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Peter D. Adams

Researcher at University of Glasgow

Publications -  128
Citations -  20807

Peter D. Adams is an academic researcher from University of Glasgow. The author has contributed to research in topics: Senescence & Chromatin. The author has an hindex of 54, co-authored 115 publications receiving 17101 citations. Previous affiliations of Peter D. Adams include Discovery Institute & Fox Chase Cancer Center.

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Human CABIN1 is a functional member of the human HIRA/UBN1/ASF1a histone H3.3 chaperone complex.

TL;DR: Data demonstrate that CABIN1 is a functional member of the human HUCA complex and so is the likely ortholog of yeast Hir3p, which is involved in heterochromatinization of the genome of senescent human cells.
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Notch Signaling Mediates Secondary Senescence

TL;DR: It is found that secondary oncogene-induced senescence in vitro and in vivo requires Notch, rather than SASP alone, as previously thought, and global transcriptomic differences, a blunted SASP response, and the induction of fibrillar collagens in secondarysenescence point toward a functional diversification between secondary and primary senescences.
Journal Article

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2459 more
- 01 Jan 2016 - 
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HP1 proteins are essential for a dynamic nuclear response that rescues the function of perturbed heterochromatin in primary human cells.

TL;DR: It is shown that primary human cells respond to a variety of small molecules that perturb DNA and histone modifications by recruiting HP1 proteins to sites of altered pericentromeric heterochromatin, which is essential to maintain the HP1-binding kinetochore protein hMis12 at Kinetochores and to suppress catastrophic mitotic defects.
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DNMT inhibitors reverse a specific signature of aberrant promoter DNA methylation and associated gene silencing in AML

TL;DR: A set of genes whose methylation and silencing in AML is reversed by DNA methyltransferase inhibitors are identified, and their reactivation byDNA methyl transferase inhibitors may contribute to therapeutic activity.