ArticleThe Journal of cell biology1984
Movement of a karyophilic protein through the nuclear pores of oocytes.
Article in The Journal of cell biology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 papers.
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Who cites it
169 citing papers in PubMed, 509 citations in OpenAlex.
- GFP-free live neuron quantitative imaging reveals compartmentalization and growth dynamics of polyQ aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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- High-speed super-resolution imaging of rotationally symmetric structures using SPEED microscopy and 2D-to-3D transformation.Nature protocols · 2021Article
- Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-α.Viruses · 2020Article
- Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2.Biochemistry · 2019Article
- In vivo analysis of protein crowding within the nuclear pore complex in interphase and mitosis.Scientific reports · 2017Article
- Review
- Multiple nuclear localization signals mediate nuclear localization of the GATA transcription factor AreA.Eukaryotic cell · 2014Article
- Large cargo transport by nuclear pores: implications for the spatial organization of FG-nucleoporins.The EMBO journal · 2013Article
- Single-molecule analysis of the recognition forces underlying nucleo-cytoplasmic transport.Angewandte Chemie (International ed. in English) · 2013Article
- Review
- Routing of Biomolecules and Transgenes' Vectors in Nuclei of Oocytes.Journal of fertilization in vitro · 2012Article
- The yeast nuclear pore complex and transport through it.Genetics · 2012Article
- Ran-dependent nuclear export mediators: a structural perspective.The EMBO journal · 2011Review
- Nuclear export dynamics of RNA-protein complexes.Nature · 2011Review
- The NPC-transporter, a ghost in the machine.Structure (London, England : 1993) · 2010Article
- A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.Molecular & cellular proteomics : MCP · 2010Article
- Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
109 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has recently been shown that large karyophilic proteins are transported across the nuclear envelope in amphibian oocytes. In consideration of this, the present experiments were performed to identify the specific sites within the envelope through which transport occurs and determine if molecular size is a limiting factor in the transport process. The following experimental procedure was employed: Colloidal gold particles, varying in size from approximately 20 to 170 A in diameter were coated with nucleoplasmin, a 165,000-mol-wt karyophilic protein, which is known to be transported through the envelope. The coated gold particles were microinjected into the cytoplasm of Xenopus oocytes, and the cells were fixed 15 min and 1 h later. The intracellular localization of the gold was then determined with the electron microscope. It was found that nucleoplasmin-coated particles readily enter the nucleus. On the basis of the distribution of the particles associated with the envelope, we concluded that transport occurs through the nuclear pores. Furthermore, the size distributions of the gold particles present in the nucleus and cytoplasm were not significantly different, indicating that the envelope does not discriminate among particles with diameters ranging from 50 to 200 A (the dimensions including the nucleoplasmin coat). Colloidal gold coated with trypsin-digested nucleoplasmin (which lacks the polypeptide domain required for transport) or exogenous polyvinylpyrrolidone were largely excluded from the nucleus and showed no evidence of transport.
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