Evidence map›Paper›PMID 31519753›Full record

ArticleThe Journal of biological chemistry2019

Human cardiac myosin-binding protein C restricts actin structural dynamics in a cooperative and phosphorylation-sensitive manner.

Thomas A Bunch, Rhye-Samuel Kanassatega, Victoria C Lepak, Brett A Colson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.1field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. In situ FRET-based localization of the N terminus of myosin binding protein-C in heart muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

4 authors at 1 institution in 1 country.

Thomas A BunchDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona 85724.
Rhye-Samuel KanassategaDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona 85724.
Victoria C LepakDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona 85724.
Brett A ColsonDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona 85724 bcolson@email.arizona.edu.ORCID 0000-0002-5721-4320
University of Arizona · US

Funding

Functional consequences of FHC mutations in cardiac MyBPCR01HL114770 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI STELZER, JULIAN · 2013 to 2023
$4.3M
Structural Dynamics of Cardiac Myosin-Binding Protein C RegulationR01HL141564 · NHLBI · UNIVERSITY OF ARIZONA · PI Brett A Colson · 2019 to 2026
$3.8M
Structural Dynamics of Cardiac Myosin Binding Protein-CR00HL122397 · NHLBI · UNIVERSITY OF ARIZONA · PI COLSON, BRETT A · 2015 to 2017
$747k
NHLBI NIH HHS R00 HL122397NHLBI NIH HHS R01 HL114770NHLBI NIH HHS R01 HL141564
6 · The paper itself

Abstract

Cardiac myosin-binding protein C (cMyBP-C) is a thick filament-associated protein that influences actin-myosin interactions. cMyBP-C alters myofilament structure and contractile properties in a protein kinase A (PKA) phosphorylation-dependent manner. To determine the effects of cMyBP-C and its phosphorylation on the microsecond rotational dynamics of actin filaments, we attached a phosphorescent probe to F-actin at Cys-374 and performed transient phosphorescence anisotropy (TPA) experiments. Binding of cMyBP-C N-terminal domains (C0-C2) to labeled F-actin reduced rotational flexibility by 20-25°, indicated by increased final anisotropy of the TPA decay. The effects of C0-C2 on actin TPA were highly cooperative (

Indexed as

Actin CytoskeletonActinsAnimalsCardiac MyosinsCarrier ProteinsCyclic AMP-Dependent Protein KinasesFluorescence PolarizationHumansLuminescent MeasurementsMuscle ContractionMuscle, SkeletalMyofibrilsMyosin Binding Protein CMyosinsPhosphorylationProtein BindingActinsCardiac MyosinsCarrier ProteinsCyclic AMP-Dependent Protein KinasesMyosin Binding Protein CMyosinsactincardiac musclecardiac myosin–binding protein C (cMyBP-C)contractile proteinmotor proteinmyofilamentphosphorylationprotein kinase A (PKA)spectroscopystructural dynamics

Identifiers

PMID31519753
PMCPMC6827302
OpenAlexW2973162316

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.