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MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
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Abstract
MotionCor2 software corrects for beam-induced sample motion, improving the resolution of cryo-EM reconstructions.
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
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
Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
Research works printed but not linked: 7
- Cheng, Y. Cell 161, 450–457 (2015). · DOI · Paper page
- Brilot, A.F. et al. J. Struct. Biol. 177, 630–637 (2012). · DOI · Paper page
- Li, X. et al. Nat. Methods 10, 584–590 (2013). · DOI · Paper page
- Liao, M., Cao, E., Julius, D. & Cheng, Y. Nature 504, 107–112 (2013). · DOI · Paper page
- Bai, X.C., Fernandez, I.S., McMullan, G. & Scheres, S.H. eLife 2, e00461 (2013). · DOI · Paper page
- Rubinstein, J.L. & Brubaker, M.A. J. Struct. Biol. 192, 188–195 (2015). · DOI · Paper page
- Grant, T. & Grigorieff, N. eLife 4, e06980 (2015). · DOI · Paper page
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Echigoya, K., Koyama, M., Negishi, L., Takizawa, Y., Mizukami, Y., Shimabayashi, H., Kuroda, A., & Kurumizaka, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-68850-1 · Cited by 47
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
Pro-phagocytic function and structural basis of GPR84 signaling
Zhang, X., Wang, Y., Supekar, S., Cao, X., Zhou, J., Dang, J., Chen, S., Jenkins, L., Marsango, S., Li, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41201-0 · Cited by 46
Ouyang, R., Costa, A. R., Cassidy, C. K., Otwinowska, A., Williams, V. C. J., Latka, A., Stansfeld, P. J., Drulis-Kawa, Z., Briers, Y., Pelt, D. M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34972-5 · Cited by 46
Structure of human TRPM8 channel
(2023) · doi:10.1038/s42003-023-05425-6 · Cited by 46
Modulating co-translational protein folding by rational design and ribosome engineering
Ahn, M., Włodarski, T., Mitropoulou, A., Chan, S. H. S., Sidhu, H., Plessa, E., Becker, T. A., Budisa, N., Waudby, C. A., Beckmann, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31906-z · Cited by 45
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
Jette, C. A., Barnes, C. O., Kirk, S. M., Melillo, B., Smith, A. B., & Bjorkman, P. J. (2021) · Nature Communications · doi:10.1038/s41467-021-21816-x · Cited by 38
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Obana, N., Takada, H., Crowe-McAuliffe, C., Iwamoto, M., Egorov, A. A., Wu, K. J. Y., Chiba, S., Murina, V., Paternoga, H., Tresco, B. I. C., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad193 · Cited by 42
Liu, Y., Bunney, T. D., Khosa, S., Macé, K., Beckenbauer, K., Askwith, T., Maslen, S., Stubbs, C., de Oliveira, T. M., Sader, K., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2019.102607 · Cited by 42
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Jansen, R. M., Peruzzo, R., Fromm, S. A., Yokom, A. L., Zoncu, R., & Hurley, J. H. (2022) · Science Advances · doi:10.1126/sciadv.add2926 · Cited by 42
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Wang, Y., Wang, C., Guan, Z., Cao, J., Xu, J., Wang, S., Cui, Y., Wang, Q., Chen, Y., Yin, Y., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114857 · Cited by 41
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Kim, S. K., Dickinson, M. S., Finer-Moore, J., Guan, Z., Kaake, R. M., Echeverria, I., Chen, J., Pulido, E. H., Sali, A., Krogan, N. J., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00918-0 · Cited by 41
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Schubert, K., Karousis, E. D., Ban, I., Lapointe, C. P., Leibundgut, M., Bäumlin, E., Kummerant, E., Scaiola, A., Schönhut, T., Ziegelmüller, J., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.09.002 · Cited by 41
Filling Adeno-Associated Virus Capsids: Estimating Success by Cryo-Electron Microscopy
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
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Qi, X., Hu, Q., Elghobashi-Meinhardt, N., Long, T., Chen, H., & Li, X. (2023) · Cell · doi:10.1016/j.cell.2023.09.021 · Cited by 40
Diverse modes of H3K36me3-guided nucleosomal deacetylation by Rpd3S
Guan, H., Wang, P., Zhang, P., Ruan, C., Ou, Y., Peng, B., Zheng, X., Lei, J., Li, B., Yan, C., et al. (2023) · Nature · doi:10.1038/s41586-023-06349-1 · Cited by 40
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Rai, A., Liu, T., Katrukha, E. A., Estévez-Gallego, J., Manka, S. W., Paterson, I., Díaz, J. F., Kapitein, L. C., Moores, C. A., & Akhmanova, A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112261118 · Cited by 38
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von Kügelgen, A., van Dorst, S., Yamashita, K., Sexton, D. L., Tocheva, E. I., Murshudov, G., Alva, V., & Bharat, T. A. M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2215808120 · Cited by 35
