Evidence map›Paper›PMID 36528065›Full record

ArticleThe Journal of biological chemistry2023

Intrinsically disordered regions that drive phase separation form a robustly distinct protein class.

Ayyam Y Ibrahim, Nathan P Khaodeuanepheng, Dhanush L Amarasekara, John J Correia, Karen A Lewis, Nicholas C Fitzkee, Loren E Hough, Steven T Whitten

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
8.1field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Article
  10. Investigating Phase Separation in Genome Folding via Multiscale Computational Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  11. Article
  12. Review
  13. Article
  14. bioRxiv : the preprint server for biology · 2026
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

16 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

8 authors at 4 institutions in 1 country.

Ayyam Y IbrahimDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas, USA.
Nathan P KhaodeuanephengDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas, USA.
Dhanush L AmarasekaraDepartment of Chemistry, Mississippi State University, Mississippi, USA.
John J CorreiaDepartment of Cell and Molecular Biology, University of Mississippi Medical Center, Jackson, Mississippi, USA.
Karen A LewisDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas, USA.
Nicholas C FitzkeeDepartment of Chemistry, Mississippi State University, Mississippi, USA.
Loren E HoughDepartment of Physics, University of Colorado Boulder, Boulder, Colorado, USA; BioFrontiers Institute, University of Colorado Boulder, Boulder, Colorado, USA. Electronic address: loren.hough@colorado.edu.
Steven T WhittenDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas, USA. Electronic address: steve.whitten@txstate.edu.
Texas State University · USMississippi State University · USUniversity of Colorado Boulder · USUniversity of Mississippi Medical Center · US

Funding

South Texas Doctoral Bridge ProgramR25GM102783 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI OYAJOBI, BABATUNDE OLUKAYODE, WHITTEN, STEVEN T · 2013 to 2022
$3.1M
Molecular dissection of the C-terminal tails of tubulin and the effect of their polyglycylation on binding and microtubule assemblyR35GM119755 · NIGMS · UNIVERSITY OF COLORADO · PI HOUGH, LOREN E · 2016 to 2020
$1.8M
Structure, Orientation, and Competitive Interactions of S. Epidermidis Biofilm Proteins on SurfacesR01AI139479 · NIAID · MISSISSIPPI STATE UNIVERSITY · PI FITZKEE, NICHOLAS C · 2018 to 2022
$1.8M
Molecular Mechanisms of the Posttranscriptional Regulator LARP6R15GM119096 · NIGMS · TEXAS STATE UNIVERSITY · PI LEWIS, KAREN ADELL · 2016 to 2019
$891k
NIAID NIH HHS R01 AI139479NIGMS NIH HHS R15 GM119096NIGMS NIH HHS R25 GM102783NIGMS NIH HHS R35 GM119755
6 · The paper itself

Abstract

Protein phase separation is thought to be a primary driving force for the formation of membrane-less organelles, which control a wide range of biological functions from stress response to ribosome biogenesis. Among phase-separating (PS) proteins, many have intrinsically disordered regions (IDRs) that are needed for phase separation to occur. Accurate identification of IDRs that drive phase separation is important for testing the underlying mechanisms of phase separation, identifying biological processes that rely on phase separation, and designing sequences that modulate phase separation. To identify IDRs that drive phase separation, we first curated datasets of folded, ID, and PS ID sequences. We then used these sequence sets to examine how broadly existing amino acid property scales can be used to distinguish between the three classes of protein regions. We found that there are robust property differences between the classes and, consequently, that numerous combinations of amino acid property scales can be used to make robust predictions of protein phase separation. This result indicates that multiple, redundant mechanisms contribute to the formation of phase-separated droplets from IDRs. The top-performing scales were used to further optimize our previously developed predictor of PS IDRs, ParSe. We then modified ParSe to account for interactions between amino acids and obtained reasonable predictive power for mutations that have been designed to test the role of amino acid interactions in driving protein phase separation. Collectively, our findings provide further insight into the classification of IDRs and the elements involved in protein phase separation.

Indexed as

Intrinsically Disordered ProteinsAmino AcidsProtein DomainsAmino AcidsIntrinsically Disordered Proteinsintrinsically disordered proteinprotein-protein interactionprotein self-assemblyprotein sequencesubcellular organelle

Identifiers

PMID36528065
PMCPMC9860499
OpenAlexW4311475743

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.