The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Cryo-EM: A Unique Tool for the Visualization of Macromolecular Complexity
Open accessAbstract
Three-dimensional cryo-electron microscopy (cryo-EM) is an expanding structural biology technique that has recently undergone a quantum leap progression in its achievable resolution and its applicability to the study of challenging biological systems. Because crystallization is not required, only small amounts of sample are needed, and, because images can be classified in a computer, the technique has the potential to deal with compositional and conformational mixtures. Therefore, cryo-EM can be used to investigate complete and fully functional macromolecular complexes in different functional states, providing a richness of biological insight. In this review we underlie some of the principles behind the cryo-EM methodology of single particle analysis and discuss some recent results of its application to challenging systems of paramount biological importance. We place special emphasis on new methodological developments that are leading to an explosion of new studies, many of which are reaching resolutions that could only be dreamed of only a couple of years ago.
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
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
Self-citationDynamic instability of microtubule growth
Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
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
Self-citationFan, L., Fuss, J. O., Cheng, Q. J., Arvai, A. S., Hammel, M., Roberts, V. A., Cooper, P. K., & Tainer, J. A. (2008) · Cell · doi:10.1016/j.cell.2008.04.030 · Cited by 369
Cited by
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Li, T., Nowell, C. J., Cipolla, D., Rades, T., & Boyd, B. J. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.8b01308 · Cited by 57
Integrative Structural Biology in the Era of Accurate Structure Prediction
Masrati, G., Landau, M., Ben-Tal, N., Lupas, A., Kosloff, M., & Kosinski, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167127 · Cited by 53
Apolipoprotein E secreted by astrocytes forms antiparallel dimers in discoidal lipoproteins
Strickland, M. R., Rau, M. J., Summers, B., Basore, K., Wulf, J., Jiang, H., Chen, Y., Ulrich, J. D., Randolph, G. J., Zhang, R., et al. (2024) · Neuron · doi:10.1016/j.neuron.2023.12.018 · Cited by 28
Amani, K., Shivnauth, V., & Castroverde, C. D. M. (2023) · Plant Direct · doi:10.1002/pld3.509 · Cited by 5
From Signal to Symphony: Exploring 2D Sequence Representations for Protein Function Prediction
Wang, Y., Cai, M., Dong, Y., Ma, Y., & Wei, K. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01768 · Cited by 3
Metadata
- Authors
- Nogales, E., & Scheres, S. H. W.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-05
- Volume
- 58
- Issue
- 4
- Pages
- 677-689
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1520649887
- Cited by
- 378
- References
- 6
- FWCI
- 16.42
- Type
- journal article
- Language
- en
- Open access
- bronze
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.