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Reyes, R. A., Raghavan, S. S. R., Hurlburt, N. K., Introini, V., Bol, S., Kana, I. H., Jensen, R. W., Martinez-Scholze, E., Gestal-Mato, M., López-Gutiérrez, B., et al. (2024) · Nature · doi:10.1038/s41586-024-08220-3 · 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
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MethodVuckovic, 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
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Li, J., Liu, H., Li, J., Liu, J., Dai, X., Zhu, A., Xiao, Q., Qian, W., Li, H., Guo, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57152-7 · Cited by 33
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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
Sokratian, A., Zhou, Y., Tatli, M., Burbidge, K. J., Xu, E., Viverette, E., Donzelli, S., Duda, A. M., Yuan, Y., Li, H., et al. (2024) · Science Advances · doi:10.1126/sciadv.adq3539 · Cited by 32
Molecular basis of mRNA delivery to the bacterial ribosome
Webster, M. W., Chauvier, A., Rahil, H., Graziadei, A., Charles, K., Miropolskaya, N., Takacs, M., Saint-André, C., Rappsilber, J., Walter, N. G., et al. (2024) · Science · doi:10.1126/science.ado8476 · Cited by 32
The kidney slit diaphragm resembles a fishnet
Birtasu, A. N., Wieland, K., Ermel, U. H., Arghittu, S. M., Manger, S., Kocylowski, M. K., Fakler, B., Scheffer, M. P., Covino, R., Grahammer, F., et al. (2025) · Kidney International · doi:10.1016/j.kint.2025.08.028 · Cited by 32
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Long, T., Li, D., Vale, G., Jiang, Y., Schmiege, P., Yang, Z. J., McDonald, J. G., & Li, X. (2024) · Cell · doi:10.1016/j.cell.2024.08.004 · Cited by 31
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Le, L. T. M., Thompson, J. R., Dehghani‐Ghahnaviyeh, S., Pant, S., Dang, P. X., French, J. B., Kanikeyo, T., Tajkhorshid, E., & Alam, A. (2023) · The EMBO Journal · doi:10.15252/embj.2022111065 · Cited by 31
Li, B., Hoel, C. M., & Brohawn, S. G. (2021) · Nature Communications · doi:10.1038/s41467-021-27283-8 · Cited by 31
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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
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Li, Y., Shen, Y., Hu, Z., & Yan, R. (2023) · Science Advances · doi:10.1126/sciadv.adg2331 · Cited by 31
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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
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Park, S. H., Han, J., Jeong, B.-C., Song, J. H., Jang, S. H., Jeong, H., Kim, B. H., Ko, Y.-G., Park, Z.-Y., Lee, K. E., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01111-7 · Cited by 31
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Wang, F., Cvirkaite-Krupovic, V., Krupovic, M., & Egelman, E. H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207037119 · Cited by 30
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Souza, D. P., Espadas, J., Chaaban, S., Moody, E. R. R., Hatano, T., Balasubramanian, M., Williams, T. A., Roux, A., & Baum, B. (2025) · Science Advances · doi:10.1126/sciadv.ads5255 · Cited by 30
Hayne, C. K., Butay, K. J. U., Stewart, Z. D., Krahn, J. M., Perera, L., Williams, J. G., Petrovitch, R. M., Deterding, L. J., Matera, A. G., Borgnia, M. J., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00991-z · Cited by 30
Park, D., Steiner, S., Shao, M., Roy, C. R., & Liu, J. (2022) · Infection and Immunity · doi:10.1128/iai.00410-22 · Cited by 30
Zhong, Y., Gao, Y., Zhou, D., Ma, X., Chen, H., Xu, Y., Yang, W., & Yu, X. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.02.093 · 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
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Hu, J. J., Lee, J. K. J., Liu, Y.-T., Yu, C., Huang, L., Aphasizheva, I., Aphasizhev, R., & Zhou, Z. H. (2023) · Structure · doi:10.1016/j.str.2022.11.015 · Cited by 29
Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport
Shen, J., Hu, M., Fan, X., Ren, Z., Portioli, C., Yan, X., Rong, M., & Zhou, M. (2022) · Structure · doi:10.1016/j.str.2022.04.011 · 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
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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
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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
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Metadata
- Authors
- Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A.
- Venue
- Nature Methods
- Published
- 2017-02-27
- Volume
- 14
- Issue
- 4
- Pages
- 331-332
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2593511418
- Cited by
- 7,777
- References
- 3
- FWCI
- 229.14
- Type
- journal article
- Language
- en
- Open access
- green
- Licence
- www.springer.com/tdm (tdm)
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.