Evidence map›Paper›PMID 34164013›Full record

ArticleChemical science2020

Does liquid-liquid phase separation drive peptide folding?

Dean N Edun, Meredith R Flanagan, Arnaldo L Serrano

Abstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Ultrafast Spectroscopy Reveals Slow Water Dynamics in Biocondensates.Journal of the American Chemical Society · 2023
    Article
  8. Article
  9. Cross-α/β polymorphism of PSMα3 fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. 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

3 authors.

Dean N EdunDepartment of Chemistry and Biochemistry, University of Notre Dame Notre Dame Indiana 46556 USA arnaldo.serrano@nd.edu.ORCID https://orcid.org/0000-0002-6509-4218
Meredith R FlanaganDepartment of Chemistry and Biochemistry, University of Notre Dame Notre Dame Indiana 46556 USA arnaldo.serrano@nd.edu.
Arnaldo L SerranoDepartment of Chemistry and Biochemistry, University of Notre Dame Notre Dame Indiana 46556 USA arnaldo.serrano@nd.edu.ORCID https://orcid.org/0000-0002-7268-1306

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proline-arginine (PR) dipeptide repeats have been shown to undergo liquid-liquid phase separation and are an example of a growing number of intrinsically disordered proteins that can assemble into membraneless organelles. These structures have been posited as nucleation sites for pathogenic protein aggregation. As such, a better understanding of the effects that the increased local concentration and volumetric crowding within droplets have on peptide secondary structure is necessary. Herein we use Fourier transform infrared (FTIR) and two-dimensional infrared (2DIR) spectroscopy to show that formation of droplets by PR

Identifiers

PMID34164013
PMCPMC8179267

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.