Evidence map›Paper›PMID 28640448›Full record

ReviewComprehensive Physiology2017

Overview of the Muscle Cytoskeleton.

Christine A Henderson, Christopher G Gomez, Stefanie M Novak, Lei Mi-Mi, Carol C Gregorio

Abstract readReview
In one paragraph

Review in Comprehensive Physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 186 papers.

0numbers the graph read from it
0cells of the map it votes in
186citing 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

186 citing papers in PubMed, 282 citations in OpenAlex.

  1. Review
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  7. bioRxiv : the preprint server for biology · 2026
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  17. Dynamic expression of the zebrafish (Danio rerio) proteome across early larval development.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2025
    Article
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  19. Article
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126 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Christine A HendersonDepartment of Cellular and Molecular Medicine, The University of Arizona, Tucson, Arizona, USA.
Christopher G GomezDepartment of Cellular and Molecular Medicine, The University of Arizona, Tucson, Arizona, USA.
Stefanie M NovakDepartment of Cellular and Molecular Medicine, The University of Arizona, Tucson, Arizona, USA.
Lei Mi-MiDepartment of Cellular and Molecular Medicine, The University of Arizona, Tucson, Arizona, USA.
Carol C GregorioDepartment of Cellular and Molecular Medicine, The University of Arizona, Tucson, Arizona, USA.
University of Arizona · US

Funding

Deciphering the role of Lmod2 in thin filament length regulation and dilated cardiomyopathyR01HL123078 · NHLBI · UNIVERSITY OF ARIZONA · PI Carol C Gregorio, Shashank Shekhar · 2015 to 2026
$5.6M
Deciphering the role of the RNA-binding protein, FXR1, in cardiac muscle assemblyR01HL108625 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2012 to 2015
$1.9M
Determining the role of Fragile X proteins in the heartF31HL117520 · NHLBI · UNIVERSITY OF ARIZONA · PI NOVAK, STEFANIE · 2013 to 2016
$134k
NHLBI NIH HHS F31 HL117520NHLBI NIH HHS R01 HL108625NHLBI NIH HHS R01 HL123078
6 · The paper itself

Abstract

Cardiac and skeletal striated muscles are intricately designed machines responsible for muscle contraction. Coordination of the basic contractile unit, the sarcomere, and the complex cytoskeletal networks are critical for contractile activity. The sarcomere is comprised of precisely organized individual filament systems that include thin (actin), thick (myosin), titin, and nebulin. Connecting the sarcomere to other organelles (e.g., mitochondria and nucleus) and serving as the scaffold to maintain cellular integrity are the intermediate filaments. The costamere, on the other hand, tethers the sarcomere to the cell membrane. Unique structures like the intercalated disc in cardiac muscle and the myotendinous junction in skeletal muscle help synchronize and transmit force. Intense investigation has been done on many of the proteins that make up these cytoskeletal assemblies. Yet the details of their function and how they interconnect have just started to be elucidated. A vast number of human myopathies are contributed to mutations in muscle proteins; thus understanding their basic function provides a mechanistic understanding of muscle disorders. In this review, we highlight the components of striated muscle with respect to their interactions, signaling pathways, functions, and connections to disease. © 2017 American Physiological Society. Compr Physiol 7:891-944, 2017.

Indexed as

ActinsAnimalsCytoskeletonHumansMuscle ContractionMyosinsSarcomeresActinsMyosins

Identifiers

PMID28640448
PMCPMC5890934
OpenAlexW2626424052

What OpenQuestion holds

Textmetadata
LicenceTDM
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.