Evidence map›Paper›PMID 19383471›Full record

ArticleBiophysical journal2009

Cardiac myosin binding protein-C is essential for thick-filament stability and flexural rigidity.

Lori R Nyland, Bradley M Palmer, Zengyi Chen, David W Maughan, Christine E Seidman, J G Seidman, Laurent Kreplak, Jim O Vigoreaux

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

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  11. Molecular modulation of actomyosin function by cardiac myosin-binding protein C.Pflugers Archiv : European journal of physiology · 2014
    Review
  12. Article
  13. Impaired contractile function due to decreased cardiac myosin binding protein C content in the sarcomere.American journal of physiology. Heart and circulatory physiology · 2013
    Article
  14. Article
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  17. Review
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Lori R NylandDepartment of Biology, University of Vermont, Burlington, Vermont 05405, USA.
Bradley M Palmer
Zengyi Chen
David W Maughan
Christine E Seidman
J G Seidman
Laurent Kreplak
Jim O Vigoreaux
University of Vermont · USDalhousie University · CAHarvard University · USHoward Hughes Medical Institute · US

Funding

Ventricular and Cardiac Fiber Characterization and Integration CoreP01HL059408 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI ROBBINS, JEFFREY · 1999 to 2014
$26.4M
Molecular Signaling in Hypertrophic CardiomyopathyR01HL084553 · NHLBI · HARVARD MEDICAL SCHOOL · PI SEIDMAN, JONATHAN G · 2007 to 2022
$5.9M
NHLBI NIH HHS HL59408NHLBI NIH HHS P01 HL059408NHLBI NIH HHS R01 HL084553
6 · The paper itself

Abstract

Using atomic force microscopy, we examined the contribution of cardiac myosin binding protein-C (cMyBP-C) to thick-filament length and flexural rigidity. Native thick filaments were isolated from the hearts of transgenic mice bearing a truncation mutation of cMyBP-C (t/t) that results in no detectable cMyBP-C and from age-matched wild-type controls (+/+). Atomic force microscopy images of these filaments were evaluated with an automated analysis algorithm that identified filament position and shape. The t/t thick-filament length (1.48 +/- 0.02 microm) was significantly (P < 0.01) shorter than +/+ (1.56 +/- 0.02 microm). This 5%-shorter thick-filament length in the t/t was reflected in 4% significantly shorter sarcomere lengths of relaxed isolated cardiomyocytes of the t/t (1.97 +/- 0.01 microm) compared to +/+ (2.05 +/- 0.01 microm). To determine if cMyBP-C contributes to the mechanical properties of thick filaments, we used statistical polymer chain mechanics to calculate a per-filament-specific persistence length, an index of flexural rigidity directly proportional to Young's modulus. Thick-filament-specific persistence length in the t/t (373 +/- 62 microm) was significantly lower than in +/+ (639 +/- 101 microm). Accordingly, Young's modulus of t/t thick filaments was approximately 60% of +/+. These results provide what we consider a new understanding for the critical role of cMyBP-C in defining normal cardiac output by sustaining force and muscle stiffness.

Indexed as

AlgorithmsAnimalsCarrier ProteinsCytoskeletonElasticityElastic ModulusMiceMice, TransgenicMicroscopy, Atomic ForceMyocytes, CardiacMyosin Binding Protein CProtein StabilitySarcomeresCarrier ProteinsMyosin Binding Protein C

Identifiers

PMID19383471
PMCPMC2718271
OpenAlexW2003087311

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.