The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Real-time cryo-electron microscopy data preprocessing with Warp
Open accessAbstract
The acquisition of cryo-electron microscopy (cryo-EM) data from biological specimens must be tightly coupled to data preprocessing to ensure the best data quality and microscope usage. Here we describe Warp, a software that automates all preprocessing steps of cryo-EM data acquisition and enables real-time evaluation. Warp corrects micrographs for global and local motion, estimates the local defocus and monitors key parameters for each recorded micrograph or tomographic tilt series in real time. The software further includes deep-learning-based models for accurate particle picking and image denoising. The output from Warp can be fed into established programs for particle classification and 3D-map refinement. Our benchmarks show improvement in the nominal resolution, which went from 3.9 Å to 3.2 Å, of a published cryo-EM data set for influenza virus hemagglutinin. Warp is easy to install from http://github.com/cramerlab/warp and computationally inexpensive, and has an intuitive, streamlined user interface. The user-friendly software tool Warp enables automated, on-the-fly preprocessing of cryo-EM data, including motion correction, defocus estimation, particle picking and image denoising.
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
Deep Residual Learning for Image Recognition
He, K., Zhang, X., Ren, S., & Sun, J. (2016) · 2016 IEEE Conference on Computer Vision and Pattern Recognition (CVPR) · doi:10.1109/cvpr.2016.90 · Cited by 235,474
ImageNet classification with deep convolutional neural networks
Krizhevsky, A., Sutskever, I., & Hinton, G. E. (2017) · Communications of the ACM · doi:10.1145/3065386 · Cited by 112,155
U-Net: Convolutional Networks for Biomedical Image Segmentation
Ronneberger, O., Fischer, P., & Brox, T. (2015) · Lecture notes in computer science · doi:10.1007/978-3-319-24574-4_28 · Cited by 99,404
Gradient-based learning applied to document recognition
Lecun, Y., Bottou, L., Bengio, Y., & Haffner, P. (1998) · Proceedings of the IEEE · doi:10.1109/5.726791 · Cited by 58,805
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
Cited by
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
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
A guide to machine learning for biologists
Greener, J. G., Kandathil, S. M., Moffat, L., & Jones, D. T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00407-0 · Cited by 2,127
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Structural and functional analysis of a potent sarbecovirus neutralizing antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · doi:10.1101/2020.04.07.023903 · Cited by 1,752
Structure-based design of prefusion-stabilized SARS-CoV-2 spikes
Hsieh, C.-L., Goldsmith, J. A., Schaub, J. M., DiVenere, A. M., Kuo, H.-C., Javanmardi, K., Le, K. C., Wrapp, D., Lee, A. G., Liu, Y., et al. (2020) · Science · doi:10.1126/science.abd0826 · Cited by 1,303
Kumar, Y., Koul, A., Singla, R., & Ijaz, M. F. (2023) · Journal of Ambient Intelligence and Humanized Computing · doi:10.1007/s12652-021-03612-z · Cited by 1,040
RetractedN-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901
“Cryo-EM data processing Movie frame alignment, estimation of the microscope contrast-transfer function parameters, particle picking and extraction (with a box size of 400 pixels(2)) were carried out usingWarp (Tegunov and Cramer, 2019).”
