Evidence map›Paper›PMID 25229147›Full record

ArticleBiophysical journal2014

Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations.

Ali Ghavami, Liesbeth M Veenhoff, Erik van der Giessen, Patrick R Onck

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 133 citations in OpenAlex.

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  12. Article
  13. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  14. Review
  15. A One-Bead-Per-Saccharide (1BPS) Model for Glycosaminoglycans.Journal of chemical theory and computation · 2023
    Article
  16. Phase separation of intrinsically disordered FG-Nups is driven by highly dynamic FG motifs.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. 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 · 2023
    Article

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Ali GhavamiZernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands.
Liesbeth M VeenhoffEuropean Institute for the Biology of Ageing, University of Groningen, Groningen, The Netherlands.
Erik van der GiessenZernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands.
Patrick R OnckZernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands. Electronic address: p.r.onck@rug.nl.
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The distribution of disordered proteins (FG-nups) that line the transport channel of the nuclear pore complex (NPC) is investigated by means of coarse-grained molecular dynamics simulations. A one-bead-per-amino-acid model is presented that accounts for the hydrophobic/hydrophilic and electrostatic interactions between different amino acids, polarity of the solvent, and screening of free ions. The results indicate that the interaction of the FG-nups forms a high-density, doughnut-like distribution inside the NPC, which is rich in FG-repeats. We show that the obtained distribution is encoded in the amino-acid sequence of the FG-nups and is driven by both electrostatic and hydrophobic interactions. To explore the relation between structure and function, we have systematically removed different combinations of FG-nups from the pore to simulate inviable and viable NPCs that were previously studied experimentally. The obtained density distributions show that the maximum density of the FG-nups inside the pore does not exceed 185 mg/mL in the inviable NPCs, whereas for the wild-type and viable NPCs, this value increases to 300 mg/mL. Interestingly, this maximum density is not correlated to the total mass of the FG-nups, but depends sensitively on the specific combination of essential Nups located in the central plane of the NPC.

Indexed as

Molecular Dynamics SimulationCell SurvivalFungal ProteinsHydrophobic and Hydrophilic InteractionsNuclear Pore Complex ProteinsProtein Structure, TertiaryProtein TransportRepetitive Sequences, Amino AcidStatic ElectricityFungal ProteinsNuclear Pore Complex Proteins

Identifiers

PMID25229147
PMCPMC4167297
OpenAlexW2134814048

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.