miller-Vedam, L. E., Bräuning, B., Popova, K. D., Schirle Oakdale, N. T., Bonnar, J. L., Prabu, J. R., Boydston, E. A., Sevillano, N., Shurtleff, M. J., Stroud, R. M., et al. (2020) · eLife · doi:10.7554/elife.62611 · Cited by 87
How Pol α-primase is targeted to replisomes to prime eukaryotic DNA replication
Jones, M. L., Aria, V., Baris, Y., & Yeeles, J. T. P. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.035 · Cited by 86
Structural basis for membrane attack complex inhibition by CD59
Couves, E. C., Gardner, S., Voisin, T. B., Bickel, J. K., Stansfeld, P. J., Tate, E. W., & Bubeck, D. (2023) · Nature Communications · doi:10.1038/s41467-023-36441-z · Cited by 85
Structures of the holo CRISPR RNA-guided transposon integration complex
Park, J.-U., Tsai, A. W.-L., Rizo, A. N., Truong, V. H., Wellner, T. X., Schargel, R. D., & Kellogg, E. H. (2023) · Nature · doi:10.1038/s41586-022-05573-5 · Cited by 80
Structural features of nucleosomes in interphase and metaphase chromosomes
Arimura, Y., Shih, R. M., Froom, R., & Funabiki, H. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.010 · Cited by 59
Structural basis for Parkinson’s disease-linked LRRK2’s binding to microtubules
Snead, D. M., Matyszewski, M., Dickey, A. M., Lin, Y. X., Leschziner, A. E., & Reck-Peterson, S. L. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00863-y · Cited by 54
DNA-measuring Wadjet SMC ATPases restrict smaller circular plasmids by DNA cleavage
Liu, H. W., Roisné-Hamelin, F., Beckert, B., Li, Y., Myasnikov, A., & Gruber, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.015 · Cited by 53
Conformational motions and ligand-binding underlying gating and regulation in IP3R channel
Fan, G., Baker, M. R., Terry, L. E., Arige, V., Chen, M., Seryshev, A. B., Baker, M. L., Ludtke, S. J., Yule, D. I., & Serysheva, I. I. (2022) · Nature Communications · doi:10.1038/s41467-022-34574-1 · Cited by 52
Mechanism of glycogen synthase inactivation and interaction with glycogenin
Marr, L., Biswas, D., Daly, L. A., Browning, C., Vial, S. C. M., Maskell, D. P., Hudson, C., Bertrand, J. A., Pollard, J., Ranson, N. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31109-6 · Cited by 47
Structure and interactions of the endogenous human Commander complex
Laulumaa, S., Kumpula, E.-P., Huiskonen, J. T., & Varjosalo, M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01246-1 · Cited by 46
The PfRCR complex bridges malaria parasite and erythrocyte during invasion
Farrell, B., Alam, N., Hart, M. N., Jamwal, A., Ragotte, R. J., Walters-Morgan, H., Draper, S. J., Knuepfer, E., & Higgins, M. K. (2024) · Nature · doi:10.1038/s41586-023-06856-1 · Cited by 39
Vuckovic, Z., Wang, J., Pham, V., Mobbs, J. I., Belousoff, M. J., Bhattarai, A., Burger, W. A., Thompson, G., Yeasmin, M., Nawaratne, V., et al. (2023) · eLife · doi:10.7554/elife.83477 · Cited by 34
Structural basis for plasmid restriction by SMC JET nuclease
Roisné-Hamelin, F., Liu, H. W., Taschner, M., Li, Y., & Gruber, S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.009 · Cited by 34
Structural mechanism of outer kinetochore Dam1-Ndc80 complex assembly on microtubules
Muir, K. W., Batters, C., Dendooven, T., Yang, J., Zhang, Z., Burt, A., & Barford, D. (2023) · Science · doi:10.1126/science.adj8736 · Cited by 34
Genome expansion by a CRISPR trimmer-integrase
Wang, J. Y., Tuck, O. T., Skopintsev, P., Soczek, K. M., Li, G., Al-Shayeb, B., Zhou, J., & Doudna, J. A. (2023) · Nature · doi:10.1038/s41586-023-06178-2 · Cited by 33
Rieske head domain dynamics and indazole-derivative inhibition of Candida albicans complex III
