Evidence map›Paper›PMID 37745361›Full record

ArticlebioRxiv : the preprint server for biology2023

Myosin-binding protein C forms C-links and stabilizes OFF states of myosin.

Anthony L Hessel, Nichlas M Engels, Michel Kuehn, Devin Nissen, Rachel L Sadler, Weikang Ma, Thomas C Irving, Wolfgang A Linke, Samantha P Harris

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 3 institutions in 3 countries.

Anthony L HesselInstitute of Physiology II, University of Muenster; Muenster, Germany.
Nichlas M EngelsDepartment of Cellular and Molecular Medicine, University of Arizona; Tucson, AZ, USA.
Michel KuehnInstitute of Physiology II, University of Muenster; Muenster, Germany.
Devin NissenBioCAT, Department of Biology, Illinois Institute of Technology; Chicago, IL, USA.
Rachel L SadlerDepartment of Physiology, University of Arizona, Tucson, AZ, USA.
Weikang MaBioCAT, Department of Biology, Illinois Institute of Technology; Chicago, IL, USA.
Thomas C IrvingBioCAT, Department of Biology, Illinois Institute of Technology; Chicago, IL, USA.
Wolfgang A LinkeInstitute of Physiology II, University of Muenster; Muenster, Germany.
Samantha P HarrisDepartment of Physiology, University of Arizona, Tucson, AZ, USA.
Augenstern · DEIllinois Institute of Technology · USUniversity of Arizona · US

Funding

The Biophysics Collaborative Access Team (User Training and Outreach)P30GM138395 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI THOMAS C IRVING · 2021 to 2026
$16.5M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
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
Mechanisms of Thin Filament Regulation by Myosin Binding Protein-CR01HL140925 · NHLBI · UNIVERSITY OF ARIZONA · PI GALKIN, VITOLD, HARRIS, SAMANTHA P · 2019 to 2022
$2.3M
Cut and paste of myosin binding protein-C in skeletal musclesR21AR081935 · NIAMS · UNIVERSITY OF ARIZONA · PI HARRIS, SAMANTHA P · 2023 to 2024
$366k
NHLBI NIH HHS R01 HL080367NHLBI NIH HHS R01 HL140925NIAMS NIH HHS R21 AR081935NIGMS NIH HHS P30 GM138395NIGMS NIH HHS P41 GM103622
6 · The paper itself

Abstract

Contraction force in muscle is produced by the interaction of myosin motors in the thick filaments and actin in the thin filaments and is fine-tuned by other proteins such as myosin-binding protein C (MyBP-C). One form of control is through the regulation of myosin heads between an ON and OFF state in passive sarcomeres, which leads to their ability or inability to interact with the thin filaments during contraction, respectively. MyBP-C is a flexible and long protein that is tightly bound to the thick filament at its C-terminal end but may be loosely bound at its middle- and N-terminal end (MyBP-C

Identifiers

PMID37745361
PMCPMC10515747
OpenAlexW4386636271

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.