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Daniel A. Bachovchin

Researcher at Memorial Sloan Kettering Cancer Center

Publications -  68
Citations -  5287

Daniel A. Bachovchin is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Inflammasome & Pyroptosis. The author has an hindex of 26, co-authored 57 publications receiving 3762 citations. Previous affiliations of Daniel A. Bachovchin include Scripps Research Institute & Harvard University.

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Quantitative reactivity profiling predicts functional cysteines in proteomes

TL;DR: It is demonstrated that quantitative reactivity profiling can form the basis for screening and functional assignment of cysteines in computationally designed proteins, where it discriminated catalytically active from inactive cysteine hydrolase designs.
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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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The pharmacological landscape and therapeutic potential of serine hydrolases

TL;DR: The current state of pharmacology for mammalian serine hydrolases is reviewed, including marketed drugs, compounds that are under clinical investigation and selective inhibitors emerging from academic probe development efforts.
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Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening

TL;DR: It is shown here that the vast majority of mammalian metabolic SHs can be labeled in proteomes by a single, active site-directed fluorophosphonate probe, and it is shown that lead carbamate inhibitors can be optimized into pharmacological probes that inactivate individual SHs with high specificity in vivo.
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Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes

TL;DR: This method identifies the bioactive alkaloid emetine as a selective inhibitor of the uncharacterized cancer-associated hydrolase RBBP9 and shows that the detoxification enzyme GSTO1, also implicated in cancer, is inhibited by several electrophilic compounds found in public libraries, some of which display high selectivity for this protein.