Evidence map›Paper›PMID 20371321›Full record

ArticleBiophysical journal2010

The mechanical properties of Drosophila jump muscle expressing wild-type and embryonic Myosin isoforms.

Catherine C Eldred, Dimitre R Simeonov, Ryan A Koppes, Chaoxing Yang, David T Corr, Douglas M Swank

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

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  15. A new experimental model to study force depression: the Drosophila jump muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2014
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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 1 institution in 1 country.

Catherine C EldredDepartment of Biology and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York.
Dimitre R Simeonov
Ryan A Koppes
Chaoxing Yang
David T Corr
Douglas M Swank
Rensselaer Polytechnic Institute · US

Funding

Myosin structural and kinetic mechanisms that differentiate fast and slow muscle R01AR055611 · NIAMS · RENSSELAER POLYTECHNIC INSTITUTE · PI SWANK, DOUGLAS M · 2007 to 2012
$1.6M
NIAMS NIH HHS AR055611NIAMS NIH HHS R01 AR055611
6 · The paper itself

Abstract

Transgenic Drosophila are highly useful for structure-function studies of muscle proteins. However, our ability to mechanically analyze transgenically expressed mutant proteins in Drosophila muscles has been limited to the skinned indirect flight muscle preparation. We have developed a new muscle preparation using the Drosophila tergal depressor of the trochanter (TDT or jump) muscle that increases our experimental repertoire to include maximum shortening velocity (V(slack)), force-velocity curves and steady-state power generation; experiments not possible using indirect flight muscle fibers. When transgenically expressing its wild-type myosin isoform (Tr-WT) the TDT is equivalent to a very fast vertebrate muscle. TDT has a V(slack) equal to 6.1 +/- 0.3 ML/s at 15 degrees C, a steep tension-pCa curve, isometric tension of 37 +/- 3 mN/mm(2), and maximum power production at 26% of isometric tension. Transgenically expressing an embryonic myosin isoform in the TDT muscle increased isometric tension 1.4-fold, but decreased V(slack) 50% resulting in no significant difference in maximum power production compared to Tr-WT. Drosophila expressing embryonic myosin jumped <50% as far as Tr-WT that, along with comparisons to frog jump muscle studies, suggests fast muscle shortening velocity is relatively more important than high tension generation for Drosophila jumping.

Indexed as

Gene Expression Regulation, DevelopmentalAnimalsAnimals, Genetically ModifiedBiophysicsCalciumDrosophilaMuscle ContractionMuscle ProteinsMusclesMutationMyosinsPromoter Regions, GeneticProtein IsoformsStress, MechanicalCalciumMuscle ProteinsMyosinsProtein Isoforms

Identifiers

PMID20371321
PMCPMC2849092
OpenAlexW1972071436

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.