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Holly Miller

Researcher at Stony Brook University

Publications -  40
Citations -  2332

Holly Miller is an academic researcher from Stony Brook University. The author has contributed to research in topics: DNA polymerase & DNA polymerase II. The author has an hindex of 24, co-authored 39 publications receiving 2217 citations. Previous affiliations of Holly Miller include State University of New York System & Wake Forest University.

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Connexin-specific cell-to-cell transfer of short interfering RNA by gap junctions.

TL;DR: The novel hypothesis that non‐hybridized and possible hybridized forms of siRNA can move between mammalian cells through connexin‐specific gap junctions is supported.
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Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation

TL;DR: Structural inferences for the stabilization of protein‐sulfenic acids are drawn from the refined 2.16‐Å structure of the streptococcal NADH peroxidase, providing a molecular basis for understanding the proposed redox functions of these novel cofactors in both enzyme catalysis and transcriptional regulation.
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The novel DNA glycosylase, NEIL1, protects mammalian cells from radiation-mediated cell death.

TL;DR: The results of these studies suggest that Neil1 is an essential component of base excision repair in mammalian cells; its presence may contribute to the redundant repair capacity observed in Ogg1-/- and Nth1 -/- mice.
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Mapping the biosphere: exploring species to understand the origin, organization and sustainability of biodiversity

TL;DR: It is concluded that an ambitious goal to describe 10 million species in less than 50 years is attainable based on the strength of 250 years of progress, worldwide collections, existing experts, technological innovation and collaborative teamwork.
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Structure of DNA Polymerase beta with the Mutagenic DNA Lesion 8-oxodeoxyguanine Reveals Structural Insights into its Coding Potential

TL;DR: This work reports the first structure of a polymerase with a promutagenic DNA lesion, 8-oxodG, in the confines of its active site, and provides insights into the mechanisms employed by polymerases to select the complementary dNTP.