Evidence map›Paper›PMID 38336971›Full record

ArticleBulletin of experimental biology and medicine2024

N-Terminal Fragment of Cardiac Myosin Binding Protein-C Increases the Duration of Actin-Myosin Interaction.

S R Nabiev, A M Kochurova, L V Nikitina, E A Beldiia, A M Matyushenko, D S Yampolskaya, S Yu Bershitsky, G V Kopylova, D V Shchepkin

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Article in Bulletin of experimental biology and medicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

S R NabievInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia. salavatik2003@gmail.com.
A M KochurovaInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.
L V NikitinaInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.
E A BeldiiaInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.
A M MatyushenkoA. N. Bakh Institute of Biochemistry, Federal Research Center Fundamentals of Biotechnology, Russian Academy of Sciences, Moscow, Russia.
D S YampolskayaA. N. Bakh Institute of Biochemistry, Federal Research Center Fundamentals of Biotechnology, Russian Academy of Sciences, Moscow, Russia.
S Yu BershitskyInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.
G V KopylovaInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.
D V ShchepkinInstitute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences, Yekaterinburg, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cardiac myosin binding protein-C (cMyBP-C) located in the C-zone of myocyte sarcomere is involved in the regulation of myocardial contraction. Its N-terminal domains C0, C1, C2, and the m-motif between C1 and C2 can bind to the myosin head and actin of the thin filament and affect the characteristics of their interaction. Measurements using an optical trap showed that the C0-C2 fragment of cMyBP-C increases the interaction time of cardiac myosin with the actin filament, while in an in vitro motility assay, it dose-dependently reduces the sliding velocity of actin filaments. Thus, it was found that the N-terminal part of cMyBP-C affects the kinetics of the myosin cross-bridge.

Indexed as

ActinsCarrier ProteinsActin CytoskeletonCardiac MyosinsMyocardiumMyosinsProtein BindingActinsCardiac MyosinsCarrier ProteinsMyosinsactin—myosin interactioncardiac myosincardiac myosin binding protein-Cin vitro motility assayoptical trap

Identifiers

PMID38336971

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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.