The DOI matches its Crossref record.
Accurate determination of local defocus and specimen tilt in electron microscopy
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
Cited by
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
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073
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
Structure and mechanogating mechanism of the Piezo1 channel
Zhao, Q., Zhou, H., Chi, S., Wang, Y., Wang, J., Geng, J., Wu, K., Liu, W., Zhang, T., Dong, M.-Q., et al. (2018) · Nature · doi:10.1038/nature25743 · Cited by 628
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
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
Self-citationThe 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
Kirschke, E., Goswami, D., Southworth, D., Griffin, P. R., & Agard, D. A. (2014) · Cell · doi:10.1016/j.cell.2014.04.038 · Cited by 399
Architecture of human mTOR complex 1
Aylett, C. H. S., Sauer, E., Imseng, S., Boehringer, D., Hall, M. N., Ban, N., & Maier, T. (2016) · Science · doi:10.1126/science.aaa3870 · Cited by 344
A wheat resistosome defines common principles of immune receptor channels
Förderer, A., Li, E., Lawson, A. W., Deng, Y.-N., Sun, Y., Logemann, E., Zhang, X., Wen, J., Han, Z., Chang, J., et al. (2022) · Nature · doi:10.1038/s41586-022-05231-w · Cited by 296
Structure of a yeast activated spliceosome at 3.5 Å resolution
Yan, C., Wan, R., Bai, R., Huang, G., & Shi, Y. (2016) · Science · doi:10.1126/science.aag0291 · Cited by 261
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
Subunit Architecture and Functional Modular Rearrangements of the Transcriptional Mediator Complex
Tsai, K.-L., Tomomori-Sato, C., Sato, S., Conaway, R. C., Conaway, J. W., & Asturias, F. J. (2014) · Cell · doi:10.1016/j.cell.2014.05.015 · Cited by 218
Xiao, Y., Luo, M., Hayes, R. P., Kim, J., Ng, S., Ding, F., Liao, M., & Ke, A. (2017) · Cell · doi:10.1016/j.cell.2017.06.012 · Cited by 208
Molecular mechanism of APC/C activation by mitotic phosphorylation
Zhang, S., Chang, L., Alfieri, C., Zhang, Z., Yang, J., Maslen, S., Skehel, M., & Barford, D. (2016) · Nature · doi:10.1038/nature17973 · Cited by 203
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190
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
The role of tubulin–tubulin lattice contacts in the mechanism of microtubule dynamic instability
Manka, S. W., & Moores, C. A. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0087-8 · Cited by 159
Cryo-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
SecM-Stalled Ribosomes Adopt an Altered Geometry at the Peptidyl Transferase Center
Bhushan, S., Hoffmann, T., Seidelt, B., Frauenfeld, J., Mielke, T., Berninghausen, O., Wilson, D. N., & Beckmann, R. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000581 · Cited by 154
Southworth, D. R., & Agard, D. A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.023 · Cited by 143
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
Plant-made polio type 3 stabilized VLPs-a candidate synthetic polio vaccine
Marsian, J., Fox, H., Bahar, M. W., Kotecha, A., Fry, E. E., Stuart, D. I., Macadam, A. J., Rowlands, D. J., & Lomonossoff, G. P. (2017) · Nature Communications · doi:10.1038/s41467-017-00090-w · Cited by 121
Kikkawa, M., & Hirokawa, N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601299 · Cited by 125
Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport
Shima, T., Morikawa, M., Kaneshiro, J., Kambara, T., Kamimura, S., Yagi, T., Iwamoto, H., Uemura, S., Shigematsu, H., Shirouzu, M., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711178 · Cited by 125
Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity
Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., et al. (2013) · Nature Communications · doi:10.1038/ncomms3416 · Cited by 119
