Evidence map›Paper›PMID 23200340›Full record

ReviewTrends in cell biology2013

Regulation and control of myosin-I by the motor and light chain-binding domains.

Michael J Greenberg, E Michael Ostap

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.0field-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

45 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Coupling between the lever arm and active site via an N-terminal extension tunes force sensitivity in the myosin-1 family.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Switch-2 determines MgFrontiers in physiology · 2024
    Article
  13. Article
  14. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
  16. Article
  17. Article
  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

2 authors at 1 institution in 1 country.

Michael J GreenbergThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
E Michael Ostap
University of Pennsylvania · US

Funding

Role of Myosin-l in Membrane Dynamics and TransportP01GM087253 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2009 to 2018
$15.3M
Training in Muscle Biology and Muscle DiseaseT32AR053461 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2006 to 2025
$4.9M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
Regulation of Myosin Ic MechanochemistryF32GM097889 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GREENBERG, MICHAEL J · 2011 to 2012
$101k
NIAMS NIH HHS T32 AR053461NIGMS NIH HHS F32 GM097889NIGMS NIH HHS P01 GM087253NIGMS NIH HHS R01 GM057247
6 · The paper itself

Abstract

Members of the myosin-I family of molecular motors are expressed in many eukaryotes, where they are involved in a multitude of critical processes. Humans express eight distinct members of the myosin-I family, making it the second largest family of myosins expressed in humans. Despite the high degree of sequence conservation in the motor and light chain-binding domains (LCBDs) of these myosins, recent studies have revealed surprising diversity of function and regulation arising from isoform-specific differences in these domains. Here we review the regulation of myosin-I function and localization by the motor and LCBDs.

Indexed as

Mechanotransduction, CellularActinsAdenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesBiomechanical PhenomenaCell MembraneHumansMyosin Type IProtein BindingProtein Interaction MappingProtein IsoformsProtein Structure, TertiaryProtein TransportActinsAdenosine TriphosphatasesAdenosine TriphosphateMYO1C protein, humanMyosin Type IProtein Isoforms

Identifiers

PMID23200340
PMCPMC3558615
OpenAlexW2028237914

What OpenQuestion holds

Textmetadata
LicenceTDM
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.