The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs
Open accessAbstract
Cryo-electron microscopy is a popular method for the determination of protein structures; however, identifying a sufficient number of particles for analysis can take months of manual effort. Current computational approaches find many false positives and require ad hoc postprocessing, especially for unusually shaped particles. To address these shortcomings, we develop Topaz, an efficient and accurate particle-picking pipeline using neural networks trained with a general-purpose positive-unlabeled learning method. This framework enables particle detection models to be trained with few sparsely labeled particles and no labeled negatives. Topaz retrieves many more real particles than conventional picking methods while maintaining low false-positive rates, is capable of picking challenging unusually shaped proteins (for example, small, non-globular and asymmetric particles), produces more representative particle sets and does not require post hoc curation. We demonstrate the performance of Topaz on two difficult datasets and three conventional datasets. Topaz is modular, standalone, free and open source (http://topaz.csail.mit.edu). The challenge of accurate particle picking in cryo-EM analysis is addressed with Topaz, a neural-network-based algorithm that shows advantages over other tools, especially in picking unusually shaped particles.
Overview
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
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Visualization of clustered protocadherin neuronal self-recognition complexes
Brasch, J., Goodman, K. M., Noble, A. J., Rapp, M., Mannepalli, S., Bahna, F., Dandey, V. P., Bepler, T., Berger, B., Maniatis, T., et al. (2019) · Nature · doi:10.1038/s41586-019-1089-3 · Cited by 99
Self-citation
Cited by
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349
Self-citationPotently neutralizing and protective human antibodies against SARS-CoV-2
Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041
Greaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016
Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519
Self-citationSARM1 is a metabolic sensor activated by an increased NMN/NAD+ ratio to trigger axon degeneration
Figley, M. D., Gu, W., Nanson, J. D., Shi, Y., Sasaki, Y., Cunnea, K., Malde, A. K., Jia, X., Luo, Z., Saikot, F. K., et al. (2021) · Neuron · doi:10.1016/j.neuron.2021.02.009 · Cited by 324
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
A hold-and-feed mechanism drives directional DNA loop extrusion by condensin
Shaltiel, I. A., Datta, S., Lecomte, L., Hassler, M., Kschonsak, M., Bravo, S., Stober, C., Ormanns, J., Eustermann, S., & Haering, C. H. (2022) · Science · doi:10.1126/science.abm4012 · Cited by 112
Deep, A., Gu, Y., Gao, Y.-Q., Ego, K. M., Herzik, M. A., Zhou, H., & Corbett, K. D. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.008 · Cited by 106
Visualization of clustered protocadherin neuronal self-recognition complexes
Brasch, J., Goodman, K. M., Noble, A. J., Rapp, M., Mannepalli, S., Bahna, F., Dandey, V. P., Bepler, T., Berger, B., Maniatis, T., et al. (2019) · Nature · doi:10.1038/s41586-019-1089-3 · Cited by 99
Self-citationIn-cell architecture of the mitochondrial respiratory chain
Waltz, F., Righetto, R. D., Lamm, L., Salinas-Giegé, T., Kelley, R., Zhang, X., Obr, M., Khavnekar, S., Kotecha, A., & Engel, B. D. (2025) · Science · doi:10.1126/science.ads8738 · Cited by 95
Structural conservation of antibiotic interaction with ribosomes
Paternoga, H., Crowe-McAuliffe, C., Bock, L. V., Koller, T. O., Morici, M., Beckert, B., Myasnikov, A. G., Grubmüller, H., Nováček, J., & Wilson, D. N. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01047-y · Cited by 94
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
Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome
Healy, M. D., McNally, K. E., Butkovič, R., Chilton, M., Kato, K., Sacharz, J., McConville, C., Moody, E. R. R., Shaw, S., Planelles-Herrero, V. J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.04.003 · Cited by 91
Structural principles of B cell antigen receptor assembly
Dong, Y., Pi, X., Bartels-Burgahn, F., Saltukoglu, D., Liang, Z., Yang, J., Alt, F. W., Reth, M., & Wu, H. (2022) · Nature · doi:10.1038/s41586-022-05412-7 · Cited by 82
Structure of SARS-CoV-2 M protein in lipid nanodiscs