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
Jomaa, A., Boehringer, D., Leibundgut, M., & Ban, N. (2016) · Nature Communications · doi:10.1038/ncomms10471 · Cited by 115
A Plug-and-Latch Mechanism for Gating the Mechanosensitive Piezo Channel
Geng, J., Liu, W., Zhou, H., Zhang, T., Wang, L., Zhang, M., Li, Y., Shen, B., Li, X., & Xiao, B. (2020) · Neuron · doi:10.1016/j.neuron.2020.02.010 · Cited by 113
Bhattacharyya, M., Stratton, M. M., Going, C. C., McSpadden, E. D., Huang, Y., Susa, A. C., Elleman, A., Cao, Y. M., Pappireddi, N., Burkhardt, P., et al. (2016) · eLife · doi:10.7554/elife.13405 · Cited by 112
4.4 Å Resolution Cryo-EM structure of human mTOR Complex 1
Yang, H., Wang, J., Liu, M., Chen, X., Huang, M., Tan, D., Dong, M.-Q., Wong, C. C. L., Wang, J., Xu, Y., et al. (2016) · Protein & Cell · doi:10.1007/s13238-016-0346-6 · Cited by 96
Mosadeghi, R., Reichermeier, K. M., Winkler, M., Schreiber, A., Reitsma, J. M., Zhang, Y., Stengel, F., Cao, J., Kim, M., Sweredoski, M. J., et al. (2016) · eLife · doi:10.7554/elife.12102 · Cited by 95
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
Toropova, K., Mladenov, M., & Roberts, A. J. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3391 · Cited by 85
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
Structure of a fungal 1,3-β-glucan synthase
Zhao, C.-R., You, Z.-L., Chen, D.-D., Hang, J., Wang, Z.-B., Ji, M., Wang, L.-X., Zhao, P., Qiao, J., Yun, C.-H., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh7820 · Cited by 75
Jomaa, A., Fu, Y.-H. H., Boehringer, D., Leibundgut, M., Shan, S.-O., & Ban, N. (2017) · Nature Communications · doi:10.1038/ncomms15470 · Cited by 66
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ
Malet, H., Canellas, F., Sawa, J., Yan, J., Thalassinos, K., Ehrmann, M., Clausen, T., & Saibil, H. R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2210 · Cited by 61
Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs
Shigematsu, H., Imasaki, T., Doki, C., Sumi, T., Aoki, M., Uchikubo-Kamo, T., Sakamoto, A., Tokuraku, K., Shirouzu, M., & Nitta, R. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711182 · Cited by 54
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
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer
Wilson, M. D., Renault, L., Maskell, D. P., Ghoneim, M., Pye, V. E., Nans, A., Rueda, D. S., Cherepanov, P., & Costa, A. (2019) · Nature Communications · doi:10.1038/s41467-019-12007-w · Cited by 42
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
A wheat resistosome defines common principles of immune receptor channels
Förderer, A., Li, E., Lawson, A., Deng, Y.-N., Sun, Y., Logemann, E., Zhang, X., Wen, J., Han, Z., Chang, J., et al. (2022) · doi:10.1101/2022.03.23.485489 · Cited by 36
Complex structure of the fission yeast SREBP-SCAP binding domains reveals an oligomeric organization
Gong, X., Qian, H., Shao, W., Li, J., Wu, J., Liu, J.-J., Li, W., Wang, H.-W., Espenshade, P., & Yan, N. (2016) · Cell Research · doi:10.1038/cr.2016.123 · Cited by 31
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
Announcing the first novel class of rapid-onset antidepressants in clinical practice
Fasipe, O., Akhideno, P., Owhin, O., & Ibiyemi-Fasipe, O. (2019) · Journal of Medical Sciences · doi:10.4103/jmedsci.jmedsci_36_19 · Cited by 6
Structural basis for negative regulation of the Escherichia coli maltose system
Wu, Y., Sun, Y., Richet, E., Han, Z., & Chai, J. (2023) · doi:10.21203/rs.3.rs-2326414/v1
Metadata
- Authors
- Mindell, J. A., & Grigorieff, N.
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 142
- Issue
- 3
- Pages
- 334-347
- ISSN
- 1047-8477 (ISSN-L)
- OpenAlex
- W2073949924
- Cited by
- 1,407
- References
- 0
- FWCI
- 14.38
- 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.
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.