Evidence map›Paper›PMID 19835881›Full record

ReviewJournal of molecular and cellular cardiology2010

Investigations into tropomyosin function using mouse models.

Ganapathy Jagatheesan, Sudarsan Rajan, David F Wieczorek

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2010. 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
3.5field-weighted citation impact, top 7% 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, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Pre-mRNA mis-splicing of sarcomeric genes in heart failure.Biochimica et biophysica acta. Molecular basis of disease · 2017
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Polymorphism in tropomyosin structure and function.Journal of muscle research and cell motility · 2013
    Review
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Ganapathy JagatheesanDepartment of Molecular Genetics, Biochemistry & Microbiology, University of Cincinnati Medical Center, Cincinnati, OH 45267-0524, USA.
Sudarsan Rajan
David F Wieczorek
University of Cincinnati Medical Center · USUniversity of Cincinnati · US

Funding

TRANSCRIPTIONAL CONTROL OF CARDIAC MYOSINSP01HL022619 · NHLBI · UNIVERSITY OF CINCINNATI · PI SCHWARTZ, ARNOLD · 1985 to 2003
$6.1M
Mechanisms of Tropomyosin Induced HypertrophyR01HL071952 · NHLBI · UNIVERSITY OF CINCINNATI · PI WIECZOREK, DAVID F · 2003 to 2006
$2.0M
The Regulation of Sarcomeric Function by TropomyosinR01HL081680 · NHLBI · UNIVERSITY OF CINCINNATI · PI WIECZOREK, DAVID F · 2007 to 2010
$1.6M
FUNCTIONAL ANALYSIS OF TROPOMYOSIN IN THE HEARTR01HL054912 · NHLBI · UNIVERSITY OF CINCINNATI · PI WIECZOREK, DAVID F · 1996 to 2000
$278k
NHLBI NIH HHS P01 HL022619NHLBI NIH HHS R01 HL054912NHLBI NIH HHS R01 HL071952NHLBI NIH HHS R01 HL081680
6 · The paper itself

Abstract

Tropomyosin plays a key role in controlling calcium regulated sarcomeric contraction through its interactions with actin and the troponin complex. The focus of this review is on striated muscle tropomyosin isoforms and the in vivo approach we have taken to define the functional differences among these isoforms in regulating cardiac physiology. In addition, we address specific regions within tropomyosin that differ among the isoforms to impart differences in the physiological performance of muscle and the sarcomere itself. There is a high degree of amino acid identity among the three striated muscle alpha-, beta-, and gamma-tropomyosin isoforms; this identity ranges from 86% to 91%. We employ transgenic mouse model systems that express the different tropomyosin isoforms or chimeric tropomyosin molecules specifically in the myocardium. Results show that the three isoforms differentially regulate the rates of cardiac contraction and relaxation, along with conferring differences in myofilament calcium sensitivity and sarcomere tension development. We also found the putative troponin T binding regions of tropomyosin (amino acids 175-190 and 258-284) appear to a play significant role in imparting these physiological differences that are observed during cardiac and sarcomeric contraction/relaxation. In addition, we have successfully used chimeric tropomyosin molecules to rescue cardiomyopathic diseased mice by normalizing sarcomeric performance. These studies illustrate not only the importance of tropomyosin structure and function for understanding muscle physiology, but also demonstrate how this information can potentially be used for gene therapy.

Indexed as

AnimalsCalciumMiceProtein IsoformsSarcomeresTropomyosinCalciumProtein IsoformsTropomyosin

Identifiers

PMID19835881
PMCPMC2871382
OpenAlexW2059892055

What OpenQuestion holds

Textmetadata
LicenceTDM
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.