ArticleThe EMBO journal2009
Cargo surface hydrophobicity is sufficient to overcome the nuclear pore complex selectivity barrier.
Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 80 citations in OpenAlex.
- Passive nuclear transport deviates from Fickian behavior in prostate and breast cell types.Nucleus (Austin, Tex.) · 2026Article
- In-Depth Study of Low-Complexity Domains: From Structural Diversity to Disease Mechanisms.Cells · 2025Review
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Comparative toxicity study of three surface-modified titanium dioxide nanoparticles following subacute inhalation.Particle and fibre toxicology · 2025Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Nuclear envelope budding and its cellular functions.Nucleus (Austin, Tex.) · 2023Article
- Colocalization Analysis of Peripheral Myelin Protein-22 and Lamin-B1 in the Schwann Cell Nuclei of Wt and TrJ Mice.Biomolecules · 2022Article
- Mutant libraries reveal negative design shielding proteins from supramolecular self-assembly and relocalization in cells.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- The Nuclear Pore Complex and mRNA Export in Cancer.Cancers · 2020Review
- The mechanistic role of alpha-synuclein in the nucleus: impaired nuclear function caused by familial Parkinson's disease SNCA mutations.Human molecular genetics · 2020Article
- Article
- Nucleocytoplasmic transport of intrinsically disordered proteins studied by high-speed super-resolution microscopy.Protein science : a publication of the Protein Society · 2020Article
- Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2.Biochemistry · 2019Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- The coming-of-age of nucleocytoplasmic transport in motor neuron disease and neurodegeneration.Cellular and molecular life sciences : CMLS · 2019Review
- Simple rules for passive diffusion through the nuclear pore complex.The Journal of cell biology · 2016Article
- The selective permeability barrier in the nuclear pore complex.Nucleus (Austin, Tex.) · 2016Review
- 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
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To fulfil their function, nuclear pore complexes (NPCs) must discriminate between inert proteins and nuclear transport receptors (NTRs), admitting only the latter. This specific permeation is thought to depend on interactions between hydrophobic patches on NTRs and phenylalanine-glycine (FG) or related repeats that line the NPC. Here, we tested this premise directly by conjugating different hydrophobic amino-acid analogues to the surface of an inert protein and examining its ability to cross NPCs unassisted by NTRs. Conjugation of as few as four hydrophobic moieties was sufficient to enable passage of the protein through NPCs. Transport of the modified protein proceeded with rates comparable to those measured for the innate protein when bound to an NTR and was relatively insensitive both to the nature and density of the amino acids used to confer hydrophobicity. The latter observation suggests a non-specific, small, and plant interaction network between cargo and FG repeats.
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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.