Evidence map›Paper›PMID 24531330›Full record

ArticleBioarchitecture

Getting myosin-V on the right track: tropomyosin sorts transport in yeast.

Luther W Pollard, Matthew Lord

Open access · bronzeAbstract readComment
In one paragraph

Article in Bioarchitecture. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Actin and Actin-Binding Proteins.Cold Spring Harbor perspectives in biology · 2016
    Review
  5. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Luther W PollardDepartment of Molecular Physiology & Biophysics; University of Vermont; Burlington, VT USA.
Matthew LordDepartment of Molecular Physiology & Biophysics; University of Vermont; Burlington, VT USA.
University of Vermont · US

Funding

Specification of actomyosin function in the cellR01GM097193 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI LOWEY, SUSAN · 2012 to 2016
$1.5M
NIGMS NIH HHS GM097193NIGMS NIH HHS R01 GM097193
6 · The paper itself

Abstract

Recent studies have revealed a novel mechanism of myosin regulation in which the actin-binding protein tropomyosin converts atypical type-V myosins into processive cargo transporters. To achieve this, tropomyosin's primary role appears to lie in its ability to influence myosin's enzyme kinetics, prolonging the strong actin-bound ADP/apo state to enable hand-over-hand walking of myosin-V dimers along actin tracks. Activation of myosin-V mediated transport by tropomyosin underscores its function in helping to direct cargos to specific actin tracks and subcellular destinations. This type of regulation supports the broader notion that tropomyosin plays a key role in actomyosin sorting.

Indexed as

Actin CytoskeletonCell Cycle ProteinsMyosinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsCell Cycle ProteinsMyosinsSchizosaccharomyces pombe Proteinsactinactomyosin sortingduty ratiointracellular transportmyosin-Vprocessivitytropomyosin

Identifiers

PMID24531330
PMCPMC4199802
OpenAlexW1554331459

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.