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Philip L. Lorenzi

Researcher at University of Texas MD Anderson Cancer Center

Publications -  128
Citations -  22127

Philip L. Lorenzi is an academic researcher from University of Texas MD Anderson Cancer Center. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 37, co-authored 96 publications receiving 17665 citations. Previous affiliations of Philip L. Lorenzi include University of Michigan & Loyola University Chicago.

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Mechanism of Catalysis by l-Asparaginase.

TL;DR: A detailed description of the reaction catalyzed by E. coli type II L-asparaginase (EcAII) is provided, providing strong evidence that EcAII catalyzes the reaction according to the double-displacement (ping-pong) mechanism, with formation of a covalent intermediate.
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A curated census of autophagy-modulating proteins and small molecules: candidate targets for cancer therapy.

TL;DR: A comprehensive, curated inventory of autophagy modulators is compiled by integrating information from published siRNA screens, multiple pathway analysis algorithms, and extensive, manually curated text-mining of the literature.
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Multiplexing siRNAs to compress RNAi-based screen size in human cells.

TL;DR: This study suggests that the screening of randomly multiplexed siRNAs may provide an important avenue towards the identification of candidate gene targets for downstream functional analyses and may also be useful for the rapid identification of positive controls for use in novel assay systems.
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Catalytic Role of the Substrate Defines Specificity of Therapeutic l-Asparaginase.

TL;DR: Evidence is presented that the aspartate product in the crystal structure of L-ASP exists in an unusual α-COOH protonation state, and a new hypothesis that the substrate's α-carboxyl serves as a proton acceptor and activates one of the catalytic threonines during L-asparaginases' nucleophilic attack on the amide carbon is explained.