Evidence map›Paper›PMID 37957331›Full record

ReviewNature reviews. Molecular cell biology2024

The molecular basis for cellular function of intrinsically disordered protein regions.

Alex S Holehouse, Birthe B Kragelund

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 409 papers.

0numbers the graph read from it
0cells of the map it votes in
409citing papers in PubMed
90.3field-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

409 citing papers in PubMed, 589 citations in OpenAlex.

  1. Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
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  6. New perspectives on plant water sensing.Science China. Life sciences · 2026
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  9. Conformational reprogramming of c-MycRSC chemical biology · 2026
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  11. CDK8 phosphorylation of DELLA limits Mediator recruitment in gibberellin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  16. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
  17. GSF-DTA: An Innovative Graph-Sequence Fusion Framework for Drug-Target Affinity Prediction.Interdisciplinary sciences, computational life sciences · 2026
    Article
  18. Article
  19. Article
  20. A Spatiotemporal Atlas of the Androgen Receptor Proximal Interactome.bioRxiv : the preprint server for biology · 2026
    Article

349 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

2 authors at 2 institutions in 2 countries.

Alex S HolehouseDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO, USA. alex.holehouse@wustl.edu.ORCID http://orcid.org/0000-0002-4155-5729
Birthe B KragelundREPIN, Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Copenhagen, Denmark. bbk@bio.ku.dk.ORCID http://orcid.org/0000-0002-7454-1761
University of Copenhagen · DKWashington University in St. Louis · US

Funding

Uncovering the regulatory logic of gene expression encoded by disordered regionsDP2CA290639 · NCI · WASHINGTON UNIVERSITY · PI Alex S Holehouse · 2023 to 2026
$2.3M
NCI NIH HHS DP2 CA290639
6 · The paper itself

Abstract

Intrinsically disordered protein regions exist in a collection of dynamic interconverting conformations that lack a stable 3D structure. These regions are structurally heterogeneous, ubiquitous and found across all kingdoms of life. Despite the absence of a defined 3D structure, disordered regions are essential for cellular processes ranging from transcriptional control and cell signalling to subcellular organization. Through their conformational malleability and adaptability, disordered regions extend the repertoire of macromolecular interactions and are readily tunable by their structural and chemical context, making them ideal responders to regulatory cues. Recent work has led to major advances in understanding the link between protein sequence and conformational behaviour in disordered regions, yet the link between sequence and molecular function is less well defined. Here we consider the biochemical and biophysical foundations that underlie how and why disordered regions can engage in productive cellular functions, provide examples of emerging concepts and discuss how protein disorder contributes to intracellular information processing and regulation of cellular function.

Indexed as

Intrinsically Disordered ProteinsAmino Acid SequenceMacromolecular SubstancesProtein ConformationIntrinsically Disordered ProteinsMacromolecular Substances

Identifiers

PMID37957331
PMCPMC11459374
OpenAlexW4388630765

What OpenQuestion 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 OpenQuestion graph.