Evidence map›Paper›PMID 37778184›Full record

ReviewCurrent opinion in structural biology2023

Protein disorder and autoinhibition: The role of multivalency and effective concentration.

Malissa Fenton, Emily Gregory, Gary Daughdrill

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. SHARK-capture identifies functional motifs in intrinsically disordered protein regions.Protein science : a publication of the Protein Society · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. The Proteomic Analysis of Cancer-Related Alterations in the Human Unfoldome.International journal of molecular sciences · 2024
    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.

Malissa FentonDepartment of Molecular Biosciences, University of South Florida, Tampa, FL 33620, USA.
Emily GregoryDepartment of Molecular Biosciences, University of South Florida, Tampa, FL 33620, USA.
Gary DaughdrillDepartment of Molecular Biosciences, University of South Florida, Tampa, FL 33620, USA. Electronic address: gdaughdrill@usf.edu.

Funding

Mechanisms of p53 activation during stress response (MPI)R01CA141244 · NCI · H. LEE MOFFITT CANCER CTR & RES INST · PI JIANDONG CHEN, Gary W Daughdrill · 2009 to 2026
$5.3M
Regulation of transcriptional activation by protein disorderR01GM115556 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI CHEN, JIANDONG, DAUGHDRILL, GARY W · 2016 to 2023
$2.6M
NCI NIH HHS R01 CA141244NIGMS NIH HHS R01 GM115556
6 · The paper itself

Abstract

Regulation of protein binding through autoinhibition commonly occurs via interactions involving intrinsically disordered regions (IDRs). These intramolecular interactions can directly or allosterically inhibit intermolecular protein or DNA binding, regulate enzymatic activity, and control the assembly of large macromolecular complexes. Autoinhibitory interactions mediated by protein disorder are inherently transient, making their identification and characterization challenging. In this review, we explore the structural and functional diversity of disorder-mediated autoinhibition for a variety of biological mechanisms, with a focus on the role of multivalency and effective concentration. We also discuss the evolution of disordered motifs that participate in autoinhibition using examples where sequence conservation varies from high to low. In some cases, identifiable motifs that are essential for autoinhibition remain intact within a rapidly evolving sequence, over long evolutionary distances. Finally, we examine the potential of AlphaFold2 to predict autoinhibitory intramolecular interactions involving IDRs.

Indexed as

Intrinsically Disordered ProteinsProteinsProtein BindingIntrinsically Disordered ProteinsProteins

Identifiers

PMID37778184
PMCPMC10841074

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.