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Showing 1–4 of 4 results
Advanced filters: Author: Robert Ekiert Clear advanced filters

  • A difference in the survival of respiratory chain complex III deficient Bcs1lp.S78G mice was observed between two congenic mouse strains. Here the authors show how in one of the strains the combined effects of a spontaneously arising non-pathogenic variant and the disease-causing Bcs1lp.S78G mutation exacerbate CIII deficiency and disease progression.

    • Janne Purhonen
    • Vladislav Grigorjev
    • Jukka Kallijärvi
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • In this study, the authors show that MeCP2 interacts with the NCoR/SMRT co-repressor complex and that a discrete cluster of Rett syndrome–causing mutations in the C-terminal domain of MeCP2 disrupts this interaction, impairing transcriptional repression. Knock-in mice expressing one of these MeCP2 missense mutations exhibit severe motor phenotypes.

    • Matthew J Lyst
    • Robert Ekiert
    • Adrian Bird
    Research
    Nature Neuroscience
    Volume: 16, P: 898-902

  • Rett syndrome is caused by mutations in MeCP2, and this study identifies a site on MeCP2, T308, whose phosphorylation is regulated by neuronal activity: phosphorylation of T308 blocks the interaction of MeCP2 with the NCoR co-repressor complex, suppressing MeCP2's ability to repress transcription, and mice carrying mutations of MeCP2 T308 show Rett-syndrome-related symptoms.

    • Daniel H. Ebert
    • Harrison W. Gabel
    • Michael E. Greenberg
    Research
    Nature
    Volume: 499, P: 341-345

  • Most human gene promoters are embedded within CpG islands that lack DNA methylation and coincide with sites at which histone H3 lysine 4 is trimethylated (H3K4me3 sites). Here, a zinc-finger protein, Cfp1, is found to be associated with non-methylated CpG islands and H3K4me3 sites throughout the genome in the mouse brain. A primary function of non-methylated CpG islands might be to genetically determine the local chromatin modification state by interaction with Cfp1 and perhaps other CpG-binding proteins.

    • John P. Thomson
    • Peter J. Skene
    • Adrian Bird
    Research
    Nature
    Volume: 464, P: 1082-1086