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Cornelius Y. Taabazuing

Researcher at Memorial Sloan Kettering Cancer Center

Publications -  22
Citations -  1454

Cornelius Y. Taabazuing is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Pyroptosis & Inflammasome. The author has an hindex of 13, co-authored 17 publications receiving 850 citations. Previous affiliations of Cornelius Y. Taabazuing include University of Massachusetts Amherst & Howard Hughes Medical Institute.

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Pyroptosis and Apoptosis Pathways Engage in Bidirectional Crosstalk in Monocytes and Macrophages.

TL;DR: Bidirectional crosstalk between apoptosis and pyroptosis in monocytes and macrophages is revealed, further illuminating the complex interplay between cell death pathways in the innate immune system.
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DPP8/DPP9 inhibitor-induced pyroptosis for treatment of acute myeloid leukemia

TL;DR: It is shown that the CARD-containing protein CARD8 mediates DPP8/9 inhibitor-induced pro-caspase-1-dependent pyroptosis in human myeloid cells, and indicates that its activation by small-molecule DPP 8/9 inhibitors represents a new potential therapeutic strategy for AML.
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N-terminal degradation activates the NLRP1B inflammasome.

TL;DR: This study used genome-wide CRISPR-Cas9 knockout screens to identify genes required for NLRP1B-mediated pyroptosis and discovered that lethal factor induces cell death via the N-end rule proteasomal degradation pathway.
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Inhibition of Dpp8/9 Activates the Nlrp1b Inflammasome.

TL;DR: This work reveals a previously unrecognized mechanism for activating an innate immune pattern recognition receptor and suggests that Dpp8/9 serve as an intracellular checkpoint to restrain Nlrp1b and the innate immune system.
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Mutually Exclusive Binding of Telomerase RNA and DNA by Ku Alters Telomerase Recruitment Model

TL;DR: It is demonstrated that deletions designed to constrict the DNA-binding ring of Ku80 disrupt nonhomologous end-joining (NHEJ), telomeric gene silencing, and telomere length maintenance, suggesting that these functions require Ku's DNA end-binding activity.