Di Trani, J. M., Liu, Z., Whitesell, L., Brzezinski, P., Cowen, L. E., & Rubinstein, J. L. (2022) · Structure · doi:10.1016/j.str.2021.08.006 · Cited by 32
Structure and mechanism of NALCN-FAM155A-UNC79-UNC80 channel complex
Kang, Y., & Chen, L. (2022) · Nature Communications · doi:10.1038/s41467-022-30403-7 · Cited by 31
Structure of mycobacterial respiratory complex I
Liang, Y., Plourde, A., Bueler, S. A., Liu, J., Brzezinski, P., Vahidi, S., & Rubinstein, J. L. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214949120 · Cited by 31
Molecular mechanism of phospholipid transport at the bacterial outer membrane interface
Yeow, J., Luo, M., & Chng, S.-S. (2023) · Nature Communications · doi:10.1038/s41467-023-44144-8 · Cited by 30
Liu, S., Xia, X., Zhen, J., Li, Z., & Zhou, Z. H. (2022) · Cell Discovery · doi:10.1038/s41421-022-00487-y · Cited by 29
Yan, Y., Xiao, J., Huang, F., Xian, W., Yu, B., Cheng, R., Wu, H., Lu, X., Wang, X., Huang, W., et al. (2024) · Nature Microbiology · doi:10.1038/s41564-024-01684-z · Cited by 29
Watkins, M. B., Wang, H., Burnim, A., & Ando, N. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2302531120 · Cited by 26
CryoDRGN-AI: neural ab initio reconstruction of challenging cryo-EM and cryo-ET datasets
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
Architecture of the RNF1 complex that drives biological nitrogen fixation
Zhang, L., & Einsle, O. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01641-1 · Cited by 25
Atomic structures of a bacteriocin targeting Gram-positive bacteria
Cai, X., He, Y., Yu, I., Imani, A., Scholl, D., Miller, J. F., & Zhou, Z. H. (2024) · Nature Communications · doi:10.1038/s41467-024-51038-w · Cited by 24
Mobbs, J. I., Black, K. A., Tran, M., Burger, W. A. C., Venugopal, H., Holman, T. R., Holinstat, M., Thal, D. M., & Glukhova, A. (2023) · Blood · doi:10.1182/blood.2023020441 · Cited by 22
Structure of the recombinant RNA polymerase from African Swine Fever Virus
Pilotto, S., Sýkora, M., Cackett, G., Dulson, C., & Werner, F. (2024) · Nature Communications · doi:10.1038/s41467-024-45842-7 · Cited by 21
Currie, M. J., Davies, J. S., Scalise, M., Gulati, A., Wright, J. D., Newton-Vesty, M. C., Abeysekera, G. S., Subramanian, R., Wahlgren, W. Y., Friemann, R., et al. (2024) · eLife · doi:10.7554/elife.92307.3 · Cited by 20
Conformational space exploration of cryo-EM structures by variability refinement
Afonine, P. V., Gobet, A., Moissonnier, L., Martin, J., Poon, B. K., & Chaptal, V. (2023) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2023.184133 · Cited by 18
Cryo-EM structure of the Rous sarcoma virus octameric cleaved synaptic complex intasome
Pandey, K. K., Bera, S., Shi, K., Rau, M. J., Oleru, A. V., Fitzpatrick, J. A. J., Engelman, A. N., Aihara, H., & Grandgenett, D. P. (2021) · Communications Biology · doi:10.1038/s42003-021-01855-2 · Cited by 14
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
Structure and activation mechanism of a Lamassu phage and plasmid defense system
Li, Y., Adams, D. W., Liu, H. W., Shaw, S. J., Uchikawa, E., Jaskólska, M., Stutzmann, S., Righi, L., Szczelkun, M. D., Blokesch, M., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01677-4 · Cited by 14
Structure of a membrane tethering complex incorporating multiple SNAREs
DAmico, K. A., Stanton, A. E., Shirkey, J. D., Travis, S. M., Jeffrey, P. D., & Hughson, F. M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01164-8 · Cited by 13
