ArticleDysphagia2010
Myosin heavy-chain composition of the human hyoglossus muscle.
Article in Dysphagia, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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.
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Who cites it
7 citing papers in PubMed.
- Lactate Activates AMPK Remodeling of the Cellular Metabolic Profile and Promotes the Proliferation and Differentiation of C2C12 Myoblasts.International journal of molecular sciences · 2022Article
- Absence of morphological and molecular correlates of sarcopenia in the macaque tongue muscle styloglossus.Experimental gerontology · 2016Article
- Absence of developmental and unconventional myosin heavy chain in human suprahyoid muscles.Muscle & nerve · 2014Article
- A new de novo missense mutation in MYH2 expands clinical and genetic findings in hereditary myosin myopathies.Neuromuscular disorders : NMD · 2013Article
- Myosin heavy chain composition of the human genioglossus muscle.Journal of speech, language, and hearing research : JSLHR · 2012Article
- Human tongue neuroanatomy: Nerve supply and motor endplates.Clinical anatomy (New York, N.Y.) · 2010Article
- Sarcomeric myosin expression in the tongue body of humans, macaques and rats.Cells, tissues, organs · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The human tongue muscle hyoglossus (HG) is active in oromotor behaviors encompassing a wide range of tongue movement speeds. Here we test the hypothesis that the human HG is composed of "uncommon" myosin heavy-chain (MHC) isoforms MHCembryonic, MHCneonatal, and MHCslow tonic as has been reported for other head and neck muscles active during kinematically diverse behaviors. Following reaction of human HG with antibodies specific for MHCI, MHCIIA, MHCII, MHCembryonic, MHCextraocular, MHCneonatal, and MHCslow tonic, only antibodies to MHCI, MHCIIA, and MHCII label more than occasional muscle fibers. These antibodies describe five phenotypes with prevalence MHCIIA > MHCI > MHCI-IIX > MHCI-IIA > MHCIIX. In MHC composition, the human HG is thus similar to human appendicular muscles and many human head and neck muscles but different from human masseter and extraocular muscles which contain five or more MHC isoforms.
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Registered trials
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