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David T. Brown

Researcher at University of Mississippi Medical Center

Publications -  42
Citations -  3776

David T. Brown is an academic researcher from University of Mississippi Medical Center. The author has contributed to research in topics: Histone H1 & Chromatin. The author has an hindex of 28, co-authored 42 publications receiving 3576 citations. Previous affiliations of David T. Brown include University of Mississippi.

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Hyperdynamic Plasticity of Chromatin Proteins in Pluripotent Embryonic Stem Cells

TL;DR: It is suggested that hyperdynamic binding of structural chromatin proteins is a functionally important hallmark of pluripotent ES cells that contributes to the maintenance of plasticity in undifferentiated ES cells and to establishing higher-order chromatin structure.
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Dynamic binding of histone H1 to chromatin in living cells

TL;DR: The results support a model in which linker histones bind dynamically to chromatin in a stop-and-go mode, suggesting a higher rate of exchange upon chromatin remodelling.
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Global Nature of Dynamic Protein-Chromatin Interactions In Vivo: Three-Dimensional Genome Scanning and Dynamic Interaction Networks of Chromatin Proteins

TL;DR: It is demonstrated that most chromatin proteins have a high turnover on chromatin with a residence time on the order of seconds, that the major fraction of each protein is bound to chromatin at steady state, and that transient binding is a common property of chromatin-associated proteins.
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Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo.

TL;DR: This work has combined systematic mutagenesis, measurement of in vivo binding by photobleaching microscopy, and structural modeling to determine the binding geometry of the globular domain of the H10 linker histone variant within the nucleosome in unperturbed, native chromatin in vivo.
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Competition between histone H1 and HMGN proteins for chromatin binding sites

TL;DR: The results provide evidence for in vivo competition among chromosomal proteins for binding sites on chromatin and suggest that the local structure of the chromatin fiber is modulated by a dynamic interplay between nucleosomal binding proteins.