Evidence map›Paper›PMID 22124140›Full record

ReviewJournal of cell science2011

Myosin-X: a MyTH-FERM myosin at the tips of filopodia.

Michael L Kerber, Richard E Cheney

Abstract readReview
In one paragraph

Review in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

88 citing papers in PubMed, 157 citations in OpenAlex.

  1. Emerging Roles of Cytoneme-Mediated Signaling in Cancer.International journal of molecular sciences · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Diffusion barriers imposed by tissue topology shape Hedgehog morphogen gradients.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Chiral growth of adherent filopodia.Biophysical journal · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

28 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

2 authors at 1 institution in 1 country.

Michael L KerberDepartment of Cell and Molecular Physiology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7545, USA.
Richard E Cheney
University of North Carolina at Chapel Hill · US

Funding

The Platelet-Leukocyte Switch in Vascular DiseaseP01HL080166 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JACOBSON, KENNETH A · 2006 to 2010
$6.7M
Myosin-X: A Novel Myosin with PH DomainsR01DC003299 · NIDCD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CHENEY, RICHARD E · 2002 to 2017
$4.4M
NHLBI NIH HHS P01 HL080166NHLBI NIH HHS P01-HL080166NIDCD NIH HHS R01 DC003299NIDCD NIH HHS R01-DC03299
6 · The paper itself

Abstract

Myosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia. Although the head domain of Myo10 enables it to function as an actin-based motor, its tail contains binding sites for several molecules with central roles in cell biology, including phosphatidylinositol (3,4,5)-trisphosphate, microtubules and integrins. Myo10 also undergoes fascinating long-range movements within filopodia, which appear to represent a newly recognized system of transport. Myo10 is also unusual in that it is a myosin with important roles in the spindle, a microtubule-based structure. Exciting new studies have begun to reveal the structure and single-molecule properties of this intriguing myosin, as well as its mechanisms of regulation and induction of filopodia. At the cellular and organismal level, growing evidence demonstrates that Myo10 has crucial functions in numerous processes ranging from invadopodia formation to cell migration.

Indexed as

AnimalsCell MovementHumansMyosinsProtein Structure, TertiaryPseudopodiaMyosins

Identifiers

PMID22124140
PMCPMC3225264
OpenAlexW2141313486

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.