Dolan, K. A., Dutta, M., Kern, D. M., Kotecha, A., Voth, G. A., & Brohawn, S. G. (2022) · eLife · doi:10.7554/elife.81702 · Cited by 82
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
A public vaccine-induced human antibody protects against SARS-CoV-2 and emerging variants
Schmitz, A. J., Turner, J. S., Liu, Z., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T. L., Darling, T. L., Adelsberg, D. C., Alsoussi, W. B., et al. (2021) · doi:10.1101/2021.03.24.436864 · Cited by 72
Structure of apolipoprotein B100 bound to the low-density lipoprotein receptor
Reimund, M., Dearborn, A. D., Graziano, G., Lei, H., Ciancone, A. M., Kumar, A., Holewinski, R., Neufeld, E. B., O’Reilly, F. J., Remaley, A. T., et al. (2025) · Nature · doi:10.1038/s41586-024-08223-0 · Cited by 63
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
High-resolution electron cryomicroscopy of V-ATPase in native synaptic vesicles
Coupland, C. E., Karimi, R., Bueler, S. A., Liang, Y., Courbon, G. M., Di Trani, J. M., Wong, C. J., Saghian, R., Youn, J.-Y., Wang, L.-Y., et al. (2024) · Science · doi:10.1126/science.adp5577 · Cited by 58
Cryo-EM structure of the complete inner kinetochore of the budding yeast point centromere
Dendooven, T., Zhang, Z., Yang, J., McLaughlin, S. H., Schwab, J., Scheres, S. H. W., Yatskevich, S., & Barford, D. (2023) · Science Advances · doi:10.1126/sciadv.adg7480 · Cited by 58
Structural insights into the iron nitrogenase complex
Schmidt, F. V., Schulz, L., Zarzycki, J., Prinz, S., Oehlmann, N. N., Erb, T. J., & Rebelein, J. G. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01124-2 · Cited by 56
Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.011 · Cited by 55
Tsutsumi, N., Hwang, S., Waghray, D., Hansen, S., Jude, K. M., Wang, N., Miao, Y., Glassman, C. R., Caveney, N. A., Janda, C. Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218238120 · Cited by 52
Cryptochrome–Timeless structure reveals circadian clock timing mechanisms
Lin, C., Feng, S., DeOliveira, C. C., & Crane, B. R. (2023) · Nature · doi:10.1038/s41586-023-06009-4 · Cited by 51
Structure of ATP synthase under strain during catalysis
Guo, H., & Rubinstein, J. L. (2022) · Nature Communications · doi:10.1038/s41467-022-29893-2 · Cited by 51
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
Structural and molecular basis of choline uptake into the brain by FLVCR2
Cater, R. J., Mukherjee, D., Gil-Iturbe, E., Erramilli, S. K., Chen, T., Koo, K., Santander, N., Reckers, A., Kloss, B., Gawda, T., et al. (2024) · Nature · doi:10.1038/s41586-024-07326-y · Cited by 45
Structure of the human outer kinetochore KMN network complex
Yatskevich, S., Yang, J., Bellini, D., Zhang, Z., & Barford, D. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01249-y · Cited by 42
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
Cryo-EM structure of the Smc5/6 holo-complex
Hallett, S. T., Campbell Harry, I., Schellenberger, P., Zhou, L., Cronin, N. B., Baxter, J., Etheridge, T. J., Murray, J. M., & Oliver, A. W. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac692 · Cited by 35
Architecture of the Tuberous Sclerosis Protein Complex
Ramlaul, K., Fu, W., Li, H., de Martin Garrido, N., He, L., Trivedi, M., Cui, W., Aylett, C. H. S., & Wu, G. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.166743 · 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
Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex
Wan, M. S. M., Muhammad, R., Koliopoulos, M. G., Roumeliotis, T. I., Choudhary, J. S., & Alfieri, C. (2023) · Nature Communications · doi:10.1038/s41467-023-38276-0 · Cited by 32
Li, B., Hoel, C. M., & Brohawn, S. G. (2021) · Nature Communications · doi:10.1038/s41467-021-27283-8 · Cited by 31
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
Mechanism of receptor assembly via the pleiotropic adipokine Leptin
Tsirigotaki, A., Dansercoer, A., Verschueren, K. H. G., Marković, I., Pollmann, C., Hafer, M., Felix, J., Birck, C., Van Putte, W., Catteeuw, D., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00941-9 · Cited by 29
Rennie, M. L., Gundogdu, M., Arkinson, C., Liness, S., Frame, S., & Walden, H. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01184 · Cited by 27
Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin
Carver, A., Yu, T.-Y., Yates, L. A., White, T., Wang, R., Lister, K., Jasin, M., & Zhang, X. (2025) · Science · doi:10.1126/science.adr7920 · Cited by 25
