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Michael Scher

Researcher at University of Medicine and Dentistry of New Jersey

Publications -  8
Citations -  2721

Michael Scher is an academic researcher from University of Medicine and Dentistry of New Jersey. The author has contributed to research in topics: Histone code & Histone H1. The author has an hindex of 7, co-authored 7 publications receiving 2495 citations. Previous affiliations of Michael Scher include New York University & Rutgers University.

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Human SirT1 Interacts with Histone H1 and Promotes Formation of Facultative Heterochromatin

TL;DR: A model for SirT1-mediated heterochromatin formation is proposed that includes deacetylation of histone tails, recruitment and deacetolation of Histone H1, and spreading of hypomethylated H3-K79 with resultant silencing.
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SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis

TL;DR: The mammalian cytoplasmic protein SirT2 is a member of the Sir2 family of NAD+-dependent protein deacetylases involved in caloric restriction-dependent life span extension and has a strong preference for histone H4K16Ac in their de acetylation activity in vitro and in vivo.
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SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress

TL;DR: It is found that SirT3 is transported from the nucleus to the mitochondria upon cellular stress, including DNA damage induced by Etoposide and UV-irradiation, as well as overexpression ofSirT3 itself.
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SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.

TL;DR: A functional link is demonstrated between the heterochromatin-related histone methyltransferase SUV39H1 and the histone deacetylase SIRT1, and these activities independently contribute to elevated levels of SUV39h1 activity resulting in increased levels of the H3K9me3 modification.