Evidence map›Paper›PMID 38705823›Full record

ReviewTrends in genetics : TIG2024

The impact of IDR phosphorylation on the RNA binding profiles of proteins.

Miha Modic, Maksimiljan Adamek, Jernej Ule

Abstract readReview
In one paragraph

Review in Trends in genetics : TIG, 2024. 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
–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

24 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Phosphorylation event changes the RNA binding mode of EZH2 disordered segment.Protein science : a publication of the Protein Society · 2026
    Article
  13. Article
  14. Review
  15. Current Understanding of Protein Aggregation in Neurodegenerative Diseases.International journal of molecular sciences · 2025
    Review
  16. Review
  17. Review
  18. Article
  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

3 authors.

Miha ModicNational Institute of Chemistry, Ljubljana, Slovenia; The Francis Crick Institute, London, UK; UK Dementia Research Institute at King's College London, London, UK. Electronic address: miha.modic@ki.si.
Maksimiljan AdamekNational Institute of Chemistry, Ljubljana, Slovenia; PhD Program 'Biosciences', Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia.
Jernej UleNational Institute of Chemistry, Ljubljana, Slovenia; The Francis Crick Institute, London, UK; UK Dementia Research Institute at King's College London, London, UK. Electronic address: jernej.ule@ki.si.

Funding

Cancer Research UK CC0102Wellcome Trust 218672Wellcome Trust CC0102
6 · The paper itself

Abstract

Due to their capacity to mediate repetitive protein interactions, intrinsically disordered regions (IDRs) are crucial for the formation of various types of protein-RNA complexes. The functions of IDRs are strongly modulated by post-translational modifications (PTMs). Phosphorylation is the most common and well-studied modification of IDRs, which can alter homomeric or heteromeric interactions of proteins and impact their ability to phase separate. Moreover, phosphorylation can influence the RNA-binding properties of proteins, and recent studies demonstrated its selective impact on the global profiles of protein-RNA binding and regulation. These findings highlight the need for further integrative approaches to understand how signalling remodels protein-RNA networks in cells.

Indexed as

Intrinsically Disordered ProteinsProtein BindingProtein Processing, Post-TranslationalRNARNA-Binding ProteinsHumansPhosphorylationIntrinsically Disordered ProteinsRNARNA-Binding Proteinsintrinsically disordered region (IDR)phosphorylationpost-translational modification (PTM)protein–RNA networkribonucleoprotein (RNP) assemblyRNA-binding protein (RBP)RNP condensate

Identifiers

PMID38705823
PMCPMC7616821

What OpenQuestion holds

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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.