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Dongfang Yang

Researcher at University of Rhode Island

Publications -  33
Citations -  1770

Dongfang Yang is an academic researcher from University of Rhode Island. The author has contributed to research in topics: Pregnane X receptor & Carboxylesterase. The author has an hindex of 23, co-authored 31 publications receiving 1657 citations.

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Anti-Influenza Prodrug Oseltamivir Is Activated by Carboxylesterase Human Carboxylesterase 1, and the Activation Is Inhibited by Antiplatelet Agent Clopidogrel

TL;DR: Con concurrent use of both drugs would inhibit the activation of oseltamivir, thus making this antiviral agent therapeutically inactive, which is epidemiologically of significance because people who receive osel Tamsivir and clopidogrel simultaneously may maintain susceptibility to influenza infection or a source of spreading influenza virus if already infected.
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Antiplatelet Agents Aspirin and Clopidogrel Are Hydrolyzed by Distinct Carboxylesterases, and Clopidogrel Is Transesterificated in the Presence of Ethyl Alcohol

TL;DR: The isoform-specific hydrolysis of aspirin and clopidogrel suggests that these two antithrombogenic agents may have pharmacokinetic interactions with different sets of ester drugs, and the altered Hydrolysis by polymorphic mutants provides a molecular explanation to the interindividual variation.
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Human carboxylesterases HCE1 and HCE2: Ontogenic expression, inter-individual variability and differential hydrolysis of oseltamivir, aspirin, deltamethrin and permethrin

TL;DR: A large inter-individual variability was detected in mRNA, protein, protein and hydrolytic activity within the same age group, particularly in the fetal and child groups, and this has important pharmacological and toxicological implications.
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The expression of antiapoptotic protein survivin is transcriptionally upregulated by DEC1 primarily through multiple sp1 binding sites in the proximal promoter

TL;DR: Findings establish that the survivin gene is a transcription target of DEC1, and induction of survivin is at least in part responsible for DEC1 antiapoptosis.