Evidence map›Paper›PMID 37657994›Full record

ReviewTrends in biochemical sciences2023

Intrinsically disordered regions are poised to act as sensors of cellular chemistry.

David Moses, Garrett M Ginell, Alex S Holehouse, Shahar Sukenik

Open access · hybridAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
16.5field-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

66 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Review
  3. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Physics-guided design of intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

6 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

4 authors at 2 institutions in 1 country.

David MosesDepartment of Chemistry and Biochemistry, University of California, Merced, CA, USA.
Garrett M GinellDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA; Center for Biomolecular Condensates (CBC), Washington University in St. Louis, St. Louis, MO, USA.
Alex S HolehouseDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA; Center for Biomolecular Condensates (CBC), Washington University in St. Louis, St. Louis, MO, USA. Electronic address: alex.holehouse@wustl.edu.
Shahar SukenikDepartment of Chemistry and Biochemistry, University of California, Merced, CA, USA; Quantitative Systems Biology Program, University of California, Merced, CA, USA. Electronic address: ssukenik@ucmerced.edu.
University of California, Merced · USWashington University in St. Louis · US

Funding

Uncovering the structural underpinnings of function in disordered transcription factor regionsR35GM137926 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI Shahar Sukenik · 2020 to 2026
$2.5M
NIGMS NIH HHS R35 GM137926
6 · The paper itself

Abstract

Intrinsically disordered proteins and protein regions (IDRs) are abundant in eukaryotic proteomes and play a wide variety of essential roles. Instead of folding into a stable structure, IDRs exist in an ensemble of interconverting conformations whose structure is biased by sequence-dependent interactions. The absence of a stable 3D structure, combined with high solvent accessibility, means that IDR conformational biases are inherently sensitive to changes in their environment. Here, we argue that IDRs are ideally poised to act as sensors and actuators of cellular physicochemistry. We review the physical principles that underlie IDR sensitivity, the molecular mechanisms that translate this sensitivity to function, and recent studies where environmental sensing by IDRs may play a key role in their downstream function.

Indexed as

Intrinsically Disordered ProteinsProtein ConformationProtein DomainsIntrinsically Disordered Proteinsbiosensorscellular environmentintrinsically disordered proteinsintrinsically disordered regionssignaling

Identifiers

PMID37657994
PMCPMC10840941
OpenAlexW4386333311

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.