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Frameshift Mutation of MED25, a Transcription Regulator, and its Mutational Heterogeneity in Colorectal Cancers.
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FOS strongly binds to the same MED25 site as ETV4 activation domain and JUN interacts with the other two MED25 sites.
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Med25, a variable member of the Mediator complex, is a coactivator of ligand-activated ERalpha that interacts with ERalpha through its C-terminal LXXLL motif after BPA exposure, and is functionally involved in BPA-induced transcriptional regulation of CYP2C9 expression and enzyme activity.
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the critical region of chromosome 19 a homozygous variant (c.418C>T, p.Arg140Trp) in Mediator complex subunit 25 predicted as deleterious.
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A model is proposed in which the N-terminal transactivation domain of ERM binds the MED25 VP16 H1 binding pocket in a helical conformation.
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Homozygous MED25 mutation implicated in eye-intellectual disability syndrome.
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MED25 is important for regulating the epigenetic landscape resulting in transcriptional activation of a highly inducible gene, CYP2C9
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Med25 is identified as a new coactivator of ERalpha that is required for ERalpha-mediated regulation of CYP2C9 expression
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Mediator subunit MED25 plays a critical role in this process and identify a MED25 domain that serves as a docking site on Mediator for the ATF6alpha transcription activation domain.
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the identification of MED25 as one of the HNF4alpha binding partners in pancreatic ss-cells leading to insulin secretion which is impaired in MODY patients
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solution NMR structure of protein MED25(391-543), comprising the activator interacting domain of subunit 25 of mediator, is presented with the measurement of polypeptide backbone heteronuclear 15N-{1H} NOEs to identify fast internal motional modes
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The regulatory interaction between Sox9, Wwp2 and Med25 defines the Sox9 transcriptional mechanisms of chondrogenesis in the forming palate.
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Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the beta-barrel, defined by strands B4-B7-B6.
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A hydrophobic furrow, formed by a beta-barrel and two alpha-helices in MED25 VBD, interacts tightly with VP16 TADn
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report the NMR structure of the Mediator subunit Med25 (also called Arc92) activator interaction domain (ACID) and analyze the structural and functional interaction of ACID with the archetypical acidic transcription activator VP16
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MED25 and PTOV1 differentially modulate retinoic acid sensitivity in cancer cells depending on their expression levels.
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These results define a role for Med25 and the Mediator complex in the regulation of xenobiotic metabolism and lipid homeostasis.
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Lana-1-induced serum response element activation was inhibited by the dominant-negative N-terminal domain of the human MED25 mediator subunit, suggesting that this subunit mediates Lana-1-induced serum response element activation.
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cloned a prostate-derived cDNA encoding a novel protein with a predicted molecular weight of 78 kDa (P(78)), and precisely mapped the cDNA sequence to chromosome 19
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biochemical purification and cloning of ARC92; identified as a specific cellular interaction partner of the VP16 activation domain