Structure and dynamics of differential ligand binding in the human ρ-type GABAA receptor
Cowgill, J., Fan, C., Haloi, N., Tobiasson, V., Zhuang, Y., Howard, R. J., & Lindahl, E. (2023) · Neuron · doi:10.1016/j.neuron.2023.08.006 · Cited by 25
Structural basis for lysophosphatidylserine recognition by GPR34
Izume, T., Kawahara, R., Uwamizu, A., Chen, L., Yaginuma, S., Omi, J., Kawana, H., Hou, F., Sano, F. K., Tanaka, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45046-z · Cited by 24
Molecular principles of redox-coupled sodium pumping of the ancient Rnf machinery
Kumar, A., Roth, J., Kim, H., Saura, P., Bohn, S., Reif-Trauttmansdorff, T., Schubert, A., Kaila, V. R. I., Schuller, J. M., & Müller, V. (2025) · Nature Communications · doi:10.1038/s41467-025-57375-8 · Cited by 24
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
Structural insights into human TFIIIC promoter recognition
(2023) · doi:10.1126/sciadv.adh2019 · Cited by 23
MacRae, M. R., Puvanendran, D., Haase, M. A. B., Coudray, N., Kolich, L., Lam, C., Baek, M., Bhabha, G., & Ekiert, D. C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104744 · Cited by 23
A broadly generalizable stabilization strategy for sarbecovirus fusion machinery vaccines
Lee, J., Stewart, C., Schäfer, A., Leaf, E. M., Park, Y.-J., Asarnow, D., Powers, J. M., Treichel, C., Sprouse, K. R., Corti, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49656-5 · Cited by 23
Polymerization of ZBTB transcription factors regulates chromatin occupancy
Park, P. M. C., Park, J., Brown, J., Hunkeler, M., Roy Burman, S. S., Donovan, K. A., Yoon, H., Nowak, R. P., Słabicki, M., Ebert, B. L., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.06.010 · Cited by 22
Bond-centric modular design of protein assemblies
Wang, S., Favor, A., Kibler, R. D., Lubner, J. M., Borst, A. J., Coudray, N., Redler, R. L., Chiang, H. T., Sheffler, W., Hsia, Y., et al. (2025) · Nature Materials · doi:10.1038/s41563-025-02297-5 · Cited by 22
DNA-binding mechanism and evolution of replication protein A
(2023) · doi:10.1038/s41467-023-38048-w · Cited by 22
Structural basis for activation of Arf1 at the Golgi complex
(2022) · doi:10.1016/j.celrep.2022.111282 · Cited by 22
Bonchuk, A. N., Balagurov, K. I., Baradaran, R., Boyko, K. M., Sluchanko, N. N., Khrustaleva, A. M., Burtseva, A. D., Arkova, O. V., Khalisova, K. K., Popov, V. O., et al. (2024) · eLife · doi:10.7554/elife.96832 · Cited by 21
The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics
Llerena Schiffmacher, D. A., Lee, S.-H., Kliza, K. W., Theil, A. F., Akita, M., Helfricht, A., Bezstarosti, K., Gonzalo-Hansen, C., van Attikum, H., Verlaan-de Vries, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50584-7 · Cited by 19
Structure of the human Bre1 complex bound to the nucleosome
Onishi, S., Uchiyama, K., Sato, K., Okada, C., Kobayashi, S., Hamada, K., Nishizawa, T., Nureki, O., Ogata, K., & Sengoku, T. (2024) · Nature Communications · doi:10.1038/s41467-024-46910-8 · Cited by 19
Cryo-EM structures of apo-APC/C and APC/CCDH1:EMI1 complexes provide insights into APC/C regulation
Höfler, A., Yu, J., Yang, J., Zhang, Z., Chang, L., McLaughlin, S. H., Grime, G. W., Garman, E. F., Boland, A., & Barford, D. (2024) · Nature Communications · doi:10.1038/s41467-024-54398-5 · Cited by 18
Thorn, A. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102368 · Cited by 16
Integrated model of the vertebrate augmin complex
Travis, S. M., Mahon, B. P., Huang, W., Ma, M., Rale, M. J., Kraus, J., Taylor, D. J., Zhang, R., & Petry, S. (2023) · Nature Communications · doi:10.1038/s41467-023-37519-4 · Cited by 16
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
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
TopBP1 utilises a bipartite GINS binding mode to support genome replication
Day, M., Tetik, B., Parlak, M., Almeida-Hernández, Y., Räschle, M., Kaschani, F., Siegert, H., Marko, A., Sanchez-Garcia, E., Kaiser, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45946-0 · Cited by 14
The GATE glycoprotein complex enhances human cytomegalovirus entry in endothelial cells
Norris, M. J., Henderson, L. A., Siddiquey, M. N. A., Yin, J., Yoo, K., Brunel, S., Mor, M., Saphire, E. O., Benedict, C. A., & Kamil, J. P. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02025-4 · Cited by 14
Phosphorylation-mediated conformational change regulates human SLFN11
