Evidence map›Paper›PMID 15469415›Full record

ArticleThe Biochemical journal2005

Overexpression of troponin T in Drosophila muscles causes a decrease in the levels of thin-filament proteins.

Raquel Marco-Ferreres, Juan J Arredondo, Benito Fraile, Margarita Cervera

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. A homozygous single-nucleotide variant inJournal of neuromuscular diseases · 2025
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  10. Context-dependent functional substitution of alpha-skeletal actin by gamma-cytoplasmic actin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  11. mef2 activity levels differentially affect gene expression during Drosophila muscle development.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  12. 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

4 authors at 2 institutions in 1 country.

Raquel Marco-FerreresDepartamento de Bioquímica and Instituto Investigaciones Biomédicas, UAM-CSIC, Facultad de Medicina, Universidad Autónoma de Madrid, Arzobispo Morcillo 4, 28029 Madrid, Spain.
Juan J Arredondo
Benito Fraile
Margarita Cervera
Universidad Autónoma de Madrid · ESUniversidad de Alcalá · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Formation of the contractile apparatus in muscle cells requires co-ordinated activation of several genes and the proper assembly of their products. To investigate the role of TnT (troponin T) in the mechanisms that control and co-ordinate thin-filament formation, we generated transgenic Drosophila lines that overexpress TnT in their indirect flight muscles. All flies that overexpress TnT were unable to fly, and the loss of thin filaments themselves was coupled with ultrastructural perturbations of the sarcomere. In contrast, thick filaments remained largely unaffected. Biochemical analysis of these lines revealed that the increase in TnT levels could be detected only during the early stages of adult muscle formation and was followed by a profound decrease in the amount of this protein as well as that of other thin-filament proteins such as tropomyosin, troponin I and actin. The decrease in thin-filament proteins is not only due to degradation but also due to a decrease in their synthesis, since accumulation of their mRNA transcripts was also severely diminished. This decrease in expression levels of the distinct thin-filament components led us to postulate that any change in the amount of TnT transcripts might trigger the down-regulation of other co-regulated thin-filament components. Taken together, these results suggest the existence of a mechanism that tightly co-ordinates the expression of thin-filament genes and controls the correct stoichiometry of these proteins. We propose that the high levels of unassembled protein might act as a sensor in this process.

Indexed as

Actin CytoskeletonAnimalsAnimals, Genetically ModifiedDrosophila melanogasterDrosophila ProteinsFeedback, PhysiologicalFlight, AnimalGene Expression Regulation, DevelopmentalMuscle ProteinsMusclesMuscular DiseasesPupaRecombinant Fusion ProteinsRNA, MessengerSarcomeresTroponin TDrosophila ProteinsMuscle ProteinsRecombinant Fusion ProteinsRNA, MessengerTroponin T

Identifiers

PMID15469415
PMCPMC1134776
OpenAlexW2168314685

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.