Evidence map›Paper›PMID 26180627›Full record

ArticleSkeletal muscle2015

Developmental myosins: expression patterns and functional significance.

Stefano Schiaffino, Alberto C Rossi, Vika Smerdu, Leslie A Leinwand, Carlo Reggiani

Open access · goldAbstract read
In one paragraph

Article in Skeletal muscle, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 325 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
325citing papers in PubMed, 1 pooled it
11.9field-weighted citation impact, top 1% 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

325 citing papers in PubMed, 1 synthesis or guideline pooled it, 513 citations in OpenAlex.

  1. Pooled it
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  4. Relaxin-2: Shaping the Proteomic Landscape of Skeletal Muscle Physiology, Glucose Trafficking, and Mitochondrial Function in Rat.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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265 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 4 institutions in 3 countries.

Stefano SchiaffinoVenetian Institute of Molecular Medicine (VIMM), Via G. Orus 2, 35129 Padova, Italy.
Alberto C RossiDepartment of Molecular, Cellular and Developmental Biology and BioFrontiers Institute, University of Colorado, Boulder, CO USA.
Vika SmerduInstitute of Anatomy, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.
Leslie A LeinwandDepartment of Molecular, Cellular and Developmental Biology and BioFrontiers Institute, University of Colorado, Boulder, CO USA.
Carlo ReggianiDepartment of Biomedical Sciences, University of Padova, Padova, Italy ; CNR Institute of Neuroscience, Padova, Italy.
University of Colorado Boulder · USUniversity of Ljubljana · SIUniversity of Padua · ITVeneto Institute of Molecular Medicine · IT

Funding

MYOSIN GENE DIVERSITY AND FUNCTIONR01GM029090 · NIGMS · YESHIVA UNIVERSITY · PI Leslie Anne Leinwand · 1985 to 2026
$12.3M
NIGMS NIH HHS R01 GM029090
6 · The paper itself

Abstract

Developing skeletal muscles express unique myosin isoforms, including embryonic and neonatal myosin heavy chains, coded by the myosin heavy chain 3 (MYH3) and MYH8 genes, respectively, and myosin light chain 1 embryonic/atrial, encoded by the myosin light chain 4 (MYL4) gene. These myosin isoforms are transiently expressed during embryonic and fetal development and disappear shortly after birth when adult fast and slow myosins become prevalent. However, developmental myosins persist throughout adult stages in specialized muscles, such as the extraocular and jaw-closing muscles, and in the intrafusal fibers of the muscle spindles. These myosins are re-expressed during muscle regeneration and provide a specific marker of regenerating fibers in the pathologic skeletal muscle. Mutations in MYH3 or MYH8 are responsible for distal arthrogryposis syndromes, characterized by congenital joint contractures and orofacial dysmorphisms, supporting the importance of muscle contractile activity and body movements in joint development and in shaping the form of the face during fetal development. The biochemical and biophysical properties of developmental myosins have only partially been defined, and their functional significance is not yet clear. One possibility is that these myosins are specialized in contracting against low loads, and thus, they may be adapted to the prenatal environment, when fetal muscles contract against a very low load compared to postnatal muscles.

Indexed as

Distal arthrogryposisEmbryonic myosinMuscle developmentMuscle regenerationMyosin heavy chainNeonatal myosin

Identifiers

PMID26180627
PMCPMC4502549
OpenAlexW1573544812

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.