Evidence map›Paper›PMID 20217194›Full record

ReviewJournal of muscle research and cell motility2009

Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C.

Justin F Shaffer, Samantha P Harris

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of muscle research and cell motility, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. MyBP-C: one protein to govern them all.Journal of muscle research and cell motility · 2020
    Review
  4. Revealing the mechanism of how cardiac myosin-binding protein C N-terminal fragments sensitize thin filaments for myosin binding.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Review
  6. Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Myosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  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

2 authors at 2 institutions in 1 country.

Justin F ShafferDepartment of Bioengineering, University of Washington, Seattle, WA, USA. jfshaffer@ucdavis.edu
Samantha P Harris
University of California, Davis · USUniversity of Washington · US

Funding

Role of Myosin Binding Protein-C in the Regulation of Myocardial ContractionR01HL080367 · NHLBI · UNIVERSITY OF WASHINGTON · PI Samantha P Harris · 2005 to 2026
$7.5M
NHLBI NIH HHS R01 HL080367
6 · The paper itself

Abstract

Cardiac myosin binding protein-C (cMyBP-C) is an accessory protein found in the A-bands of vertebrate sarcomeres and mutations in the cMyBP-C gene are a leading cause of familial hypertrophic cardiomyopathy. The regulatory functions of cMyBP-C have been attributed to the N-terminus of the protein, which is composed of tandem immunoglobulin (Ig)-like domains (C0, C1, and C2), a region rich in proline and alanine residues (the Pro-Ala rich region) that links C0 and C1, and a unique sequence referred to as the MyBP-C motif, or M-domain, that links C1 and C2. Recombinant proteins that contain various combinations of the N-terminal domains of cMyBP-C can activate actomyosin interactions in the absence of Ca(2+), but the specific sequences required for these effects differ between species; the Pro-Ala region has been implicated in human cMyBP-C whereas the C1 and M-domains appear important in mouse cMyBP-C. To investigate whether species-specific differences in sequence can account for the observed differences in function, we compared sequences of the Pro-Ala rich region in cMyBP-C isoforms from different species. Here we report that the number of proline and alanine residues in the Pro-Ala rich region varies significantly between different species and that the number correlates directly with mammalian body size and inversely with heart rate. Thus, systematic sequence differences in the Pro-Ala rich region of cMyBP-C may contribute to observed functional differences in human versus mouse cMyBP-C isoforms and suggest that the Pro-Ala region may be important in matching contractile speed to cardiac function across species.

Indexed as

Amino Acid MotifsAnimalsCarrier ProteinsDipeptidesHeartHumansMiceMutationMyosin Binding Protein CProtein Structure, TertiaryRecombinant ProteinsSarcomeresSpecies SpecificityalanylprolineCarrier ProteinsDipeptidesMyosin Binding Protein CRecombinant Proteins

Identifiers

PMID20217194
PMCPMC2839467
OpenAlexW2067985969

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.