Evidence map›Paper›PMID 30768849›Full record

ArticleThe FEBS journal2019

Congenital myopathy-related mutations in tropomyosin disrupt regulatory function through altered actin affinity and tropomodulin binding.

Joanna Moraczewska, Katarzyna Robaszkiewicz, Małgorzata Śliwinska, Marta Czajkowska, Thu Ly, Alla Kostyukova, Han Wen, Wenjun Zheng

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2019. 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
1.8field-weighted citation impact, top 14% 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, 21 citations in OpenAlex.

  1. Alterations of actin in aging.Journal of cell science · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Troponin and a Myopathy-Linked Mutation inInternational journal of molecular sciences · 2023
    Article
  8. A Novel Variant inInternational journal of molecular sciences · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mutations Q93H and E97K inInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. 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

8 authors at 3 institutions in 2 countries.

Joanna MoraczewskaDepartment of Biochemistry and Cell Biology, Faculty of Natural Sciences, Kazimierz Wielki University, Bydgoszcz, Poland.
Katarzyna RobaszkiewiczDepartment of Biochemistry and Cell Biology, Faculty of Natural Sciences, Kazimierz Wielki University, Bydgoszcz, Poland.
Małgorzata ŚliwinskaDepartment of Biochemistry and Cell Biology, Faculty of Natural Sciences, Kazimierz Wielki University, Bydgoszcz, Poland.
Marta CzajkowskaDepartment of Biochemistry and Cell Biology, Faculty of Natural Sciences, Kazimierz Wielki University, Bydgoszcz, Poland.
Thu LyVoiland School of Chemical Engineering and Bioengineering, University of Washington, Pullman, WA, USA.
Alla KostyukovaVoiland School of Chemical Engineering and Bioengineering, University of Washington, Pullman, WA, USA.
Han WenDepartment of Physics, University at Buffalo, SUNY, NY, USA.
Wenjun ZhengDepartment of Physics, University at Buffalo, SUNY, NY, USA.
Kazimierz Wielki University in Bydgoszcz · PLUniversity at Buffalo, State University of New York · USWashington State University · US

Funding

Deciphering the role of Lmod2 in thin filament length regulation and dilated cardiomyopathyR01HL123078 · NHLBI · UNIVERSITY OF ARIZONA · PI Carol C Gregorio, Shashank Shekhar · 2015 to 2026
$5.6M
REGULATION OF THE ACTIN FILAMENT POINTED END DYNAMICS IN HEALTH AND DISEASER01GM120137 · NIGMS · WASHINGTON STATE UNIVERSITY · PI GALKIN, VITOLD, GREGORIO, CAROL C · 2017 to 2024
$4.0M
NHLBI NIH HHS R01 HL123078NIGMS NIH HHS R01 GM120137
6 · The paper itself

Abstract

Tropomyosin (Tpm) binds along actin filaments and regulates myosin binding to control muscle contraction. Tropomodulin binds to the pointed end of a filament and regulates actin dynamics, which maintains the length of a thin filament. To define the structural determinants of these Tpm functions, we examined the effects of two congenital myopathy mutations, A4V and R91C, in the Tpm gene, TPM3, which encodes the Tpm3.12 isoform, specific for slow-twitch muscle fibers. Mutation A4V is located in the tropomodulin-binding, N-terminal region of Tpm3.12. R91C is located in the actin-binding period 3 and directly interacts with actin. The A4V and R91C mutations resulted in a 2.5-fold reduced affinity of Tpm3.12 homodimers for F-actin in the absence and presence of troponin, and a two-fold decrease in actomyosin ATPase activation in the presence of Ca

Indexed as

Point MutationActin CytoskeletonActinsAdenosine TriphosphatasesCalciumHumansMolecular Dynamics SimulationMuscular DiseasesPolymerizationTropomodulinTropomyosinActinsAdenosine TriphosphatasesCalciumTMOD1 protein, humanTPM3 protein, humanTropomodulinTropomyosincongenital myopathyisoformslow-twitch musclethin filamenttropomodulintropomyosin

Identifiers

PMID30768849
PMCPMC7202179
OpenAlexW2914896391

What OpenQuestion holds

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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.