Evidence map›Paper›PMID 36040869›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory.

Yuki Toyama, Atul Kaushik Rangadurai, Julie D Forman-Kay, Lewis E Kay

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.9field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Ion NMR for Biomolecular Systems.Journal of molecular biology · 2025
    Review
  4. Article
  5. Article
  6. Client-scaffold interactions suppress aggregation of a client protein in model condensates.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Crucial role of the cGAS N terminus in mediating flowable and functional cGAS-DNA condensate formation via DNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  20. Review
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.

Yuki ToyamaDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.ORCID 0000-0003-0457-678X
Atul Kaushik RangaduraiDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Julie D Forman-KayDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.ORCID 0000-0001-8265-972X
Lewis E KayDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
University of Toronto · CA

Funding

CIHR FND-148375CIHR FND-503573
6 · The paper itself

Abstract

Electrostatic interactions and charge balance are important for the formation of biomolecular condensates involving proteins and nucleic acids. However, a detailed, atomistic picture of the charge distribution around proteins during the phase-separation process is lacking. Here, we use solution NMR spectroscopy to measure residue-specific near-surface electrostatic potentials (

Indexed as

Biochemical PhenomenaIntrinsically Disordered ProteinsPhase TransitionRNA-Binding ProteinsStatic ElectricityAdenosine TriphosphateNuclear Magnetic Resonance, BiomolecularSurface PropertiesAdenosine TriphosphateIntrinsically Disordered ProteinsRNA-Binding ProteinsATPbiomolecular condensatesintrinsically disordered proteinsparamagnetic relaxation enhancementsolution NMR

Identifiers

PMID36040869
PMCPMC9457416
OpenAlexW4293579455

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.