ArticleEMBO reports2002
Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes.
Article in EMBO reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 50 citations in OpenAlex.
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Characterization of cell-to-cell variation in nuclear transport rates and identification of its sources.iScience · 2023Article
- Characterizing Binding Interactions That Are Essential for Selective Transport through the Nuclear Pore Complex.International journal of molecular sciences · 2021Article
- DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins.Journal of the American Chemical Society · 2021Article
- Bound-State Diffusion due to Binding to Flexible Polymers in a Selective Biofilter.Biophysical journal · 2020Article
- Design principles of selective transport through biopolymer barriers.Physical review. E · 2019Article
- Polymer translocation through a hairy channel mimicking the inner plug of a nuclear pore complex.European biophysics journal : EBJ · 2019Article
- How to operate a nuclear pore complex by Kap-centric control.Nucleus (Austin, Tex.) · 2015Review
- Single-molecule studies of nucleocytoplasmic transport: from one dimension to three dimensions.Integrative biology : quantitative biosciences from nano to macro · 2012Review
- Dynamics of single mRNP nucleocytoplasmic transport and export through the nuclear pore in living cells.Nature cell biology · 2010Article
- Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.Eukaryotic cell · 2009Review
- Functionalization of a nanopore: the nuclear pore complex paradigm.Biochimica et biophysica acta · 2009Review
- A top-down approach to mechanistic biological modeling: application to the single-chain antibody folding pathway.Biophysical journal · 2008Article
- Continuous fluorescence microphotolysis and correlation spectroscopy using 4Pi microscopy.Biophysical journal · 2007Article
- The nuclear pore complex: the gateway to successful nonviral gene delivery.Pharmaceutical research · 2006Review
- Nanopore unitary permeability measured by electrochemical and optical single transporter recording.Biophysical journal · 2005Article
- Nuclear transport of single molecules: dwell times at the nuclear pore complex.The Journal of cell biology · 2005Article
- Metastable network model of protein transport through nuclear pores.Biophysical journal · 2004Article
- Optical microwell assay of membrane transport kinetics.Biophysical journal · 2003Article
- On the right track: following the nucleo-cytoplasmic path of an mRNA.Nucleus (Austin, Tex.)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
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism by which macromolecules are translocated through the nuclear pore complex (NPC) is little understood. However, recent measurements of nuclear transport in permeabilized cells showed that molecules binding to phenylalanine-glycine-rich repeats (FG repeats) in NPC proteins were translocated much faster through the NPC than molecules not interacting with FG repeats. We have studied that substrate preference of the NPC in isolated oocyte nuclei and purified nuclear envelopes by optical single transporter recording. NTF2, the transport receptor of RanGDP, was exported approximately 30 times faster than green fluorescent protein, an inert molecule of approximately the same size. The data confirm that restricted diffusion of inert molecules and facilitated transport of FG-repeat binding proteins are basic types of translocation through the NPC, demonstrating that the functional integrity of the NPC can be conserved in isolated nuclei and nuclear envelopes and thus opening new avenues to the analysis of nucleocytoplasmic transport.
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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.