ArticleCell research2020
Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.
Article in Cell research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 62 citations in OpenAlex.
- Visualizing nuclear pore complex plasticity with pan-expansion microscopy.The Journal of cell biology · 2025Article
- Visualizing nuclear pore complex plasticity with pan-Expansion Microscopy.bioRxiv : the preprint server for biology · 2025Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- Unlocking the Gateway: The Spatio-Temporal Dynamics of the p53 Family Driven by the Nuclear Pores and Its Implication for the Therapeutic Approach in Cancer.International journal of molecular sciences · 2024Review
- Overcoming resolution attenuation during tilted cryo-EM data collection.Nature communications · 2024Article
- Plant nuclear envelope as a hub connecting genome organization with regulation of gene expression.Nucleus (Austin, Tex.) · 2023Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels.Nature structural & molecular biology · 2023Article
- Article
- Insights into the role of Nup62 and Nup93 in assembling cytoplasmic ring and central transport channel of the nuclear pore complex.Molecular biology of the cell · 2022Article
- Application of Peptides in Construction of Nonviral Vectors for Gene Delivery.Nanomaterials (Basel, Switzerland) · 2022Review
- 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.Protein & cell · 2022Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold.Science (New York, N.Y.) · 2022Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex.Cell research · 2022Article
- Near-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex.Cell research · 2022Article
- Review
- Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex.Cell research · 2022Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear pore complex (NPC) exhibits structural plasticity and has only been characterized at local resolutions of up to 15 Å for the cytoplasmic ring (CR). Here we present a single-particle cryo-electron microscopy (cryo-EM) structure of the CR from Xenopus laevis NPC at average resolutions of 5.5-7.9 Å, with local resolutions reaching 4.5 Å. Improved resolutions allow identification and placement of secondary structural elements in the majority of the CR components. The two Y complexes in each CR subunit interact with each other and associate with those from flanking subunits, forming a circular scaffold. Within each CR subunit, the Nup358-containing region wraps around the stems of both Y complexes, likely stabilizing the scaffold. Nup205 connects the short arms of the two Y complexes and associates with the stem of a neighboring Y complex. The Nup214-containing region uses an extended coiled-coil to link Nup85 of the two Y complexes and protrudes into the axial pore of the NPC. These previously uncharacterized structural features reveal insights into NPC assembly.
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