C
Christine Magill
Researcher at Wellcome Trust
Publications - 6
Citations - 893
Christine Magill is an academic researcher from Wellcome Trust. The author has contributed to research in topics: G2-M DNA damage checkpoint & Transcription factor II B. The author has an hindex of 6, co-authored 6 publications receiving 847 citations. Previous affiliations of Christine Magill include University of Cambridge & Wellcome Trust/Cancer Research UK Gurdon Institute.
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DNA helicases Sgs1 and BLM promote DNA double-strand break resection
TL;DR: It is revealed that in the absence of exonuclease Exo1 activity, deletion or mutation of the Saccharomyces cerevisiae RecQ-family helicase, Sgs1, causes pronounced hypersensitivity to DSB-inducing agents, and it is established that this reflects severely compromised DSB resection, deficient DNA damage signaling, and strongly impaired HR-mediated repair.
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Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeast
TL;DR: It is shown that H2A phosphorylation is required for cell‐cycle arrest in response to DNA damage at the G1/S transition in budding yeast and that constitutive Tudor domain‐mediated and damage‐specific BRCT domain–phospho‐H2A‐dependent interactions of Rad9 with chromatin cooperate to establish G1 checkpoint arrest.
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Basal and regulated transcription in Archaea
TL;DR: The mode of action of two regulators has been characterized to determine how these 'bacterial-like' regulators impinge on the 'eucaryal- like' basal machinery.
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ATM-dependent phosphorylation of heterogeneous nuclear ribonucleoprotein K promotes p53 transcriptional activation in response to DNA damage.
TL;DR: The data indicate that ATM-dependent hnRNP K phosphorylation is required for its stabilization and its function as a p53 transcriptional cofactor in response to DNA damage.
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Identification of a Conserved Archaeal RNA Polymerase Subunit Contacted by the Basal Transcription Factor TFB
TL;DR: Using systematic yeast two-hybrid and biochemical analyses, an interaction between the N-terminal domain of TFB and an evolutionarily conserved subunit of the RNA polymerase, RpoK is identified.