Evidence map›Paper›PMID 21257752›Full record

ReviewThe Journal of biological chemistry2011

Signaling and myosin-binding protein C.

Jeanne James, Jeffrey Robbins

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 42 citations in OpenAlex.

  1. Trial
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  5. Review
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  7. Article
  8. Interaction between cardiac myosin-binding protein C and formin Fhod3.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Review
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  11. Review
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  14. Review
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  18. Review
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  20. Loss of actomyosin regulation in distal arthrogryposis myopathy due to mutant myosin binding protein-C slow.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    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 1 institution in 1 country.

Jeanne JamesDepartment of Pediatrics and the Heart Institute, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio 45229, USA.
Jeffrey Robbins
Cincinnati Children's Hospital Medical Center · US

Funding

WNT/^-catenin Signaling and Cardiac Fibrosis P01HL069779 · NHLBI · CINCINNATI CHILDRENS HOSP MED CTR · PI OSINSKA, HANNA · 2002 to 2017
$27.0M
Ventricular and Cardiac Fiber Characterization and Integration CoreP01HL059408 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI ROBBINS, JEFFREY · 1999 to 2014
$26.4M
PKCa Signaling Regulates Contractility and Heart FailureP50HL077101 · NHLBI · UNIVERSITY OF CINCINNATI · PI KRANIAS, EVANGELIA G · 2005 to 2009
$19.1M
Cardiomyocyte Toxicity and Heart Failure in Desmin Related CardiomyopathyR01HL087862 · NHLBI · CINCINNATI CHILDRENS HOSP MED CTR · PI ROBBINS, JEFFREY · 2008 to 2010
$600k
NHLBI NIH HHS P01 HL059408NHLBI NIH HHS P01 HL069779NHLBI NIH HHS P01 HL077101NHLBI NIH HHS P01 HL69779NHLBI NIH HHS P50 HL077101NHLBI NIH HHS R01 HL087862
6 · The paper itself

Abstract

Myosin-binding protein C (MyBP-C) is a thick filament protein consisting of 1274 amino acid residues (149 kDa) that was identified by Starr and Offer over 30 years ago as a contaminant present in a preparation of purified myosin. Since then, numerous studies have defined the muscle-specific isoforms, the structure, and the importance of the proteins in normal striated muscle structure and function. Underlying the critical role the protein plays, it is now apparent that mutations in the cardiac isoform (cMyBP-C) are responsible for a substantial proportion (30-40%) of genotyped cases of familial hypertrophic cardiomyopathy. Although generally accepted that MyBP-C can interact with all three filament systems within the sarcomere (the thick, thin, and titin filaments), the exact nature of these interactions and the functional consequences of modified binding remain obscure. In addition to these structural considerations, cMyBP-C can serve as a point of convergence for signaling processes in the cardiomyocyte via post-translational modifications mediated by kinases that phosphorylate residues in the cardiac-specific isoform sequence. Thus, cMyBP-C is a critical nodal point that has both important structural and signaling roles and whose modifications are known to cause significant human cardiac disease.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAnimalsCardiomyopathy, Hypertrophic, FamilialCarrier ProteinsHumansMutationMyosin Binding Protein CPhosphorylationProtein IsoformsProtein KinasesSarcomeresCarrier ProteinsMyosin Binding Protein CProtein IsoformsProtein Kinases

Identifiers

PMID21257752
PMCPMC3060544
OpenAlexW2051058132

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.