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Patrizia Filetici

Researcher at Sapienza University of Rome

Publications -  54
Citations -  2048

Patrizia Filetici is an academic researcher from Sapienza University of Rome. The author has contributed to research in topics: Acetylation & Histone acetyltransferase. The author has an hindex of 23, co-authored 52 publications receiving 1870 citations. Previous affiliations of Patrizia Filetici include University of Cagliari & National Research Council.

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Journal ArticleDOI

The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p

TL;DR: The findings suggest that the Gcn5p bromodomain may discriminate between different acetylated lysine residues depending on the context in which they are displayed.
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Small-molecule inhibitors of histone acetyltransferase activity: identification and biological properties.

TL;DR: Starting from a yeast phenotypic screening performed on 21 compounds, the identification of two small molecules able to significantly reduce the S. cerevisiae cell growth, thus miming the effect of GCN5 deletion mutant is described.
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The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4

TL;DR: A glutathione S-transferase pull down assay is used to show that Gcn5p binds the amino-terminal tails of histones H3 and H4, but not H2A and H2B, and suggests a new structural role for the highly evolutionary conserved bromodomain.
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A novel histone acetyltransferase inhibitor modulating Gcn5 network: cyclopentylidene-[4-(4'-chlorophenyl)thiazol-2-yl)hydrazone.

TL;DR: The results demonstrate that CPTH2 is a novel HAT inhibitor modulating Gcn5p network in vitro and in vivo, and demonstrated a specific chemical-genetic interaction betweenCPTH2 and HAT GCN5p, indicating that CP TH2 inhibits the Gcn 5p dependent functional network.
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The Neurospora crassa White Collar-1 dependent blue light response requires acetylation of histone H3 lysine 14 by NGF-1.

TL;DR: In this article, it was shown that residue K14 of histone H3 associated with the light-inducible albino-3 (al-3) promoter becomes transiently acetylated after photoinduction.