ArticleBiophysical journal2003
Quantitative topographical analysis of nuclear pore complex function using scanning force microscopy.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Atomic force microscopy reveals structural variability amongst nuclear pore complexes.Life science alliance · 2018Article
- Towards reconciling structure and function in the nuclear pore complex.Histochemistry and cell biology · 2008Review
- Biology and biophysics of the nuclear pore complex and its components.International review of cell and molecular biology · 2008Review
- Article
- Autoantigens of the nuclear pore complex.Journal of molecular medicine (Berlin, Germany) · 2004Review
- Transient permeability leak of nuclear envelope induced by aldosterone.The Journal of membrane biology · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The only avenue for macromolecular communication between nucleoplasmic and cytoplasmic compartments of the cell is through the nuclear pore complexes (NPCs), which are thus situated at a key location for the control of downstream transcriptional processes. The translocation of cargo through the NPC is mediated by transport receptors, which have the difficult task of making specific, yet transitory, interactions with the NPC in order to support efficient transport. In this report we have examined two stages in the translocation process using scanning force microscopy. We show that the initial docking of importin beta 45-462 is rapid and occurs at nanomolar concentrations. Later stages of transport involve translocation through the central lumen of the NPC and are thought to involve hydrophobic interactions between transport receptors and the NPC. Using calcium-depleted nuclear envelopes we argue that luminal regions of the NPC exhibit hydrophobic characteristics that are not observed for other regions of the NPC.
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What OpenQuestion holds
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.