The DOI matches its Crossref record; 121 of the 121 references it cites were found in a registry or an index.
The Nuclear Pore Complex as a Flexible and Dynamic Gate
Open accessAbstract
Nuclear pore complexes (NPCs) perforate the nuclear envelope and serve as the primary transport gates for molecular exchange between nucleus and cytoplasm. Stripping the megadalton complex down to its most essential organizational elements, one can divide the NPC into scaffold components, and the disordered elements attached to it that generate a selective barrier between compartments. These structural elements exhibit flexibility, which may hold a clue in understanding NPC assembly and function. Here we review the current status of NPC research with a focus on the functional implications of its structural and compositional heterogeneity.
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Citations
Cites
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The molecular architecture of the nuclear pore complex
Alber, F., Dokudovskaya, S., Veenhoff, L. M., Zhang, W., Kipper, J., Devos, D., Suprapto, A., Karni-Schmidt, O., Williams, R., Chait, B. T., et al. (2007) · Nature · doi:10.1038/nature06405 · Cited by 1,057
Proteomic analysis of the mammalian nuclear pore complex
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Nuclear Pore Complex Is Able to Transport Macromolecules with Diameters of ∼39 nm
Panté, N., & Kann, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-06-0308 · Cited by 776
Kinetic analysis of translocation through nuclear pore complexes
Ribbeck, K., & Görlich, D. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1320 · Cited by 772
Identification of long-lived proteins reveals exceptional stability of essential cellular structures
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Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex
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Probing nuclear pore complex architecture with proximity-dependent biotinylation
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Cited by
Integrative structure and functional anatomy of a nuclear pore complex
Kim, S. J., Fernandez-Martinez, J., Nudelman, I., Shi, Y., Zhang, W., Raveh, B., Herricks, T., Slaughter, B. D., Hogan, J. A., Upla, P., et al. (2018) · Nature · doi:10.1038/nature26003 · Cited by 490
Mechanisms and functions of nuclear envelope remodelling
Ungricht, R., & Kutay, U. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.153 · Cited by 346
HIV-1 uncoats in the nucleus near sites of integration
Burdick, R. C., Li, C., Munshi, M., Rawson, J. M. O., Nagashima, K., Hu, W.-S., & Pathak, V. K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920631117 · Cited by 313
“It is unclear how an intact viral core with a width of ∼61 nm (5) can be imported through a NPC with an inner diameter of ∼39 nm (49).”
BackgroundPrinciples for Integrative Structural Biology Studies
Rout, M. P., & Sali, A. (2019) · Cell · doi:10.1016/j.cell.2019.05.016 · Cited by 258
Structure and Assembly of the Nuclear Pore Complex
Hampoelz, B., Andres-Pons, A., Kastritis, P., & Beck, M. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115308 · Cited by 257
Metadata
- Authors
- Knockenhauer, K. E., & Schwartz, T. U.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2016-03
- Volume
- 164
- Issue
- 6
- Pages
- 1162-1171
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2293002570
- Cited by
- 406
- References
- 121
- FWCI
- 23.32
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
