D
David G. Skalnik
Researcher at Indiana University – Purdue University Indianapolis
Publications - 62
Citations - 4013
David G. Skalnik is an academic researcher from Indiana University – Purdue University Indianapolis. The author has contributed to research in topics: DNA methylation & Epigenetics. The author has an hindex of 32, co-authored 60 publications receiving 3680 citations. Previous affiliations of David G. Skalnik include Indiana University & Riley Hospital for Children.
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CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex.
Jeong Heon Lee,David G. Skalnik +1 more
TL;DR: The presence of CFP1 in this complex implicates this protein as a critical epigenetic regulator of histone modification in addition to cytosine methylation and reveals one mechanism by which this protein intersects with the epigenetic machinery.
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Histone Deacetylase Activity Is Required for Embryonic Stem Cell Differentiation
TL;DR: Preservation of global histone deacetylation by treatment with trichostatin A prevents ES cell differentiation, and ES cells undergo functionally important global and gene‐specific remodeling of chromatin structure during in vitro differentiation.
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Identification and Characterization of the Human Set1B Histone H3-Lys4 Methyltransferase Complex
TL;DR: Two human protein complexes that differ only in the identity of the catalytic histone methyltransferase are revealed, suggesting that Set1A and Set1B each bind to a unique set of target genes and thus make non-redundant contributions to the epigenetic control of chromatin structure and gene expression.
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Cfp1 integrates both CpG content and gene activity for accurate H3K4me3 deposition in embryonic stem cells
Thomas Clouaire,Shaun Webb,Peter J Skene,Robert S. Illingworth,Alastair R.W. Kerr,Robert Andrews,Jeong Heon Lee,David G. Skalnik,Adrian Bird +8 more
TL;DR: The results demonstrate that Cfp1 is a specificity factor that integrates multiple signals, including promoter CpG content and gene activity, to regulate genome-wide patterns of H3K4me3.
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Cloning of a mammalian transcriptional activator that binds unmethylated CpG motifs and shares a CXXC domain with DNA methyltransferase, human trithorax, and methyl-CpG binding domain protein 1.
TL;DR: Data indicate that hCGBP is a transcriptional activator that recognizes unmethylated CpG dinucleotides, suggesting a role in modulating the expression of genes located within C pG islands.