ArticleJournal of molecular biology2007
Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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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
32 citing papers in PubMed, 49 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
- A Pan-Cancer Analysis of the Oncogenic Role of Nuclear Transport Factor 2 in Human Cancers.Frontiers in oncology · 2022Article
- The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021Review
- One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex.Trends in biochemical sciences · 2021Review
- Persistent growth of microtubules at low density.Molecular biology of the cell · 2021Article
- Microtubules in Influenza Virus Entry and Egress.Viruses · 2020Review
- Near-Infrared Light-Controlled Gene Expression and Protein Targeting in Neurons and Non-neuronal Cells.Chembiochem : a European journal of chemical biology · 2018Article
- Article
- Karyopherins regulate nuclear pore complex barrier and transport function.The Journal of cell biology · 2017Article
- Article
- In vivo analysis of protein crowding within the nuclear pore complex in interphase and mitosis.Scientific reports · 2017Article
- Cinnamaldehyde and eugenol change the expression folds of AKT1 and DKC1 genes and decrease the telomere length of human adipose-derived stem cells (hASCs): An experimental and in silico study.Iranian journal of basic medical sciences · 2017Article
- Deciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches.Journal of molecular biology · 2016Review
- CGG Repeats in the 5'UTR of FMR1 RNA Regulate Translation of Other RNAs Localized in the Same RNA Granules.PloS one · 2016Article
- Promiscuous binding of Karyopherinβ1 modulates FG nucleoporin barrier function and expedites NTF2 transport kinetics.Biophysical journal · 2015Article
- How to operate a nuclear pore complex by Kap-centric control.Nucleus (Austin, Tex.) · 2015Review
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- Selective transport control on molecular velcro made from intrinsically disordered proteins.Nature nanotechnology · 2014Article
- Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins.Biophysical journal · 2014Article
- Model inspired by nuclear pore complex suggests possible roles for nuclear transport receptors in determining its structure.Biophysical journal · 2013Article
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 1 institution in 1 country.
Funding
Abstract
Nuclear transport requires freely diffusing nuclear transport proteins to facilitate movement of cargo molecules through the nuclear pore. We analyzed dynamic properties of importin alpha, importin beta, Ran and NTF2 in nucleus, cytoplasm and at the nuclear pore of neuroblastoma cells using fluorescence correlation spectroscopy. Mobile components were quantified by global fitting of autocorrelation data from multiple cells. Immobile components were quantified by analysis of photobleaching kinetics. Wild-type Ran was compared to various mutant Ran proteins to identify components representing GTP or GDP forms of Ran. Untreated cells were compared to cells treated with nocodazole or latrunculin to identify components associated with cytoskeletal elements. The results indicate that freely diffusing importin alpha, importin beta, Ran and NTF2 are in dynamic equilibrium with larger pools associated with immobile binding partners such as microtubules in the cytoplasm. These findings suggest that formation of freely diffusing nuclear transport intermediates is in competition with binding to immobile partners. Variation in concentrations of freely diffusing nuclear transport intermediates among cells indicates that the nuclear transport system is sufficiently robust to function over a wide range of conditions.
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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.