BNT162b vaccines protect rhesus macaques from SARS-CoV-2
Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03275-y · Cited by 694
De novo design of picomolar SARS-CoV-2 miniprotein inhibitors
Cao, L., Goreshnik, I., Coventry, B., Case, J. B., Miller, L., Kozodoy, L., Chen, R. E., Carter, L., Walls, A. C., Park, Y.-J., et al. (2020) · Science · doi:10.1126/science.abd9909 · Cited by 742
Automated model building and protein identification in cryo-EM maps
Jamali, K., Käll, L., Zhang, R., Brown, A., Kimanius, D., & Scheres, S. H. W. (2023) · doi:10.1101/2023.05.16.541002 · Cited by 686
Automated model building and protein identification in cryo-EM maps
Jamali, K., Käll, L., Zhang, R., Brown, A., Kimanius, D., & Scheres, S. H. W. (2024) · Nature · doi:10.1038/s41586-024-07215-4 · Cited by 686
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510
Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412
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
Self-citationNucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function
Dodonova, S. O., Zhu, F., Dienemann, C., Taipale, J., & Cramer, P. (2020) · Nature · doi:10.1038/s41586-020-2195-y · Cited by 265
Self-citationStructures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0334-7 · Cited by 260
Molecular glue CELMoD compounds are regulators of cereblon conformation
Watson, E. R., Novick, S., Matyskiela, M. E., Chamberlain, P. P., H. de la Peña, A., Zhu, J., Tran, E., Griffin, P. R., Wertz, I. E., & Lander, G. C. (2022) · Science · doi:10.1126/science.add7574 · Cited by 208
Visualizing translation dynamics at atomic detail inside a bacterial cell
Xue, L., Lenz, S., Zimmermann-Kogadeeva, M., Tegunov, D., Cramer, P., Bork, P., Rappsilber, J., & Mahamid, J. (2022) · Nature · doi:10.1038/s41586-022-05255-2 · Cited by 184
Self-citationFundamental behaviors emerge from simulations of a living minimal cell
Thornburg, Z. R., Bianchi, D. M., Brier, T. A., Gilbert, B. R., Earnest, E. E., Melo, M. C. R., Safronova, N., Sáenz, J. P., Cook, A. T., Wise, K. S., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.025 · Cited by 165
“1) Syn3A cells were imaged using cryo-ET by the lab of Elizabeth Villa at UCSD and ribosome coordinates were determined by applying an iterative binary classification procedure (Tegunov and Cramer, 2019) to tomographic reconstructions of Syn3A cells.”
Structural basis of TFIIH activation for nucleotide excision repair
Kokic, G., Chernev, A., Tegunov, D., Dienemann, C., Urlaub, H., & Cramer, P. (2019) · Nature Communications · doi:10.1038/s41467-019-10745-5 · Cited by 163
Self-citationVogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2020) · doi:10.1101/2020.09.08.280818 · Cited by 126
Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome
Yatskevich, S., Muir, K. W., Bellini, D., Zhang, Z., Yang, J., Tischer, T., Predin, M., Dendooven, T., McLaughlin, S. H., & Barford, D. (2022) · Science · doi:10.1126/science.abn3810 · Cited by 120
The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains
Lacey, S. E., Foster, H. E., & Pigino, G. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00905-5 · Cited by 119
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
Structural basis for strand-transfer inhibitor binding to HIV intasomes
Passos, D. O., Li, M., Jóźwik, I. K., Zhao, X. Z., Santos-Martins, D., Yang, R., Smith, S. J., Jeon, Y., Forli, S., Hughes, S. H., et al. (2020) · Science · doi:10.1126/science.aay8015 · Cited by 106
One-step nanoscale expansion microscopy reveals individual protein shapes
Shaib, A. H., Chouaib, A. A., Chowdhury, R., Altendorf, J., Mihaylov, D., Zhang, C., Krah, D., Imani, V., Spencer, R. K. W., Georgiev, S. V., et al. (2025) · Nature Biotechnology · doi:10.1038/s41587-024-02431-9 · Cited by 104
Structure of H3K36-methylated nucleosome–PWWP complex reveals multivalent cross-gyre binding
Wang, H., Farnung, L., Dienemann, C., & Cramer, P. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0345-4 · Cited by 93
