ArticleBiophysical journal2005
High-resolution near-field optical imaging of single nuclear pore complexes under physiological conditions.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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
11 citing papers in PubMed.
- High-sensitivity infrared vibrational nanospectroscopy in water.Light, science & applications · 2017Article
- Decoupling absorption and emission processes in super-resolution localization of emitters in a plasmonic hotspot.Nature communications · 2017Article
- Review
- Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy.Nature communications · 2013Article
- A guide to super-resolution fluorescence microscopy.The Journal of cell biology · 2010Review
- Nanoscale imaging of epidermal growth factor receptor clustering: effects of inhibitors.The Journal of biological chemistry · 2010Article
- Nuclear pore disassembly from endoplasmic reticulum membranes promotes Ca2+ signalling competency.The Journal of physiology · 2008Article
- Article
- Vertebrate membrane proteins: structure, function, and insights from biophysical approaches.Pharmacological reviews · 2008Review
- Trends in fluorescence imaging and related techniques to unravel biological information.HFSP journal · 2007Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Scanning near-field optical microscopy (SNOM) circumvents the diffraction limit of conventional light microscopy and is able to achieve optical resolutions substantially below 100 nm. However, in the field of cell biology SNOM has been rarely applied, probably because previous techniques for sample-distance control are less sensitive in liquid than in air. Recently we developed a distance control based on a tuning fork in tapping mode, which is also well-suited for imaging in solution. Here we show that this approach can be used to visualize single membrane protein complexes kept in physiological media throughout. Nuclear envelopes were isolated from Xenopus laevis oocytes at conditions shown recently to conserve the transport functions of the nuclear pore complex (NPC). Isolated nuclear envelopes were fluorescently labeled by antibodies against specific proteins of the NPC (NUP153 and p62) and imaged at a resolution of approximately 60 nm. The lateral distribution of epitopes within the supramolecular NPC could be inferred from an analysis of the intensity distribution of the fluorescence spots. The different number densities of p62- and NUP153-labeled NPCs are determined and discussed. Thus we show that SNOM opens up new possibilities for directly visualizing the transport of single particles through single NPCs and other transporters.
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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.