Evidence map›Paper›PMID 39663388›Full record

ArticleNature communications2024

PICNIC accurately predicts condensate-forming proteins regardless of their structural disorder across organisms.

Anna Hadarovich, Hari Raj Singh, Soumyadeep Ghosh, Maxim Scheremetjew, Nadia Rostam, Anthony A Hyman, Agnes Toth-Petroczy

Abstract read
In one paragraph

Article in Nature communications, 2024. 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
–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

30 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. 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
  7. Sketching microprotein portraits.Protein science : a publication of the Protein Society · 2026
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Article
  17. Article
  18. 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

7 authors.

Anna Hadarovich *Max Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.
Hari Raj Singh *Max Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.
Soumyadeep GhoshMax Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.ORCID 0000-0002-4691-3636
Maxim ScheremetjewMax Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.
Nadia RostamMax Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.
Anthony A HymanMax Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.ORCID 0000-0003-0851-704X
Agnes Toth-PetroczyMax Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany. toth-petroczy@mpi-cbg.de.ORCID 0000-0002-0333-604X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecular condensates are membraneless organelles that can concentrate hundreds of different proteins in cells to operate essential biological functions. However, accurate identification of their components remains challenging and biased towards proteins with high structural disorder content with focus on self-phase separating (driver) proteins. Here, we present a machine learning algorithm, PICNIC (Proteins Involved in CoNdensates In Cells) to classify proteins that localize to biomolecular condensates regardless of their role in condensate formation. PICNIC successfully predicts condensate members by learning amino acid patterns in the protein sequence and structure in addition to the intrinsic disorder. Extensive experimental validation of 24 positive predictions in cellulo shows an overall ~82% accuracy regardless of the structural disorder content of the tested proteins. While increasing disorder content is associated with organismal complexity, our analysis of 26 species reveals no correlation between predicted condensate proteome content and disorder content across organisms. Overall, we present a machine learning classifier to interrogate condensate components at whole-proteome levels across the tree of life.

Indexed as

Biomolecular CondensatesMachine LearningAlgorithmsAmino Acid SequenceAnimalsComputational BiologyHumansIntrinsically Disordered ProteinsProteinsProteomeIntrinsically Disordered ProteinsProteinsProteome

Identifiers

PMID39663388
PMCPMC11634905

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.