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Jean-Pierre Quivy

Researcher at Centre national de la recherche scientifique

Publications -  56
Citations -  4735

Jean-Pierre Quivy is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Chromatin & Heterochromatin. The author has an hindex of 27, co-authored 50 publications receiving 4298 citations. Previous affiliations of Jean-Pierre Quivy include Curie Institute & University of Paris.

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Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component.

TL;DR: The results show that both H3-K9 acetylation and methylation can occur on independent sets of H3 molecules in pericentric heterochromatin, and identify an RNA- and histone modification–dependent structure that brings methylated H1 protein–binding tails together in a specific configuration required for the accumulation of HP1 proteins in these domains.
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HIRA Is Critical for a Nucleosome Assembly Pathway Independent of DNA Synthesis

TL;DR: A nucleosome assembly pathway that depends on HIRA is delineated, and this defect was largely corrected by reintroduction of HIRA along with (H3-H4)(2) tetramers.
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A CAF-1–PCNA-Mediated Chromatin Assembly Pathway Triggered by Sensing DNA Damage

TL;DR: It is shown that the presence of single-strand breaks and gaps, formed either directly or during DNA damage processing, can trigger the propagation of nucleosomal arrays, which involves the histone chaperone chromatin assembly factor 1 (CAF-1).
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Histone chaperones: assisting histone traffic and nucleosome dynamics.

TL;DR: The importance of histone chaperones during development is discussed and how misregulation of the histone flow can link to disease is described, to show how they affect dynamics during DNA replication, DNA damage, and transcription, and how they maintain genome integrity.
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Human Asf1 regulates the flow of S phase histones during replicational stress

TL;DR: It is suggested that hAsf1 provides the cells with a buffering system for histone excess generated in response to stalled replication and explains how mammalian cells maintain a critical "active" histone pool available for deposition during recovery from replication stresses.