Evidence map›Paper›PMID 29306779›Full record

ReviewCurrent opinion in structural biology2018

IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.

Ho Yee Joyce Fung, Melissa Birol, Elizabeth Rhoades

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing 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

78 citing papers in PubMed.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Non-Fickian diffusion within assemblies of the intrinsically disordered protein β-casein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Structure of the Drp1 Lattice on Membrane.Journal of molecular biology · 2025
    Article
  17. Article
  18. Review
  19. SHARK-capture identifies functional motifs in intrinsically disordered protein regions.Protein science : a publication of the Protein Society · 2025
    Article
  20. Article

18 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

3 authors.

Ho Yee Joyce FungDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, United States.
Melissa BirolDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, United States.
Elizabeth RhoadesDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, United States; Biochemistry & Molecular Biophysics Graduate Group, University of Pennsylvania, Philadelphia, PA 19104, United States. Electronic address: elizabeth.rhoades@sas.upenn.edu.

Funding

Molecular mechanisms and cellular implications of tau dysfunctionRF1AG053951 · NIA · UNIVERSITY OF PENNSYLVANIA · PI ODDE, DAVID J., RHOADES, ELIZABETH · 2016 to 2018
$2.9M
Self-association and membrane-binding of alpha-synucleinR01NS079955 · NINDS · YALE UNIVERSITY · PI RHOADES, ELIZABETH · 2013 to 2017
$1.7M
NIA NIH HHS RF1 AG053951NINDS NIH HHS R01 NS079955
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) have critical roles in a diverse array of cellular functions. Of relevance here is that they are components of macromolecular complexes, where their conformational flexibility helps mediate interactions with binding partners. IDPs often interact with their binding partners through short sequence motifs, commonly repeated within the disordered regions. As such, multivalent interactions are common for IDPs and their binding partners within macromolecular complexes. Here we discuss the importance of IDP multivalency in three very different macromolecular assemblies: biomolecular condensates, the nuclear pore, and the cytoskeleton.

Indexed as

AnimalsBinding SitesCytoskeletonHumansIntrinsically Disordered ProteinsMacromolecular SubstancesNuclear PoreProtein BindingProtein ConformationIntrinsically Disordered ProteinsMacromolecular Substances

Identifiers

PMID29306779
PMCPMC5915967

What OpenQuestion holds

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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.