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Rebecca C. Burgess

Researcher at Stevenson University

Publications -  18
Citations -  2107

Rebecca C. Burgess is an academic researcher from Stevenson University. The author has contributed to research in topics: DNA repair & Homologous recombination. The author has an hindex of 14, co-authored 16 publications receiving 1980 citations. Previous affiliations of Rebecca C. Burgess include Mayo Clinic & Columbia University Medical Center.

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Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins

TL;DR: The cellular response to DSBs and DNA replication stress is likely directed by the Mre11 complex detecting and processing DNA ends in conjunction with Sae2 and by RP-A recognizing single-stranded DNA and recruiting additional checkpoint and repair proteins.
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Megakaryoblastic Leukemia 1, a Potent Transcriptional Coactivator for Serum Response Factor (SRF), Is Required for Serum Induction of SRF Target Genes

TL;DR: The RBM15-MKL1 fusion protein formed by the t(1;22) translocation of acute megakaryoblastic leukemia had a markedly increased ability to activate SRE reporter genes, suggesting that its activation of SRF target genes may contribute to leukemogenesis.
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Activation of DNA Damage Response Signaling by Condensed Chromatin

TL;DR: It is found that, in response to DNA damage chromatin regions transiently expand before undergoing extensive compaction, and it is demonstrated that interference with chromatin condensation results in failure to fully activate DDR.
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The Slx5-Slx8 Complex Affects Sumoylation of DNA Repair Proteins and Negatively Regulates Recombination†

TL;DR: It is proposed that, during replication, the Slx5-Slx8 complex helps prevent DNA lesions that are acted upon by recombination, and the complex inhibits Rad51-independent recombination via modulating the sumoylation of DNA repair proteins.
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The Shu complex, which contains Rad51 paralogues, promotes DNA repair through inhibition of the Srs2 anti-recombinase

TL;DR: A novel role for the Shucomplex in DNA recombination is proposed in which the Shu complex shifts the balance of repair toward Rad51 filament stabilization by inhibiting the disassembly reaction of Srs2.