Evidence map›Paper›PMID 36018855›Full record

ArticleJournal of the American Chemical Society2022

Peptidyl Prolyl Isomerase A Modulates the Liquid-Liquid Phase Separation of Proline-Rich IDPs.

Maria Babu, Filippo Favretto, Marija Rankovic, Markus Zweckstetter

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Proline/sidechain C-H/O interactions stabilizePhysical chemistry chemical physics : PCCP · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. ProlineJournal of the American Chemical Society · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Liquid-liquid phase separation in Alzheimer's disease.Journal of molecular medicine (Berlin, Germany) · 2024
    Review
  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 2 institutions in 1 country.

Maria BabuDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold Straße 3a, Göttingen, 37075, Germany.
Filippo FavrettoDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold Straße 3a, Göttingen, 37075, Germany.
Marija RankovicMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen, 37077, Germany.
Markus ZweckstetterDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold Straße 3a, Göttingen, 37075, Germany.ORCID 0000-0002-2536-6581
German Center for Neurodegenerative Diseases · DEMax Planck Institute for Multidisciplinary Sciences

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) and the action of molecular chaperones are tightly connected. An important class of molecular chaperones are peptidyl prolyl isomerases, which enhance the cis/trans-isomerization of proline. However, little is known about the impact of peptidyl prolyl isomerases on the LLPS of IDPs, which often contain many prolines. Here, we demonstrate that the most ubiquitous peptidyl prolyl isomerase, peptidyl prolyl isomerase A (PPIA), concentrates inside liquid-like droplets formed by the Alzheimer's disease-associated protein tau, as well as inside RNA-induced coacervates of a proline-arginine dipeptide repeat protein. We further show that the recruitment of PPIA into the IDP droplets triggers their dissolution and return to a single mixed phase. NMR-based binding and proline isomerization studies provide insights into the mechanism of LLPS modulation. Together, the results establish a regulatory role of proline isomerases on the liquid-liquid phase separation of proline-rich IDPs.

Indexed as

Intrinsically Disordered ProteinsPeptidylprolyl IsomeraseMolecular ChaperonesProlinetau ProteinsIntrinsically Disordered ProteinsMolecular ChaperonesPeptidylprolyl IsomeraseProlinetau Proteins

Identifiers

PMID36018855
PMCPMC9460772
OpenAlexW4293155569

What OpenQuestion holds

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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.