ReviewInternational review of cell and molecular biology2014
The UNC-45 myosin chaperone: from worms to flies to vertebrates.
Review in International review of cell and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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.
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.
Who cites it
46 citing papers in PubMed, 70 citations in OpenAlex.
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Altered chaperone-nonmuscle myosin II interactions drive pathogenicity of the UNC45A c.710T>C variant in osteo-oto-hepato-enteric syndrome.JCI insight · 2025Article
- Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Newly Described Mutations of theCurrent pediatric reviews · 2025Article
- Review
- Optogenetic induction of mechanical muscle stress identifies myosin regulatory ubiquitin ligase NHL-1 in C. elegans.Nature communications · 2024Article
- UNC-45 assisted myosin folding depends on a conserved FXNature communications · 2024Article
- Review
- Review
- SPR spectroscopic analysis of myosin binding to wild type and mutant UNC45B.microPublication biology · 2024Article
- A ubiquitin fusion reporter to monitor muscle proteostasis inmicroPublication biology · 2023Article
- Article
- UCS Chaperone Folding of the Myosin Head: A Function That Evolved before Animals and Fungi Diverged from a Common Ancestor More than a Billion Years Ago.Biomolecules · 2022Review
- UNC45A deficiency causes microvillus inclusion disease-like phenotype by impairing myosin VB-dependent apical trafficking.The Journal of clinical investigation · 2022Article
- A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- The Drosophila anterior-posterior axis is polarized by asymmetric myosin activation.Current biology : CB · 2022Article
- Case report: Osteo-oto-hepato-enteric syndrome caused by UNC45A deficiency.Frontiers in genetics · 2022Article
- Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity.Protein science : a publication of the Protein Society · 2021Article
- Disruption of Drosophila larval muscle structure and function by UNC45 knockdown.BMC molecular and cell biology · 2021Article
- Article
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 at 1 institution in 1 country.
Funding
Abstract
UNC-45 (uncoordinated mutant number 45) is a UCS (UNC-45, CRO1, She4p) domain protein that is critical for myosin stability and function. It likely aides in folding myosin during cellular differentiation and maintenance, and protects myosin from denaturation during stress. Invertebrates have a single unc-45 gene that is expressed in both muscle and nonmuscle tissues. Vertebrates possess one gene expressed in striated muscle (unc-45b) and another that is more generally expressed (unc-45a). Structurally, UNC-45 is composed of a series of α-helices connected by loops. It has an N-terminal tetratricopeptide repeat domain that binds to Hsp90 and a central domain composed of armadillo repeats. Its C-terminal UCS domain, which is also comprised of helical armadillo repeats, interacts with myosin. In this chapter, we present biochemical, structural, and genetic analyses of UNC-45 in Caenorhabditis elegans, Drosophila melanogaster, and various vertebrates. Further, we provide insights into UNC-45 functions, its potential mechanism of action, and its roles in human disease.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.