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Jacques Côté

Researcher at Laval University

Publications -  160
Citations -  21037

Jacques Côté is an academic researcher from Laval University. The author has contributed to research in topics: Chromatin & Histone. The author has an hindex of 66, co-authored 149 publications receiving 19330 citations. Previous affiliations of Jacques Côté include Howard Hughes Medical Institute & Pennsylvania State University.

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mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases

TL;DR: A mass spectrometry-based method is developed that generates a KAT protein interaction network from which a unique link between NuA4 and the spindle pole body is identified and may serve as a valuable tool in connecting KATs with their cellular targets.
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Regulation of histone and beta A-globin gene expression during differentiation of chicken erythroid cells.

TL;DR: Use of protein and DNA synthesis inhibitors indicated that the content of H5 mRNA was regulated at the posttranscriptional level by a control mechanism(s) differing from those for the other histones.
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Acetylation of PCNA Sliding Surface by Eco1 Promotes Genome Stability through Homologous Recombination.

TL;DR: It is demonstrated that acetylation of lysine residues at the inner surface of PCNA is induced by DNA lesions, and cohesin acetyltransferase Eco1 targets lysin 20 at the sliding surface of the PCNA ring in vitro and in vivo in response to DNA damage.
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Recognition of Histone H3K14 Acylation by MORF

TL;DR: The crystal structure of the MORF DPF-H3K14butyryl complex offers insight into the selectivity of this reader toward lipophilic acyllysine substrates and support the mechanism by which the acetyltransferase MORF promotes spreading of histone acylation.
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Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome

TL;DR: These results argue that methylated histone reader modules in NuA4 are not responsible for its recruitment to the promoter or coding regions but, rather, are required to orient its acetyltransferase catalytic site to the methylatedhistone 3-bearing nucleosomes in the surrounding chromatin, cooperating to allow proper transition from transcription initiation to elongation.