ReviewJournal of molecular biology2016
Deciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches.
Review in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- The nuclear envelope and nuclear pore complexes in neurodegenerative diseases.Frontiers in cell and developmental biology · 2025Review
- Kinetic cooperativity resolves bidirectional clogging within the nuclear pore complex.Biophysical journal · 2024Article
- Self-regulation of the nuclear pore complex enables clogging-free crowded transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- On the role of phase separation in the biogenesis of membraneless compartments.The EMBO journal · 2022Article
- Parallel import mechanisms ensure the robust nuclear localization of actin inFrontiers in molecular biosciences · 2022Article
- Super-resolved 3D tracking of cargo transport through nuclear pore complexes.Nature cell biology · 2022Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Nanoelectrochemical Study of Molecular Transport through the Nuclear Pore Complex.Chemical record (New York, N.Y.) · 2021Review
- Article
- Nanocompartmentalization of the Nuclear Pore Lumen.Biophysical journal · 2020Article
- Probing High Permeability of Nuclear Pore Complexes by Scanning Electrochemical Microscopy: CaAnalytical chemistry · 2019Article
- The path of pre-ribosomes through the nuclear pore complex revealed by electron tomography.Nature communications · 2019Article
- Article
- Article
- Multi-color single-molecule tracking and subtrajectory analysis for quantification of spatiotemporal dynamics and kinetics upon T cell activation.Scientific reports · 2017Article
- Floppy but not sloppy: Interaction mechanism of FG-nucleoporins and nuclear transport receptors.Seminars in cell & developmental biology · 2017Review
- Localisation Microscopy of Breast Epithelial ErbB-2 Receptors and Gap Junctions: Trafficking after γ-Irradiation, Neuregulin-1β, and Trastuzumab Application.International journal of molecular sciences · 2017Article
- Temporal and spatial regulation of mRNA export: Single particle RNA-imaging provides new tools and insights.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Due to its central role in macromolecular trafficking and nucleocytoplasmic information transfer, the nuclear pore complex (NPC) has been studied in great detail using a wide spectrum of methods. Consequently, many aspects of its architecture, general function, and role in the life cycle of a cell are well understood. Over the last decade, fluorescence microscopy methods have enabled the real-time visualization of single molecules interacting with and transiting through the NPC, allowing novel questions to be examined with nanometer precision. While initial single-molecule studies focused primarily on import pathways using permeabilized cells, it has recently proven feasible to investigate the export of mRNAs in living cells. Single-molecule assays can address questions that are difficult or impossible to answer by other means, yet the complexity of nucleocytoplasmic transport requires that interpretation be based on a firm genetic, biochemical, and structural foundation. Moreover, conceptually simple single-molecule experiments remain technically challenging, particularly with regard to signal intensity, signal-to-noise ratio, and the analysis of noise, stochasticity, and precision. We discuss nuclear transport issues recently addressed by single-molecule microscopy, evaluate the limits of existing assays and data, and identify open questions for future studies. We expect that single-molecule fluorescence approaches will continue to be applied to outstanding nucleocytoplasmic transport questions, and that the approaches developed for NPC studies are extendable to additional complex systems and pathways within cells.
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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.