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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

MyoD family inhibitor

I-mfa, MDFI, I-mf, inhibitor of MyoD family a
This protein is a transcription factor that negatively regulates other myogenic family proteins. Studies of the mouse homolog, I-mf, show that it interferes with myogenic factor function by masking nuclear localization signals and preventing DNA binding. Knockout mouse studies show defects in the formation of vertebrae and ribs that also involve cartilage formation in these structures. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Hic, CAN, MyoD, POLYMERASE, p63
Papers on I-mfa
I-mfa domain proteins specifically interact with HTLV-1 Tax and repress its transactivating functions.
New
Ikeda et al., Kagoshima, Japan. In Virology, Dec 2015
The I-mfa domain proteins HIC (also known as MDFIC) and I-mfa (also known as MDFI) are candidate tumor suppressor genes that are involved in cellular and viral transcriptional regulation.
p53-Regulated Networks of Protein, mRNA, miRNA, and lncRNA Expression Revealed by Integrated Pulsed Stable Isotope Labeling With Amino Acids in Cell Culture (pSILAC) and Next Generation Sequencing (NGS) Analyses.
New
Hermeking et al., München, Germany. In Mol Cell Proteomics, Oct 2015
We confirmed up-regulation of the novel direct p53 target genes LINC01021, MDFI, ST14 and miR-486 and showed that ectopic LINC01021 expression inhibits proliferation in SW480 cells.
A specific DNA methylation profile correlates with a high risk of disease progression in stage I classical (Alibert-Bazin type) mycosis fungoides.
Colantuoni et al., Benevento, Italy. In Br J Dermatol, 2014
METHODS: We analysed DNA methylation at 12 different loci and long interspersed nucleotide elements-1 (LINE-1), as a surrogate marker of global methylation, on tissue samples from 41 patients with stage I MF followed up for at least 12 years or until disease progression.
Treatment of pruritus in early-stage hypopigmented mycosis fungoides with aprepitant.
Rodríguez Mateos et al., Cadiz, Spain. In Dermatol Ther, 2014
In this paper, we describe an excellent response to aprepitant in a female patient with severe pruritus secondary to hypopigmented stage I MF.
A TRPC1 protein-dependent pathway regulates osteoclast formation and function.
Tsiokas et al., Oklahoma City, United States. In J Biol Chem, 2013
Here, we show that the transient receptor potential canonical 1 (TRPC1) channel and the inhibitor of MyoD family, I-mfa, function antagonistically in the regulation of osteoclastogenesis.
Genes responsible for the characteristics of primary cultured invasive phenotype hepatocellular carcinoma cells.
Chuang et al., Kao-hsiung, Taiwan. In Biomed Pharmacother, 2012
Among these genes, only three up-regulated genes (CNN1, PLAT, SPARC) and one down-regulated tumor suppressor gene (MDFI) had same expressions in invasive cells originated from purchased cell line.
Stool DNA testing for the detection of pancreatic cancer: assessment of methylation marker candidates.
Ahlquist et al., Rochester, United States. In Cancer, 2012
RESULTS: Areas under the receiver operating characteristics curves (AUCs) for tissue BMP3, NDRG4, EYA4, UCHL1, MDFI, Vimentin, CNTNAP2, SFRP2, and TFPI2 were 0.90, 0.79, 0.78, 0.78, 0.77, 0.77, 0.69, 0.67, and 0.66, respectively.
Xenopus Zic3 controls notochord and organizer development through suppression of the Wnt/β-catenin signaling pathway.
Aruga et al., Wako, Japan. In Dev Biol, 2012
Furthermore, Zic3 co-precipitated with Tcf1 (a β-catenin co-factor) and XIC (I-mfa domain containing factor required for dorsoanterior development).
I-mfa domain proteins specifically interact with SERTA domain proteins and repress their transactivating functions.
GeneRIF
Eizuru et al., Kagoshima, Japan. In Biochimie, 2011
I-mfa domain proteins may be involved in their oncogenic functions by negatively regulating their transcriptional activities.
Cell cycle switch to endocycle: the nucleolus lends a hand.
Review
Riley et al., London, United Kingdom. In Cell Cycle, 2008
We recently showed that Hand1 is sequestered in the nucleoli of rodent trophoblast stem (TS) cells by the I-mfa domain-containing protein HICp40 and that this is associated with their proliferation and continuing self-renewal.
Nucleolar release of Hand1 acts as a molecular switch to determine cell fate.
Impact
Riley et al., London, United Kingdom. In Nat Cell Biol, 2007
We identify a novel interaction of Hand1 with a protein that contains an I-mfa (inhibitor of myogenic factor) domain that anchors Hand1 in the nucleolus where it negatively regulates Hand1 activity.
TRPC1: store-operated channel and more.
Review
Beech, Leeds, United Kingdom. In Pflugers Arch, 2005
At another level, TRPC1 is embedded in a protein complex that can include inositol trisphosphate receptor, homer, calmodulin, caveolin-1, FKBP25, I-mfa, MxA, GluR1alpha, bFGFR-1, G(q/11) protein, phospholipase C-beta/gamma, protein kinase C-alpha and RhoA.
Myogenic repressor I-mfa interferes with the function of Zic family proteins.
GeneRIF
Aruga et al., Wako, Japan. In Biochem Biophys Res Commun, 2004
These results suggest that the physical and functional interaction between Zic and I-mfa proteins can play a role in the vertebrate development.
Inhibitor of myogenic family, a novel suppressor of store-operated currents through an interaction with TRPC1.
GeneRIF
Tsiokas et al., Oklahoma City, United States. In J Biol Chem, 2004
I-mfa functions as a molecular switch to suppress the store dependence of TRPC1
Regulatory transcription factors controlling function and differentiation of human trophoblast--a review.
Review
Knöfler et al., Vienna, Austria. In Placenta, 2003
In transgenic mice, homozygous mutations of trophoblast-specific transcription factors such as Hand1, Mash-2, I-mfa or GCM1 revealed their key regulatory roles in induction, maintenance or differentiation of distinct placental trophoblast subpopulations in vivo.
How the sequestration of a protein interferes with its mechanism of action: example of a new family of proteins characterized by a particular cysteine-rich carboxy-terminal domain involved in gene expression regulation.
Review
Mesnard et al., San Francisco, United States. In Curr Protein Pept Sci, 2001
This family presently includes three members: I-mfa (inhibitor of MyoD family), HIC p40 and HIC p32 (human I-mfa domain-containing protein).
I-mf, a novel myogenic repressor, interacts with members of the MyoD family.
Impact
Weintraub et al., Seattle, United States. In Cell, 1996
We have isolated a novel myogenic repressor, I-mf (Inhibitor of MyoD family), which is highly expressed in the sclerotome.
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