Evidence map›Paper›PMID 15711885›Full record

ArticleJournal of muscle research and cell motility2004

Simultaneous measurement of rotations of myosin, actin and ADP in a contracting skeletal muscle fiber.

A A Shepard, D Dumka, I Akopova, J Talent, J Borejdo

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
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

5 authors at 2 institutions in 1 country.

A A ShepardDepartment of Molecular Biology and Immunology, University of North Texas, 3500 Camp Bowie Building, Fort Worth, TX 76107, USA.
D Dumka
I Akopova
J Talent
J Borejdo
University of North Texas Health Science Center · USUniversity of North Texas · US

Funding

Rotation of Single Cross-Bridge in Skeletal Muscle FiberR01AR048622 · NIAMS · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI BOREJDO, JULIAN · 2003 to 2007
$870k
NCI NIH HHS R21CA9732NCRR NIH HHS RR-08119NIAMS NIH HHS R01AR048622
6 · The paper itself

Abstract

The rotation of myosin heads and actin were measured simultaneously with an indicator of the enzymatic activity of myosin. To minimize complications due to averaging of signals from many molecules, the signal was measured in a small population residing in a femtoliter volume of a muscle fiber. The onset of rotation was synchronized by a sudden release of caged ATP. The orientation of cross-bridges was measured by anisotropy of recombinant fluorescent regulatory light chains exchanged with native regulatory light chains. The orientation of actin was measured by anisotropy of phalloidin added to actin filaments. The enzymatic activity of myosin was measured by dissociation of fluorescent ADP from the active site. The onset of all three events occurred at the same time. This suggests that in contracting muscle, actin does not move independently of myosin and that ATP hydrolysis is strongly coupled to the rotation of cross-bridges.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsMuscle ContractionMuscle Fibers, SkeletalMuscle, SkeletalMyosinsRabbitsRotationTime FactorsActinsAdenosine DiphosphateAdenosine TriphosphateMyosins

Identifiers

PMID15711885
OpenAlexW2113169351

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.