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David J. Segal

Researcher at University of California, Davis

Publications -  173
Citations -  13467

David J. Segal is an academic researcher from University of California, Davis. The author has contributed to research in topics: Zinc finger & Gene. The author has an hindex of 55, co-authored 162 publications receiving 11965 citations. Previous affiliations of David J. Segal include University of Melbourne & University of Utah.

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The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer models

TL;DR: It is demonstrated that S63845 potently kills MCL1-dependent cancer cells, including multiple myeloma, leukaemia and lymphoma cells, by activating the BAX/BAK-dependent mitochondrial apoptotic pathway.
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Stimulation of homologous recombination through targeted cleavage by chimeric nucleases.

TL;DR: Chimeric nucleases that are hybrids between a nonspecific DNA cleavage domain and a zinc finger DNA recognition domain were tested for their ability to find and cleave their target sites in living cells, and two chimeric enzymes with different binding specificities could collaborate to stimulate recombination when their individual sites were appropriately placed.
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Toward controlling gene expression at will: Specific regulation of the erbB-2/HER-2 promoter by using polydactyl zinc finger proteins constructed from modular building blocks

TL;DR: It is demonstrated that both gene repression and activation can be achieved by targeting designed proteins to a single site within the transcribed region of a gene, indicating that gene-specific transcriptional regulators of the type described here will find diverse applications in gene therapy, functional genomics, and the generation of transgenic organisms.
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Structure-based redesign of the dimerization interface reduces the toxicity of zinc-finger nucleases.

TL;DR: A structure-based approach to reducing off-target cleavage of zinc-finger nucleases by preventing homodimerization and lowering the dimerization energy is described, which increased the specificity of target site cleavage.