ArticleMolecular biology of the cell1995
Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex.
Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
67 citing papers in PubMed, 156 citations in OpenAlex.
- Light and Shadows: Insights from Large-Scale Visual Screens for Arabidopsis Leaf Morphology Mutants.International journal of molecular sciences · 2025Review
- Identification of divergentbioRxiv : the preprint server for biology · 2025Article
- NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility.Nature communications · 2022Article
- Molecular and structural analysis of central transport channel in complex with Nup93 of nuclear pore complex.Protein science : a publication of the Protein Society · 2020Article
- Nuclear pore protein Nup98 is involved in replication of Rift Valley fever virus and nuclear import of virulence factor NSs.The Journal of general virology · 2020Article
- Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 1 Beta Interacts with Nucleoporin 62 To Promote Viral Replication and Immune Evasion.Journal of virology · 2019Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Sliding Mechanism at a Coiled-Coil Interface.Biophysical journal · 2019Article
- Nucleoporin Nup58 localizes to centrosomes and mid-bodies during mitosis.Cell division · 2019Article
- Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.Molecular & cellular proteomics : MCP · 2016Article
- Review
- Architecture of the fungal nuclear pore inner ring complex.Science (New York, N.Y.) · 2015Article
- Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution.The Journal of biological chemistry · 2015Article
- Identification of P-glycoprotein co-fractionating proteins and specific binding partners in rat brain microvessels.Journal of neurochemistry · 2015Article
- The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Molecular biology of the cell · 2014Article
- Cancer driver candidate genes AVL9, DENND5A and NUPL1 contribute to MDCK cystogenesis.Oncoscience · 2014Article
- Nucleoporin Nup62 maintains centrosome homeostasis.Cell cycle (Georgetown, Tex.) · 2013Article
- Ring cycle for dilating and constricting the nuclear pore.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- In vivo analysis of human nucleoporin repeat domain interactions.Molecular biology of the cell · 2013Article
- Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes.The EMBO journal · 2013Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The p62 complex is an oligomeric assembly of O-linked glycoproteins of the nuclear pore complex that interacts with cytosolic transport factors and is part of the machinery for nuclear protein import. In this study we have purified the p62 complex from rat liver nuclear envelopes and analyzed its structure and composition. The p62 complex consists of four distinct polypeptides (p62, p58, p54, and p45) and has a mass of approximately 234 kDa, calculated from its hydrodynamic properties and supported by chemical cross-linking and scanning transmission electron microscopy. These data suggest that the p62 complex contains one copy of each constituent polypeptide. Analysis of preparations of the p62 complex by electron microscopy using rotary metal shadowing and negative staining revealed donut-shaped particles with a diameter of approximately 15 nm. Immunogold electron microscopy of isolated rat liver nuclear envelopes demonstrated that p62 occurs on both the nucleoplasmic and cytoplasmic sides of the pore complex near the central gated channel involved in active transport of proteins and RNAs. The properties and localization of the p62 complex suggest that it may be involved in binding transport ligands near the center of the nuclear pore complex and in subsequently transferring them to the gated transport channel.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.