Self-citationThe 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
Lee, S. C., Adams, D. W., Ipsaro, J. J., Cahn, J., Lynn, J., Kim, H.-S., Berube, B., Major, V., Calarco, J. P., LeBlanc, C., et al. (2023) · Cell · doi:10.1016/j.cell.2023.08.001 · Cited by 89
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
Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization
Zhu, X., Xie, X., Das, H., Tan, B. G., Shi, Y., Al-Behadili, A., Peter, B., Motori, E., Valenzuela, S., Posse, V., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.006 · Cited by 69
A cryo-ET survey of microtubules and intracellular compartments in mammalian axons
Foster, H. E., Ventura Santos, C., & Carter, A. P. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202103154 · Cited by 69
Grushin, K., Kalyana Sundaram, R. V., Sindelar, C. V., & Rothman, J. E. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121259119 · Cited by 66
Imprinted antibody responses against SARS-CoV-2 Omicron sublineages
Park, Y.-J., Pinto, D., Walls, A. C., Liu, Z., De Marco, A., Benigni, F., Zatta, F., Silacci-Fregni, C., Bassi, J., Sprouse, K. R., et al. (2022) · doi:10.1101/2022.05.08.491108 · Cited by 251
Cryo-EM and artificial intelligence visualize endogenous protein community members
Skalidis, I., Kyrilis, F. L., Tüting, C., Hamdi, F., Chojnowski, G., & Kastritis, P. L. (2022) · Structure · doi:10.1016/j.str.2022.01.001 · Cited by 61
Csx28 is a membrane pore that enhances CRISPR-Cas13b–dependent antiphage defense
VanderWal, A. R., Park, J.-U., Polevoda, B., Nicosia, J. K., Molina Vargas, A. M., Kellogg, E. H., & O’Connell, M. R. (2023) · Science · doi:10.1126/science.abm1184 · Cited by 55
Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET
Dutka, P., Metskas, L. A., Hurt, R. C., Salahshoor, H., Wang, T.-Y., Malounda, D., Lu, G. J., Chou, T.-F., Shapiro, M. G., & Jensen, G. J. (2023) · Structure · doi:10.1016/j.str.2023.03.011 · Cited by 51
Kouba, T., Vogel, D., Thorkelsson, S. R., Quemin, E. R. J., Williams, H. M., Milewski, M., Busch, C., Günther, S., Grünewald, K., Rosenthal, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27305-5 · Cited by 50
Determinants shaping the nanoscale architecture of the mouse rod outer segment
Pöge, M., Mahamid, J., Imanishi, S. S., Plitzko, J. M., Palczewski, K., & Baumeister, W. (2021) · eLife · doi:10.7554/elife.72817 · Cited by 50
In situ cryo-electron tomography reveals local cellular machineries for axon branch development
Nedozralova, H., Basnet, N., Ibiricu, I., Bodakuntla, S., Biertümpfel, C., & Mizuno, N. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202106086 · Cited by 43
Structural basis for human mitochondrial tRNA maturation
(2024) · doi:10.1038/s41467-024-49132-0 · Cited by 41
Integrating machine learning to advance epitope mapping
Grewal, S., Hegde, N., & Yanow, S. K. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1463931 · Cited by 35
Gilbert, B. R., Thornburg, Z. R., Lam, V., Rashid, F.-Z. M., Glass, J. I., Villa, E., Dame, R. T., & Luthey-Schulten, Z. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.644133 · Cited by 30
Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography
Watanabe, R., Zyla, D., Parekh, D., Hong, C., Jones, Y., Schendel, S. L., Wan, W., Castillon, G., & Saphire, E. O. (2024) · Cell · doi:10.1016/j.cell.2024.08.044 · Cited by 33
CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage
Conners, R., McLaren, M., Łapińska, U., Sanders, K., Stone, M. R. L., Blaskovich, M. A. T., Pagliara, S., Daum, B., Rakonjac, J., & Gold, V. A. M. (2021) · Nature Communications · doi:10.1038/s41467-021-26610-3 · Cited by 32
The structural basis for RNA slicing by human Argonaute2
Mohamed, A. A., Wang, P. Y., Bartel, D. P., & Vos, S. M. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115166 · Cited by 32
Structure and design of Langya virus glycoprotein antigens