Kugler, M., Metzner, F. J., Witte, G., Hopfner, K.-P., & Lammens, K. (2024) · Nature Communications · doi:10.1038/s41467-024-54833-7 · Cited by 13
Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate
Zuo, P., Wang, W., Dai, Z., Zheng, J., Yu, S., Wang, G., Yin, Y., Liang, L., & Yin, Y. (2025) · Nature Communications · doi:10.1038/s41467-025-58200-y · Cited by 13
Structure of Mycobacterial NDH-2 Bound to a 2-Mercapto-Quinazolinone Inhibitor
Liang, Y., Bueler, S. A., Cook, G. M., & Rubinstein, J. L. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00049 · 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
High-affinity PQQ import is widespread in Gram-negative bacteria
Munder, F., Voutsinos, M., Hantke, K., Venugopal, H., & Grinter, R. (2025) · Science Advances · doi:10.1126/sciadv.adr2753 · 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
In vitro characterization of the full-length human dynein-1 cargo adaptor BicD2
Fagiewicz, R., Crucifix, C., Klos, T., Deville, C., Kieffer, B., Nominé, Y., Busselez, J., Rossolillo, P., & Schmidt, H. (2022) · Structure · doi:10.1016/j.str.2022.08.009 · Cited by 11
Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction
Sokolova, V., Miratsky, J., Svetlov, V., Brenowitz, M., Vant, J., Lewis, T. S., Dryden, K., Lee, G., Sarkar, S., Nudler, E., et al. (2024) · Structure · doi:10.1016/j.str.2024.09.013 · Cited by 11
Structure shows that the BIR2 domain of E3 ligase XIAP binds across the RIPK2 kinase dimer interface
Lethier, M., Huard, K., Hons, M., Favier, A., Brutscher, B., Boeri Erba, E., Abbott, D. W., Cusack, S., & Pellegrini, E. (2023) · Life Science Alliance · doi:10.26508/lsa.202201784 · Cited by 11
Ghazi Esfahani, B., Walia, N., Neselu, K., Garg, Y., Aragon, M., Askenasy, I., Wei, H. A., Mendez, J. H., & Stroupe, M. E. (2025) · Nature Communications · doi:10.1038/s41467-025-58037-5 · Cited by 10
Structural analysis of the dynamic ribosome-translocon complex
Lewis, A. J., Zhong, F., Keenan, R. J., & Hegde, R. S. (2024) · eLife · doi:10.7554/elife.95814.3 · Cited by 9
Liu, Y., van den Ent, F., & Löwe, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2309984121 · Cited by 9
Structure of yeast RAVE bound to a partial V 1 complex
(2024) · doi:10.1073/pnas.2414511121 · 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
Shihoya, W., Akasaka, H., Jordan, P. A., Lechner, A., Okada, B. K., Costa Machado da Cruz, G., Sano, F. K., Tanaka, T., Kawahara, R., Chaudhari, R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57960-x · Cited by 8
CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply
Jeong, T.-K., Frater, R. C. M., Yoon, J., Groth, A., & Song, J.-J. (2025) · Nature Communications · doi:10.1038/s41467-025-56976-7 · Cited by 8
4D structural biology–quantitative dynamics in the eukaryotic RNA exosome complex
Liebau, J., Lazzaretti, D., Fürtges, T., Bichler, A., Pilsl, M., Rudack, T., & Sprangers, R. (2025) · Nature Communications · doi:10.1038/s41467-025-62982-6 · Cited by 7
Ligand identification in CryoEM and X-ray maps using deep learning
Karolczak, J., Przybyłowska, A., Szewczyk, K., Taisner, W., Heumann, J. M., Stowell, M. H. B., Nowicki, M., & Brzezinski, D. (2024) · Bioinformatics · doi:10.1093/bioinformatics/btae749 · Cited by 7
Lamm, G. H. U., Marin, E., Alekseev, A., Schellbach, A. V., Stetsenko, A., Haro-Moreno, J. M., Bourenkov, G., Borshchevskiy, V., Asido, M., Agthe, M., et al. (2025) · Science Advances · doi:10.1126/sciadv.adv1015 · Cited by 7
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
Stevens, A., Kashyap, S., Crofut, E., Alvarez-Cabrera, A. L., Jih, J., Liu, Y.-T., & Zhou, Z. H. (2025) · Journal of Virology · doi:10.1128/jvi.00504-25 · Cited by 5
Architecture of the ATP-driven motor for protein import into chloroplasts
Wang, N., Xing, J., Su, X., Pan, J., Chen, H., Shi, L., Si, L., Yang, W., & Li, M. (2024) · Molecular Plant · doi:10.1016/j.molp.2024.09.010 · Cited by 5
Shvarev, D., Scholz, A. I., & Moeller, A. (2023) · mBio · doi:10.1128/mbio.01893-23 · Cited by 5
Metadata
- Authors
- Bepler, T., Morin, A., Rapp, M., Brasch, J., Shapiro, L., Noble, A. J., & Berger, B.
- Venue
- Nature Methods
- Published
- 2019-10-07
- Volume
- 16
- Issue
- 11
- Pages
- 1153-1160
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2793402357
- Cited by
- 1,606
- References
- 2
- FWCI
- 31.95
- 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.