ArticleThe Journal of cell biology1993
Intranuclear filaments containing a nuclear pore complex protein.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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
57 citing papers in PubMed, 130 citations in OpenAlex.
- Regulation of Glycosylation in Bone Metabolism.International journal of molecular sciences · 2024Review
- GBPL3 localizes to the nuclear pore complex and functionally connects the nuclear basket with the nucleoskeleton in plants.PLoS biology · 2022Article
- Review
- Article
- The Nucleoskeleton.Cold Spring Harbor perspectives in biology · 2017Review
- HIV-1 capsid is involved in post-nuclear entry steps.Retrovirology · 2016Article
- Influenza virus-induced caspase-dependent enlargement of nuclear pores promotes nuclear export of viral ribonucleoprotein complexes.Journal of virology · 2015Article
- Nuclear routing networks span between nuclear pore complexes and genomic DNA to guide nucleoplasmic trafficking of biomolecules.Journal of fertilization in vitro · 2012Article
- Routing of Biomolecules and Transgenes' Vectors in Nuclei of Oocytes.Journal of fertilization in vitro · 2012Article
- The nucleoskeleton as a genome-associated dynamic 'network of networks'.Nature reviews. Molecular cell biology · 2011Review
- Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors.The Journal of cell biology · 2006Article
- Nup153 affects entry of messenger and ribosomal ribonucleoproteins into the nuclear basket during export.Molecular biology of the cell · 2005Article
- Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex.Molecular biology of the cell · 2005Article
- Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.Molecular biology of the cell · 2004Article
- NO66, a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin.Molecular biology of the cell · 2004Article
- The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the nuclear envelope and attenuates NES-mediated nuclear export.The Journal of cell biology · 2003Article
- Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.Molecular biology of the cell · 2003Article
- Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains.Molecular and cellular biology · 2002Article
- Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes.Molecular biology of the cell · 2002Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes (NPCs) are anchoring sites of intranuclear filaments of 3-6 nm diameter that are coaxially arranged on the perimeter of a cylinder and project into the nuclear interior for lengths varying in different kinds of cells. Using a specific monoclonal antibody we have found that a polypeptide of approximately 190 kD on SDS-PAGE, which appears to be identical to the recently described NPC protein "nup 153," is a general constituent of these intranuclear NPC-attached filaments in different types of cells from diverse species, including amphibian oocytes where these filaments are abundant and can be relatively long. We have further observed that during mitosis this filament protein transiently disassembles, resulting in a distinct soluble molecular entity of approximately 12.5 S, and then disperses over most of the cytoplasm. Similarly, the amphibian oocyte protein appears in a soluble form of approximately 16 S during meiotic metaphase and can be immunoprecipitated from egg cytoplasmic supernatants. We conclude that this NPC protein can assemble into a filamentous form at considerable distance from the nuclear envelope and discuss possible functions of these NPC-attached filaments, from a role as guidance structure involved in nucleocytoplasmic transport to a form of excess storage of NPC proteins in oocytes.
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Registered trials
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.