Wang, Z., McCallum, M., Yan, L., Gibson, C. A., Sharkey, W., Park, Y.-J., Dang, H. V., Amaya, M., Person, A., Broder, C. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314990121 · Cited by 32
Cryo-EM structure of the HIV-1 Pol polyprotein provides insights into virion maturation
Harrison, J. J. E. K., Passos, D. O., Bruhn, J. F., Bauman, J. D., Tuberty, L., DeStefano, J. J., Ruiz, F. X., Lyumkis, D., & Arnold, E. (2022) · Science Advances · doi:10.1126/sciadv.abn9874 · Cited by 31
A Pattern Recognition Method of Personalized Adaptive Learning in Online Education
Peng, P., & Fu, W. (2022) · Mobile Networks and Applications · doi:10.1007/s11036-022-01942-6 · Cited by 29
Structural basis for non-canonical integrin engagement by Bordetella adenylate cyclase toxin
Goldsmith, J. A., DiVenere, A. M., Maynard, J. A., & McLellan, J. S. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111196 · Cited by 28
Dolce, L. G., Zimmer, A. A., Tengo, L., Weis, F., Rubio, M. A. T., Alfonzo, J. D., & Kowalinski, E. (2022) · Nature Communications · doi:10.1038/s41467-022-34441-z · Cited by 27
FilamentID reveals the composition and function of metabolic enzyme polymers during gametogenesis
Hugener, J., Xu, J., Wettstein, R., Ioannidi, L., Velikov, D., Wollweber, F., Henggeler, A., Matos, J., & Pilhofer, M. (2024) · Cell · doi:10.1016/j.cell.2024.04.026 · 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
Structural insights into human TFIIIC promoter recognition
(2023) · doi:10.1126/sciadv.adh2019 · 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
Gong, R., Reynolds, M. J., Sun, X., & Alushin, G. M. (2025) · Science Advances · doi:10.1126/sciadv.adu0989 · Cited by 21
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
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1
Düring, J., Wolter, M., Toplak, J. J., Torres, C., Dybkov, O., Fokkens, T. J., Bohnsack, K. E., Urlaub, H., Steinchen, W., Dienemann, C., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01203-4 · Cited by 20
Structure of a SARS-CoV-2 spike S2 subunit in a pre-fusion, open conformation
Olmedillas, E., Rajamanickam, R. R., Avalos, R. D., Ana-Sosa-Batiz, F., Zyla, D., Zandonatti, M. A., Harkins, S. S., Shresta, S., Hastie, K. M., & Saphire, E. O. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116052 · Cited by 19
T cell toxicity induced by tigecycline binding to the mitochondrial ribosome
Shao, Q., Khawaja, A., Nguyen, M. D., Singh, V., Zhang, J., Liu, Y., Nordin, J., Adori, M., Axel Innis, C., Castro Dopico, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59388-9 · Cited by 16
Thorn, A. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102368 · Cited by 16
CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics
Lee, J. K. J., Liu, Y.-T., Hu, J. J., Aphasizheva, I., Aphasizhev, R., & Zhou, Z. H. (2023) · Journal of Structural Biology: X · doi:10.1016/j.yjsbx.2023.100088 · Cited by 16
Structural basis of eukaryotic transcription termination by the Rat1 exonuclease complex
Yanagisawa, T., Murayama, Y., Ehara, H., Goto, M., Aoki, M., & Sekine, S.-I. (2024) · Nature Communications · doi:10.1038/s41467-024-52157-0 · Cited by 15
Structures of aberrant spliceosome intermediates on their way to disassembly
Soni, K., Horvath, A., Dybkov, O., Schwan, M., Trakansuebkul, S., Flemming, D., Wild, K., Urlaub, H., Fischer, T., & Sinning, I. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01480-7 · Cited by 14
May, M. B., Lopez-Perez, G. S., & Davis, J. H. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2521210123 · Cited by 13
Molecular mechanisms of flotillin complexes in organizing membrane microdomains
Lu, M.-A., Qian, Y., Ma, L., Hong, J., Li, X., Yu, L., Guo, Q., & Gao, N. (2026) · Nature Communications · doi:10.1038/s41467-026-69197-3 · Cited by 13
Zhang, L., Gordiyenko, Y., Morgan, T., Franco, C., Tufegdžić Vidaković, A., & Zhang, S. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01586-6 · Cited by 12
Archaeal type six secretion system mediates contact-dependent antagonism
