Evidence map›Paper›PMID 15647169›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004

Myosin VI: cellular functions and motor properties.

Rhys Roberts, Ida Lister, Stephan Schmitz, Matthew Walker, Claudia Veigel, John Trinick, Folma Buss, John Kendrick-Jones

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Trip6 promotes dendritic morphogenesis through dephosphorylated GRIP1-dependent myosin VI and F-actin organization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  9. Article
  10. Review
  11. Article
  12. Proteomics approach to study the functions of Drosophila myosin VI through identification of multiple cargo-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Fifty years on: where have we reached?Journal of muscle research and cell motility · 2006
    Article
  20. Introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    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

8 authors at 3 institutions in 1 country.

Rhys RobertsMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Ida Lister
Stephan Schmitz
Matthew Walker
Claudia Veigel
John Trinick
Folma Buss
John Kendrick-Jones
MRC Laboratory of Molecular Biology · GBUniversity of Leeds · GBUniversity of Cambridge · GB

Funding

Wellcome Trust 071162
6 · The paper itself

Abstract

Myosin VI has been localized in membrane ruffles at the leading edge of cells, at the trans-Golgi network compartment of the Golgi complex and in clathrin-coated pits or vesicles, indicating that it functions in a wide variety of intracellular processes. Myosin VI moves along actin filaments towards their minus end, which is the opposite direction to all of the other myosins so far studied (to our knowledge), and is therefore thought to have unique properties and functions. To investigate the cellular roles of myosin VI, we identified various myosin VI binding partners and are currently characterizing their interactions within the cell. As an alternative approach, we have expressed and purified full-length myosin VI and studied its in vitro properties. Previous studies assumed that myosin VI was a dimer, but our biochemical, biophysical and electron microscopic studies reveal that myosin VI can exist as a stable monomer. We observed, using an optical tweezers force transducer, that monomeric myosin VI is a non-processive motor which, despite a relatively short lever arm, generates a large working stroke of 18 nm. Whether monomer and/or dimer forms of myosin VI exist in cells and their possible functions will be discussed.

Indexed as

Models, BiologicalActinsAnimalsCalciumCalmodulinCell MovementEndocytosisMolecular Motor ProteinsMuscle ContractionMyosin Heavy ChainsPhosphorylationProtein BindingProtein ConformationProtein Structure, TertiaryActinsCalciumCalmodulinMolecular Motor ProteinsMyosin Heavy Chainsmyosin VI

Identifiers

PMID15647169
PMCPMC1693462
OpenAlexW3023183167

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.