Evidence map›Paper›PMID 26712748›Full record

ArticleInternational journal of molecular sciences2015

Compartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments.

Fanchi Meng, Insung Na, Lukasz Kurgan, Vladimir N Uversky

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Prediction of Disordered Linkers Using APOD.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. Evaluation of predictions of disordered binding regions in the CAID2 experiment.Computational and structural biotechnology journal · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Chaotic aging: intrinsically disordered proteins in aging-related processes.Cellular and molecular life sciences : CMLS · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Deep learning in prediction of intrinsic disorder in proteins.Computational and structural biotechnology journal · 2022
    Review
  18. Article
  19. Article
  20. Article
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 3 institutions in 4 countries.

Fanchi MengDepartment of Electrical and Computer Engineering, University of Alberta, Edmonton, AB T6G 2V4, Canada. fanchi@ualberta.ca.
Insung NaDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA. ina2@health.usf.edu.
Lukasz KurganDepartment of Electrical and Computer Engineering, University of Alberta, Edmonton, AB T6G 2V4, Canada. lkurgan@ualberta.ca.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA. vuversky@health.usf.edu.
University of Alberta · CAKing Abdulaziz University · SAUniversity of South Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell nucleus contains a number of membrane-less organelles or intra-nuclear compartments. These compartments are dynamic structures representing liquid-droplet phases which are only slightly denser than the bulk intra-nuclear fluid. They possess different functions, have diverse morphologies, and are typically composed of RNA (or, in some cases, DNA) and proteins. We analyzed 3005 mouse proteins localized in specific intra-nuclear organelles, such as nucleolus, chromatin, Cajal bodies, nuclear speckles, promyelocytic leukemia (PML) nuclear bodies, nuclear lamina, nuclear pores, and perinuclear compartment and compared them with ~29,863 non-nuclear proteins from mouse proteome. Our analysis revealed that intrinsic disorder is enriched in the majority of intra-nuclear compartments, except for the nuclear pore and lamina. These compartments are depleted in proteins that lack disordered domains and enriched in proteins that have multiple disordered domains. Moonlighting proteins found in multiple intra-nuclear compartments are more likely to have multiple disordered domains. Protein-protein interaction networks in the intra-nuclear compartments are denser and include more hubs compared to the non-nuclear proteins. Hubs in the intra-nuclear compartments (except for the nuclear pore) are enriched in disorder compared with non-nuclear hubs and non-nuclear proteins. Therefore, our work provides support to the idea of the functional importance of intrinsic disorder in the cell nucleus and shows that many proteins associated with sub-nuclear organelles in nuclei of mouse cells are enriched in disorder. This high level of disorder in the mouse nuclear proteins defines their ability to serve as very promiscuous binders, possessing both large quantities of potential disorder-based interaction sites and the ability of a single such site to be involved in a large number of interactions.

Indexed as

Amino Acid SequenceAnimalsCell NucleusDNA-Binding ProteinsIntrinsically Disordered ProteinsMiceMolecular Sequence DataProtein BindingProteomeRNA-Binding ProteinsDNA-Binding ProteinsIntrinsically Disordered ProteinsProteomeRNA-Binding Proteinscell nucleusDNA-binding proteinintra-nuclear compartmentsintrinsically disordered proteinmembrane-less organellesRNA-binding protein

Identifiers

PMID26712748
PMCPMC4730271
OpenAlexW2218000956

What OpenQuestion holds

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Registered trials

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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.