ArticleProceedings of the National Academy of Sciences of the United States of America2004
Imaging of single-molecule translocation through nuclear pore complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 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.
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Who cites it
150 citing papers in PubMed, 266 citations in OpenAlex.
- RNA export through the nuclear pore complex: pathways, mechanisms, and imaging strategies.RNA biology · 2026Review
- Multiscale Architecture and Mechanics of the Cell Nucleus: Implications for Disease, Bioengineering and Nanomedicine.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Toward an integrated view of nuclear pore transport.Trends in cell biology · 2026Review
- The structural basis of RanGAP1 regulation and catalysis in nuclear transport.bioRxiv : the preprint server for biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Mechanical Coupling With the Nuclear Envelope Shapes the Schizosaccharomyces pombe Mitotic Spindle.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.Nature communications · 2025Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025Review
- The nuclear envelope and nuclear pore complexes in neurodegenerative diseases.Frontiers in cell and developmental biology · 2025Review
- The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection.PLoS pathogens · 2025Article
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection.bioRxiv : the preprint server for biology · 2024Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Dynamics of nuclear export of pre-ribosomal subunits revealed by high-speed single-molecule microscopy in live cells.iScience · 2023Article
- Single-molecule tracking (SMT): a window into live-cell transcription biochemistry.Biochemical Society transactions · 2023Article
- Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.Nature communications · 2023Article
90 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Nuclear pore complexes (NPCs) mediate bidirectional transport of proteins, RNAs, and ribonucleoprotein complexes across the double-membrane nuclear envelope. In vitro studies with purified transport cofactors have revealed a general scheme of cofactor-dependent transport energetically driven by the G protein Ran. However, the size and complexity of NPCs have made it difficult to clearly define the loci and kinetics of the cofactor-NPC interactions required for transport. We now report the use of single-molecule fluorescence microscopy to directly monitor a model protein substrate undergoing transport through NPCs in permeabilized cells. This substrate, NLS-2xGFP, interacts with NPCs for an average of 10 +/- 1 ms during transport. However, because the maximum nuclear accumulation rate of NLS-2xGFP was measured to be at least approximately 10(3) molecules per NPC per s, NPCs must be capable of transporting at least approximately 10 substrate molecules simultaneously. Molecular tracking reveals that substrate molecules spend most of their transit time randomly moving in the central pore of the NPC and that the rate-limiting step is escape from the central pore.
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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.