Evidence map›Paper›PMID 16399836›Full record

ArticleBiophysical journal2006

An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics.

Douglas M Swank, Joan Braddock, Waylon Brown, Heather Lesage, Sanford I Bernstein, David W Maughan

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  9. To understand muscle you must take it apart.Frontiers in physiology · 2014
    Review
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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

6 authors at 3 institutions in 1 country.

Douglas M SwankDepartment of Biology and Center for Biotechnology, Rensselaer Polytechnic Institute, Troy, New York 12180, USA. swankd@rpi.edu
Joan Braddock
Waylon Brown
Heather Lesage
Sanford I Bernstein
David W Maughan
University of Vermont · USRensselaer Polytechnic Institute · USSan Diego State University · US

Funding

Genetics and Molecular Biology of Striated Muscle MyosinR01GM032443 · NIGMS · SAN DIEGO STATE UNIVERSITY · PI BERNSTEIN, SANFORD I · 1985 to 2016
$6.4M
Myosin structural regions that determine muscle shorten*R03AR051473 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI SWANK, DOUGLAS M · 2004 to 2006
$232k
NIAMS NIH HHS AR0494256NIAMS NIH HHS AR51473NIAMS NIH HHS R03 AR051473NIGMS NIH HHS GM32443NIGMS NIH HHS R01 GM032443
6 · The paper itself

Abstract

We examined the importance of alternative versions of a region near the ATP binding site of Drosophila myosin heavy chain for muscle mechanical properties. Previously, we exchanged two versions of this region (encoded by alternative exon 7s) between the indirect flight muscle myosin isoform (IFI) and an embryonic myosin isoform (EMB) and found, surprisingly, that in vitro solution actin-activated ATPase rates were increased (higher Vmax) by both exon exchanges. Here we examined the effect of increased ATPase rate on indirect flight muscle (IFM) fiber mechanics and Drosophila locomotion. IFM expressing EMB with the exon 7a domain replaced by the IFM specific exon 7d domain (EMB-7d) exhibited 3.2-fold greater maximum oscillatory power (Pmax) and 1.5-fold greater optimal frequency of power generation (fmax) versus fibers expressing EMB. In contrast, IFM expressing IFI with the exon 7d region replaced by the EMB exon 7a region (IFI-7a), showed no change in Pmax, fmax, step response, or isometric muscle properties compared to native IFI fibers. A slight decrement in IFI-7a flight ability was observed, suggesting a negative influence of the increased ATPase rate on Drosophila locomotion, perhaps due to energy supply constraints. Our results show that exon 7 plays a substantial role in establishing fiber speed and flight performance, and that the limiting step that sets ATPase rate in Drosophila myosin has little to no direct influence in setting fmax for fast muscle fiber types.

Indexed as

ActomyosinAdenosine TriphosphatasesAdenosine TriphosphateAlternative SplicingAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBinding SitesBiophysicsCrosses, GeneticDrosophilaElasticityExonsKineticsModels, ChemicalMolecular Sequence DataActomyosinAdenosine TriphosphatasesAdenosine TriphosphateMyosinsProtein IsoformsRecombinant Fusion Proteins

Identifiers

PMID16399836
PMCPMC1403199
OpenAlexW2085155299

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.