Evidence map›Paper›PMID 25313062›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.

Bo Xue, Cedric Leyrat, Jonathan M Grimes, Robert C Robinson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Pareto optimality reveals an atlas of cellular archetypes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Engineered Tandem Thymosin Peptide Promotes Corneal Wound Healing.Investigative ophthalmology & visual science · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Thymosin βCells · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. International journal of molecular sciences · 2022
    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

4 authors at 2 institutions in 2 countries.

Bo XueInstitute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Biopolis, Singapore 138673; bxue@imcb.a-star.edu.sg.
Cedric LeyratDivision of Structural Biology, Henry Wellcome Building for Genomic Medicine, Oxford, OX3 7BN, United Kingdom;
Jonathan M GrimesDivision of Structural Biology, Henry Wellcome Building for Genomic Medicine, Oxford, OX3 7BN, United Kingdom; Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, United Kingdom; and.
Robert C RobinsonInstitute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Biopolis, Singapore 138673; Department of Biochemistry, National University of Singapore, Singapore 117597.
Agency for Science, Technology and Research · SGCentre for Human Genetics · GB

Funding

Wellcome Trust 075491/Z/04Wellcome Trust 090532
6 · The paper itself

Abstract

Thymosin-β4 (Tβ4) and profilin are the two major sequestering proteins that maintain the pool of monomeric actin (G-actin) within cells of higher eukaryotes. Tβ4 prevents G-actin from joining a filament, whereas profilin:actin only supports barbed-end elongation. Here, we report two Tβ4:actin structures. The first structure shows that Tβ4 has two helices that bind at the barbed and pointed faces of G-actin, preventing the incorporation of the bound G-actin into a filament. The second structure displays a more open nucleotide binding cleft on G-actin, which is typical of profilin:actin structures, with a concomitant disruption of the Tβ4 C-terminal helix interaction. These structures, combined with biochemical assays and molecular dynamics simulations, show that the exchange of bound actin between Tβ4 and profilin involves both steric and allosteric components. The sensitivity of profilin to the conformational state of actin indicates a similar allosteric mechanism for the dissociation of profilin during filament elongation.

Indexed as

PolymerizationActin CytoskeletonActinsAllosteric RegulationAmino Acid SequenceAnimalsBinding, CompetitiveCrystallography, X-RayFluorescence PolarizationHumansKineticsMolecular Dynamics SimulationMolecular Sequence DataPrincipal Component AnalysisProfilinsRabbitsActinsProfilinsThymosinThymosin beta(4)crystallographyfluorescencemolecular dynamicsprotein complexthermodynamics

Identifiers

PMID25313062
PMCPMC4217450
OpenAlexW1999305610

What OpenQuestion holds

Textmetadata
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.