Zachs, T., Malit, J. J. L., Xu, J., Schürch, A., Sivabalasarma, S., Nußbaum, P., Albers, S.-V., & Pilhofer, M. (2024) · Science Advances · doi:10.1126/sciadv.adp7088 · Cited by 12
Berkamp, S., Jungbluth, L., Katranidis, A., Mostafavi, S., Korculanin, O., Lu, P.-H., Ickert, L., Dierig, M. M., Sharma, L., Thukral, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66785-7 · Cited by 12
CryoET shows cofilactin filaments inside the microtubule lumen
Ventura Santos, C., Rogers, S. L., & Carter, A. P. (2023) · The EMBO Reports · doi:10.15252/embr.202357264 · Cited by 11
Structure of the Human Signal Peptidase Complex Reveals the Determinants for Signal Peptide Cleavage
Liaci, A. M., Steigenberger, B., Tamara, S., de Souza, P. C. T., Gröllers-Mulderij, M., Ogrissek, P., Marrink, S. J., Scheltema, R. A., & Förster, F. (2020) · doi:10.1101/2020.11.11.378711 · Cited by 10
Furlanetto, V., Kalyani, D. C., Kostelac, A., Puc, J., Haltrich, D., Hällberg, B. M., & Divne, C. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168547 · Cited by 9
In situ structural mechanism of epothilone-B-induced CNS axon regeneration
Bodakuntla, S., Taira, K., Yamada, Y., Alvarez-Brecht, P., Cada, A. K., Basnet, N., Zhang, R., Martinez-Sanchez, A., Biertümpfel, C., & Mizuno, N. (2025) · Nature · doi:10.1038/s41586-025-09654-z · Cited by 9
Yan, Y., Shetty, M., Harding, H. P., George, G., Zyryanova, A., Labbé, K., Mafi, A., Hao, Q., Sidrauski, C., & Ron, D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320013121 · Cited by 7
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395
Structure and function of the human apoptotic scramblase Xkr4
Chakraborty, S., Feng, Z., Lee, S., Alvarenga, O. E., Panda, A., Zhang, S., Bruni, R., Khelashvili, G., Gupta, K., & Accardi, A. (2025) · Nature Communications · doi:10.1038/s41467-025-62739-1 · Cited by 5
Structural and dynamic changes in P-Rex1 upon activation by PIP3 and inhibition by IP4
Ravala, S. K., Adame-Garcia, S. R., Li, S., Chen, C.-L., Cianfrocco, M. A., Silvio Gutkind, J., Cash, J. N., & Tesmer, J. J. (2024) · eLife · doi:10.7554/elife.92822.4 · Cited by 4
New insights into the molecular architecture of neurons by cryo-electron tomography
Petrovic, A., Do, T. T., & Fernández-Busnadiego, R. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102939 · Cited by 4
Cryo-electron tomography reveals the microtubule-bound form of inactive LRRK2
Chen, S., Basiashvili, T., Hutchings, J., Sanz Murillo, M., Villagran Suarez, A., Xiong, E., Alegrio Louro, J., Leschziner, A. E., & Villa, E. (2025) · eLife · doi:10.7554/elife.100799.3 · Cited by 3
Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution
Pellegrino, S., Dent, K. C., Spikes, T., & Warren, A. J. (2022) · doi:10.1101/2022.01.16.475527 · Cited by 3
Casu, B., Sallmen, J. W., Haas, P. E., Chandra, G., Afanasyev, P., Xu, J., Pilhofer, M., & Schlimpert, S. (2025) · eLife · doi:10.7554/elife.104064 · Cited by 3
Casu, B., Sallmen, J. W., Haas, P. E., Chandra, G., Afanasyev, P., Xu, J., Pilhofer, M., & Schlimpert, S. (2024) · doi:10.1101/2024.06.25.600559 · Cited by 1
Cryo-electron tomography reveals the microtubule-bound form of inactive LRRK2
Chen, S., Basiashvili, T., Hutchings, J., Sanz Murillo, M., Villagran Suarez, A., Xiong, E., Alegrio Louro, J., Leschziner, A. E., & Villa, E. (2025) · eLife · doi:10.7554/elife.100799 · Cited by 1
Structural and dynamic changes in P-Rex1 upon activation by PIP 3 and inhibition by IP 4
Ravala, S. K., Adame-Garcia, S. R., Li, S., Chen, C.-L., Cianfrocco, M. A., Gutkind, J. S., Cash, J. N., & Tesmer, J. J. G. (2023) · doi:10.1101/2023.09.15.557836
Metadata
- Authors
- Tegunov, D., & Cramer, P.
- Venue
- Nature Methods
- Published
- 2019-10-07
- Volume
- 16
- Issue
- 11
- Pages
- 1146-1152
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2977933365
- Cited by
- 1,332
- References
- 5
- FWCI
- 57.03
- 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.