Shafaq-Zadah, M., Dransart, E., Hamitouche, I., Wunder, C., Chambon, V., Valades-Cruz, C. A., Leconte, L., Sarangi, N. K., Robinson, J., Bai, S.-K., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64523-7 · Cited by 12
Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport
Watanabe, S., Kise, Y., Yonezawa, K., Inoue, M., Shimizu, N., Nureki, O., & Inaba, K. (2024) · Nature Communications · doi:10.1038/s41467-024-46747-1 · Cited by 12
Chen, M. (2025) · Communications Biology · doi:10.1038/s42003-025-08202-9 · Cited by 11
Structural mechanism of CRL4‐instructed STAT2 degradation via a novel cytomegaloviral DCAF receptor
Le‐Trilling, V. T. K., Banchenko, S., Paydar, D., Leipe, P. M., Binting, L., Lauer, S., Graziadei, A., Klingen, R., Gotthold, C., Bürger, J., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112351 · Cited by 10
SNARE disassembly requires Sec18/NSF side loading
(2025) · doi:10.1038/s41594-025-01590-w · Cited by 9
Structure and regulation of full-length human leucine-rich repeat kinase 1
Metcalfe, R. D., Martinez Fiesco, J. A., Bonet-Ponce, L., Kluss, J. H., Cookson, M. R., & Zhang, P. (2023) · Nature Communications · doi:10.1038/s41467-023-40532-2 · Cited by 8
Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G
Ho, M.-R., Wu, Y.-M., Lu, Y.-C., Ko, T.-P., & Wu, K.-P. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107958 · Cited by 8
Nucleosome structural variations in interphase and metaphase chromosomes
Arimura, Y., Shih, R. M., Froom, R., & Funabiki, H. (2020) · doi:10.1101/2020.11.12.380386 · Cited by 5
Molecular exaptation by the integrin αI domain
Hollis, J. A., Chan, M. C., Malik, H. S., & Campbell, M. G. (2025) · Science Advances · doi:10.1126/sciadv.adx9567 · Cited by 4
Peer, L., Dym, O., Elad, N., Tirosh, A., Jacobovitch, J., Sivan, E., Angel, M., Albeck, S., Schuldiner, M., Peleg, Y., et al. (2025) · Journal of Cell Science · doi:10.1242/jcs.263890 · Cited by 4
Curvature Generation and Engineering Principles from Shewanella oneidensis Multi-flagellin Flagellum
Lou, Q., Fan, H., Liu, Y., Miller, J. F., Huang, Y., & Zhou, Z. H. (2025) · ACS Nano · doi:10.1021/acsnano.5c02744 · Cited by 4
Structural insights into cobalamin loading and reactivation of human methionine synthase
Ferreira, D. S. M., McLennan, K., Diamond, C., Vollmar, M., Kiyani, W., Froese, D. S., Kopec, J., Bailey, H. J., Chalk, R., Baslé, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72899-3 · Cited by 3
Shatarupa, A., Brown, D., Olinares, P. D. B., Chase, J., Isiorho, E., Chait, B. T., & Jeruzalmi, D. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1139 · Cited by 3
Omura, S. N., Nakagawa, R., Kajimoto, S., Okazaki, S., Ishiguro, S., Mori, H., Onishi, K., Kashiwakura, Y., Hiramoto, T., Horinaka, K., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71626-2 · Cited by 2
Guo, Y., Shukla, S., Minasov, G., Inniss, N. L., Klose, T., Tokars, V. L., Mondragón, A., Otwinowski, Z., Borek, D., & Satchell, K. J. F. (2026) · Protein Science · doi:10.1002/pro.70609 · Cited by 1
Structure of the human CTF18−RFC clamp loader bound to PCNA
(2026) · doi:10.7554/elife.103493.4 · Cited by 1
Metadata
- Authors
- Punjani, A., & Fleet, D. J.
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2021-06
- Volume
- 213
- Issue
- 2
- Pages
- 107702
- ISSN
- 1047-8477 (ISSN-L)
- OpenAlex
- W3131760520
- Cited by
- 977
- References
- 7
- FWCI
- 60.96
- Type
- journal article
- Language
- en
- Open access
- green
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.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
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.