J
James R. Davie
Researcher at University of Manitoba
Publications - 212
Citations - 18112
James R. Davie is an academic researcher from University of Manitoba. The author has contributed to research in topics: Chromatin & Histone code. The author has an hindex of 63, co-authored 204 publications receiving 17091 citations. Previous affiliations of James R. Davie include University of A Coruña & Duke University.
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Journal ArticleDOI
Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Michael Shogren-Knaak,Haruhiko Ishii,Jian-Min Sun,Michael J. Pazin,James R. Davie,Craig L. Peterson +5 more
TL;DR: H4-K16Ac inhibits the ability of the adenosine triphosphate–utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.
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A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression.
Thorsten Heinzel,Robert M. Lavinsky,Tina-Marie Mullen,Mats Söderström,Carol D. Laherty,Joseph Torchia,Wen-Ming Yang,Gyan Brard,Sally D. Ngo,James R. Davie,Edward Seto,Robert N. Eisenman,David W. Rose,Christopher K. Glass,Michael G. Rosenfeld +14 more
TL;DR: Data predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity.
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Inhibition of Histone Deacetylase Activity by Butyrate
TL;DR: The model is proposed in which inhibition of Sp1/Sp3-associated HDAC activity leads to histone hyperacetylation and transcriptional activation of the p21(Waf1/Cip1) gene, which inhibits cyclin-dependent kinase 2 activity and thereby arrests cell cycling.
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Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression
TL;DR: It is proposed that Mad-Max functions by recruiting the mSin3-HDAC corepressor complex that deacetylates nucleosomal histones, producing alterations in chromatin structure that block transcription.
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Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family
TL;DR: Several human cDNAs encoding a histone deacetylase protein, HDAC3, have been isolated and analysis of the predicted amino acid sequence revealed an open reading frame of 428 amino acids with a predicted molecular mass of 49 kDa.