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The nuclear pore complex: understanding its function through structural insight
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Nuclear envelope rupture and repair during cancer cell migration
Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318
The Human Nuclear Pore Complex as Revealed by Cryo-Electron Tomography
Maimon, T., Elad, N., Dahan, I., & Medalia, O. (2012) · Structure · doi:10.1016/j.str.2012.03.025 · Cited by 196
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Self-citationLocal and global influences on protein turnover in neurons and glia
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G4C2 Repeat RNA Initiates a POM121-Mediated Reduction in Specific Nucleoporins in C9orf72 ALS/FTD
Coyne, A. N., Zaepfel, B. L., Hayes, L., Fitchman, B., Salzberg, Y., Luo, E.-C., Bowen, K., Trost, H., Aigner, S., Rigo, F., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.027 · Cited by 156
Coyne, A. N., Baskerville, V., Zaepfel, B. L., Dickson, D. W., Rigo, F., Bennett, F., Lusk, C. P., & Rothstein, J. D. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe1923 · Cited by 143
Nuclear pore complexes — a doorway to neural injury in neurodegeneration
Coyne, A. N., & Rothstein, J. D. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00653-6 · Cited by 96
Postmitotic nuclear pore assembly proceeds by radial dilation of small membrane openings
Otsuka, S., Steyer, A. M., Schorb, M., Hériché, J.-K., Hossain, M. J., Sethi, S., Kueblbeck, M., Schwab, Y., Beck, M., & Ellenberg, J. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0001-9 · Cited by 90
Self-citationSystematic detection of functional proteoform groups from bottom-up proteomic datasets
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Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex
Huang, G., Zhan, X., Zeng, C., Liang, K., Zhu, X., Zhao, Y., Wang, P., Wang, Q., Zhou, Q., Tao, Q., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00633-x · Cited by 33
An essential and highly selective protein import pathway encoded by nucleus-forming phage
Morgan, C. J., Enustun, E., Armbruster, E. G., Birkholz, E. A., Prichard, A., Forman, T., Aindow, A., Wannasrichan, W., Peters, S., Inlow, K., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321190121 · Cited by 25
Khodaeiaminjan, M., Gomes, C., Pagano, A., Kruszka, D., Sulima, P., Przyborowski, J. A., Krajewski, P., & Paiva, J. A. P. (2024) · Physiologia Plantarum · doi:10.1111/ppl.14403 · Cited by 9
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Stuke, J. F. M., & Hummer, G. (2025) · Autophagy · doi:10.1080/15548627.2025.2493999 · Cited by 8
Latham, A. P., Zhang, W., Tempkin, J. O. B., Otsuka, S., Ellenberg, J., & Sali, A. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2415674122 · Cited by 8
Advances in 2,3-Dimethylmaleic Anhydride (DMMA)-Modified Nanocarriers in Drug Delivery Systems
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Multifunctional roles of Brl1-Brr6 in nuclear envelope fusion during nuclear pore complex biogenesis
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Metadata
- Authors
- Beck, M., & Hurt, E.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2016-12-21
- Volume
- 18
- Issue
- 2
- Pages
- 73-89
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2564335181
- Cited by
- 696
- References
- 2
- FWCI
- 3.55
- Type
- journal article
- Language
- en
- Open access
- closed
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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.