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Michael J. Pikaart

Researcher at Hope College

Publications -  24
Citations -  1307

Michael J. Pikaart is an academic researcher from Hope College. The author has contributed to research in topics: Binding site & Protein structure. The author has an hindex of 10, co-authored 21 publications receiving 1220 citations. Previous affiliations of Michael J. Pikaart include National Institutes of Health & Laboratory of Molecular Biology.

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Loss of transcriptional activity of a transgene is accompanied by DNA methylation and histone deacetylation and is prevented by insulators

TL;DR: It is shown that the chicken insulator can protect a stably integrated gene, which is otherwise subject to great variability of expression, from chromatin-mediated repression in cell culture, and proposed a model for the insulator's ability to protect against extinction in the transformed cell lines and to function as a chromatin boundary for the chicken beta-globin locus in normal erythroid cells.
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Position-effect protection and enhancer blocking by the chicken β-globin insulator are separable activities

TL;DR: It is shown here that a 250-bp “core” element from within 5′HS4 is sufficient to confer protection against silencing of transgenes caused by CPE, and compared with those of other CTCF-binding enhancer-blocking elements suggests that CPE protection is associated with maintenance of a high level of histone acetylation near the insulator.
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Structural and functional conservation at the boundaries of the chicken β‐globin domain

TL;DR: Both boundaries of the chicken β‐globin domain are capable of playing functionally similar roles and that the same protein is a necessary component of the molecular mechanism through which these boundaries are defined.
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Role of histone acetylation and DNA methylation in the maintenance of the imprinted expression of the H19 and Igf2 genes.

TL;DR: The results indicate that histone acetylation as well as DNA methylation contribute to the somatic maintenance of H19 and Igf2 imprinting and that silencing of the imprinted alleles of these two genes is maintained via distinct mechanisms.
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Perturbation of nucleosome structure by the erythroid transcription factor GATA-1.

TL;DR: DNase I and micrococcal nuclease probes show that GATA-1 binding causes extensive, cooperative breakage of the histone/DNA contacts to generate a complex very similar to that formed by the factor with free DNA, and suggest that formation of this complex may be a step in the generation of a fully hypersensitive site in vivo over regulatory elements containing GATA family binding sites.