S
Susan P. Lees-Miller
Researcher at University of Calgary
Publications - 166
Citations - 18750
Susan P. Lees-Miller is an academic researcher from University of Calgary. The author has contributed to research in topics: DNA repair & DNA damage. The author has an hindex of 78, co-authored 161 publications receiving 17673 citations. Previous affiliations of Susan P. Lees-Miller include Michigan State University & Brookhaven National Laboratory.
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Journal ArticleDOI
DNA-dependent protein kinase catalytic subunit: A relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product
Katharine O. Hartley,David A. Gell,Graeme C. M. Smith,Hong Zhang,Nullin Divecha,Margery A. Connelly,Arie Admon,Susan P. Lees-Miller,Carl W. Anderson,Stephen P. Jackson +9 more
TL;DR: The cloning of the DNA- PKcs cDNA is described and it is shown that DNA-PKcs falls into the phosphatidylinositol (PI) 3-kinase family, which is most similar to PI kinase family members involved in cell cycle control, DNA repair, and DNA damage responses.
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Repair of ionizing radiation-induced DNA double strand breaks by non-homologous end-joining
TL;DR: The present review will discuss the current understanding of the mechanism of NHEJ in mammalian cells and discuss the roles of DNA-PKcs and DNA- PK-mediated phosphorylation in NHEH (non-homologous end-joining).
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GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase
TL;DR: It is reported that SV40 infection induces Sp1 phosphorylation, and it is discovered that Sp1 becomes quantitatively phosphorylated in an in vitro transcription extract.
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Absence of p350 subunit of DNA-activated protein kinase from a radiosensitive human cell line
Susan P. Lees-Miller,Roseline Godbout,Doug W. Chan,Michael Weinfeld,Rufus S. Day,Geraldine M. Barron,Joan Allalunis-Turner +6 more
TL;DR: The radiosensitive rodent mutant cell line xrs-5 is defective in DNA double-strand break repair and lacks the Ku component of the DNA-activated protein kinase, DNA-PK, which suggests that DNA- PK kinase activity is involved in DNAdouble-stranded break repair.
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Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53.
TL;DR: The study suggests that DNA-PK may have a role in regulating cell growth and indicates how phosphorylation of serine 15 in DNA-bound p53 could alter p53 function.