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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.


Msc, MyoR, ABF-1, Musculin
The protein encoded by this gene is a transcriptional repressor capable of binding an E-box element either as a homodimer or as a heterodimer with E2A in vitro. The encoded protein also forms heterodimers with E2A proteins in vivo. This protein is capable of inhibiting the transactivation capability of E47, an E2A protein, in mammalian cells. This gene is a downstream target of the B-cell receptor signal transduction pathway. [provided by RefSeq, Jul 2008] (from NCBI)
Papers using Msc antibodies
Redox-shift of the pheromone-binding protein in the silkmoth Antheraea polyphemus
Leal Walter S. et al., In Journal of Chemical Ecology, 1994
... Msc I and Bam HI or Xho I (New England Biolabs, Ipswich, MA, USA), and ...
Papers on Msc
Musculin and TCF21 coordinate the maintenance of myogenic regulatory factor expression levels during mouse craniofacial development.
Carvajal et al., London, United Kingdom. In Development, 2012
Data show that correct levels of expression of Myf5 and MyoD during mouse craniofacial development result from activation by musculin and TCF21 through direct binding to specific enhancers.
Abnormal mitoferrin-1 expression in patients with erythropoietic protoporphyria.
Bloomer et al., Birmingham, United States. In Exp Hematol, 2011
Data show that abnormal MFRN1 expression can contribute to erythropoietic protoporphyria phenotype in some patients, probably by causing a reduction in FECH activity.
MicroRNA-378 targets the myogenic repressor MyoR during myoblast differentiation.
Dutta et al., Charlottesville, United States. In J Biol Chem, 2011
a feed-forward loop where MyoD indirectly down-regulates MyoR via miR-378
Competitive binding of musclin to natriuretic peptide receptor 3 with atrial natriuretic peptide.
Shimomura et al., Ōsaka, Japan. In J Endocrinol, 2009
Musclin binds to NPR3 competitively with ANP and may affect ANP concentrations in a local or systemic manner.
Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling.
Shibahara et al., Sendai, Japan. In Febs J, 2009
hypoxia induces the expression of mitoferrin mRNAs through separate mechanisms in erythroid cells
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