Evidence map›Paper›PMID 18234857›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.

Vitold E Galkin, Albina Orlova, Olga Cherepanova, Marie-Christine Lebart, Edward H Egelman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

73 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Excessive CabioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Review
  6. De NovoHuman mutation · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. Structural mechanism for bidirectional actin cross-linking by T-plastin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. LCP1 is a prognostic biomarker correlated with immune infiltrates in gastric cancer.Cancer biomarkers : section A of Disease markers · 2021
    Article
  18. Article
  19. Article
  20. Article

13 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

5 authors at 2 institutions in 2 countries.

Vitold E GalkinDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA.
Albina Orlova
Olga Cherepanova
Marie-Christine Lebart
Edward H Egelman
University of Virginia · USLaboratory of Pathogens and Host Immunity · FR

Funding

Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
NIGMS NIH HHS GM081303NIGMS NIH HHS R01 GM081303
6 · The paper itself

Abstract

Many actin binding proteins have a modular architecture, and calponin-homology (CH) domains are one such structurally conserved module found in numerous proteins that interact with F-actin. The manner in which CH-domains bind F-actin has been controversial. Using cryo-EM and a single-particle approach to helical reconstruction, we have generated 12-A-resolution maps of F-actin alone and F-actin decorated with a fragment of human fimbrin (L-plastin) containing tandem CH-domains. The high resolution allows an unambiguous fit of the crystal structure of fimbrin into the map. The interaction between fimbrin ABD2 (actin binding domain 2) and F-actin is different from any interaction previously observed or proposed for tandem CH-domain proteins, showing that the structural conservation of the CH-domains does not lead to a conserved mode of interaction with F-actin. Both the stapling of adjacent actin protomers and the additional closure of the nucleotide binding cleft in F-actin when the fimbrin fragment binds may explain how fimbrin can stabilize actin filaments. A mechanism is proposed where ABD1 of fimbrin becomes activated for binding a second actin filament after ABD2 is bound to a first filament, and this can explain how mutations of residues buried in the interface between ABD2 and ABD1 can rescue temperature-sensitive defects in actin.

Indexed as

ActinsCryoelectron MicroscopyHumansMembrane GlycoproteinsMicrofilament ProteinsPhosphoproteinsProtein ConformationProtein Structure, TertiaryActinsMembrane GlycoproteinsMicrofilament ProteinsPhosphoproteinsplastin

Identifiers

PMID18234857
PMCPMC2234172
OpenAlexW2022682918

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.