ArticleBiophysical journal2008
4Pi microscopy of the nuclear pore complex.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 47 citations in OpenAlex.
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- Combined alteration of lamin and nuclear morphology influences the localization of the tumor-associated factor AKTIP.Journal of experimental & clinical cancer research : CR · 2022Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Super-Resolution Microscopy of Chromatin.Genes · 2019Review
- Intrinsic refractive index matched 3D dSTORM with two objectives: Comparison of detection techniques.Scientific reports · 2018Article
- Nuclear pore complex plasticity during developmental process as revealed by super-resolution microscopy.Scientific reports · 2017Article
- Single-Molecule Real-Time 3D Imaging of the Transcription Cycle by Modulation Interferometry.Cell · 2016Article
- Multiscale dynamics in nucleocytoplasmic transport.Current opinion in cell biology · 2012Review
- Single-molecule studies of nucleocytoplasmic transport: from one dimension to three dimensions.Integrative biology : quantitative biosciences from nano to macro · 2012Review
- Nuclear export dynamics of RNA-protein complexes.Nature · 2011Review
- A readily retrievable pool of synaptic vesicles.Nature neuroscience · 2011Article
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Journal of cell science · 2011Article
- A guide to super-resolution fluorescence microscopy.The Journal of cell biology · 2010Review
- Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.The EMBO journal · 2010Article
- AP-1/sigma1B-adaptin mediates endosomal synaptic vesicle recycling, learning and memory.The EMBO journal · 2010Article
- Structure, dynamics and function of nuclear pore complexes.Trends in cell biology · 2008Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
To explore whether super-resolution fluorescence microscopy is able to resolve topographic features of single cellular protein complexes, a two-photon 4Pi microscope was used to study the nuclear pore complex (NPC). The microscope had an axial resolution of 110-130 nm and a two-color localization accuracy of 5-10 nm. In immune-labeled HeLa cells, NPCs could be resolved much better by 4Pi than by confocal microscopy. When two epitopes of the NPC, one localized at the tip of the cytoplasmic filaments and the other at the ring of the nuclear basket, were immune-labeled, they could be clearly resolved in single NPCs, with the distance between them determined to be 152 +/- 30 nm. In cells expressing a green fluorescent protein construct localized at the NPC center, the distances between the ring of the nuclear filaments and the NPC center was 76 +/- 12 (Potorous tridactylus cells) or 91 +/- 21 nm (normal rat kidney cells), whereas the distance between the NPC center and the tips of the cytoplasmic filaments was 84 +/- 18 nm, all values in good agreement with previous electron or single-molecule fluorescence estimates. We conclude that super-resolution fluorescence microscopy is a powerful method for analyzing single protein complexes and the cellular nanomachinery in general.
Indexed as
Identifiers
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.