Evidence map›Paper›PMID 11956227›Full record

ArticleThe Journal of cell biology2002

The utrophin actin-binding domain binds F-actin in two different modes: implications for the spectrin superfamily of proteins.

Vitold E Galkin, Albina Orlova, Margaret S VanLoock, Inna N Rybakova, James M Ervasti, Edward H Egelman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Dystrophin- and Utrophin-Based Therapeutic Approaches for Treatment of Duchenne Muscular Dystrophy: A Comparative Review.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2024
    Review
  6. International journal of molecular sciences · 2022
    Article
  7. Nuclear Actin Dynamics in Gene Expression, DNA Repair, and Cancer.Results and problems in cell differentiation · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

6 authors at 2 institutions in 1 country.

Vitold E GalkinDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA.
Albina Orlova
Margaret S VanLoock
Inna N Rybakova
James M Ervasti
Edward H Egelman
University of Virginia · USUniversity of Wisconsin–Madison · US

Funding

CYTOSKELETAL INTERACTIONS OF DYSTROPHINR01AR042423 · NIAMS · UNIVERSITY OF WISCONSIN MADISON · PI ERVASTI, JAMES M · 1994 to 2025
$9.3M
STRUCTURAL STUDIES OF ACTIN AND TUBULINR01AR042023 · NIAMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI EGELMAN, EDWARD H. · 1994 to 2006
$2.1M
Structural Studies of the SV40 Large T AntigenF32AI050372 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI VANLOOCK, MARGARET S · 2001 to 2002
$72k
NIAID NIH HHS AI50372NIAID NIH HHS F32 AI050372NIAMS NIH HHS AR42023NIAMS NIH HHS AR42423NIAMS NIH HHS R01 AR042023NIAMS NIH HHS R01 AR042423
6 · The paper itself

Abstract

Utrophin, like its homologue dystrophin, forms a link between the actin cytoskeleton and the extracellular matrix. We have used a new method of image analysis to reconstruct actin filaments decorated with the actin-binding domain of utrophin, which contains two calponin homology domains. We find two different modes of binding, with either one or two calponin-homology (CH) domains bound per actin subunit, and these modes are also distinguishable by their very different effects on F-actin rigidity. Both modes involve an extended conformation of the CH domains, as predicted by a previous crystal structure. The separation of these two modes has been largely dependent upon the use of our new approach to reconstruction of helical filaments. When existing information about tropomyosin, myosin, actin-depolymerizing factor, and nebulin is considered, these results suggest that many actin-binding proteins may have multiple binding sites on F-actin. The cell may use the modular CH domains found in the spectrin superfamily of actin-binding proteins to bind actin in manifold ways, allowing for complexity to arise from the interactions of a relatively few simple modules with actin.

Indexed as

ActinsBinding SitesCrystallography, X-RayCytoskeletal ProteinsCytoskeletonMembrane ProteinsMicroscopy, ElectronModels, BiologicalModels, MolecularProtein BindingProtein Structure, QuaternaryProtein Structure, TertiarySpectrinUtrophinActinsCytoskeletal ProteinsMembrane ProteinsSpectrinUtrophin

Identifiers

PMID11956227
PMCPMC2199260
OpenAlexW2090847463

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.