Evidence map›Paper›PMID 18780150›Full record

ArticleJournal of muscle research and cell motility2008

Myosin as a potential redox-sensor: an in vitro study.

Chiara Passarelli, Stefania Petrini, Anna Pastore, Valentina Bonetto, Patrizio Sale, Laura M Gaeta, Giulia Tozzi, Enrico Bertini, Monica Canepari, Rosetta Rossi and 1 more

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 42 citations in OpenAlex.

  1. A quantitative redox proteome of the human muscle response to exercise.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Redox-sensitive residue in the actin-binding interface of myosin.Biochemical and biophysical research communications · 2014
    Article
  11. Review
  12. Protein glutathionylation in cardiovascular diseases.International journal of molecular sciences · 2013
    Review
  13. Oxidative stress and sarcomeric proteins.Circulation research · 2013
    Review
  14. Article
  15. Redox signaling and cardiac sarcomeres.The Journal of biological chemistry · 2011
    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

11 authors at 6 institutions in 2 countries.

Chiara PassarelliMolecular Medicine Unit, Children's Hospital and Research Institute Bambino Gesù, Department of Biology, University of Rome Roma Tre, P.za S. Onofrio, 4, Rome, 00165, Italy.
Stefania Petrini
Anna Pastore
Valentina Bonetto
Patrizio Sale
Laura M Gaeta
Giulia Tozzi
Enrico Bertini
Monica Canepari
Rosetta Rossi
Fiorella Piemonte
Bambino Gesù Children's Hospital · ITBoston Children's Hospital · USUniversity of Pavia · ITDulbecco Telethon Institute · ITIRCCS Ospedale San Raffaele · ITRoma Tre University · IT

Funding

Telethon TCR08002
6 · The paper itself

Abstract

A balanced redox status is necessary to optimize force production in contractile apparatus, where free radicals generated by skeletal muscle are involved in some basic physiological processes like excitation-contraction coupling. Protein glutathionylation has a key role in redox regulation of proteins and signal transduction. Here we show that myosin is sensitive to in vitro glutathionylation and MALDI-TOF analysis identified three potential sites of glutathione binding, two of them locating on the myosin head. Glutathionylation of myosin has an important impact on the protein structure, as documented by the lower fluorescence quantum yield of glutathionylated myosin and its increased susceptibility to the proteolytic cleavage. Myosin function is also sensitive to glutathionylation, which modulates its ATPase activity depending on GSSG redox balance. Thus, like the phosphorylation/dephosphorylation cycle, glutathionylation may represent a mechanism by which glutathione modulates sarcomere functions depending on the tissue redox state, and myosin may constitute a muscle redox-sensor.

Indexed as

Adenosine TriphosphatasesAnimalsBlotting, WesternCatalysisDithiothreitolGlutathioneGlutathione DisulfideMyosinsOxidation-ReductionPeptide FragmentsProtein ConformationRatsSpectrometry, FluorescenceSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSulfhydryl CompoundsTrypsinAdenosine TriphosphatasesDithiothreitolGlutathioneGlutathione DisulfideMyosinsPeptide FragmentsSulfhydryl CompoundsTrypsin

Identifiers

PMID18780150
OpenAlexW2087986257

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.