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Wei Duan

Researcher at Deakin University

Publications -  279
Citations -  13287

Wei Duan is an academic researcher from Deakin University. The author has contributed to research in topics: Cancer & Aptamer. The author has an hindex of 55, co-authored 259 publications receiving 11292 citations. Previous affiliations of Wei Duan include Beijing Jiaotong University & National University of Singapore.

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Herb-drug interactions: a literature review.

TL;DR: An extensive review of the literature identified reported herb-drug interactions with clinical significance, although the underlying mechanisms for the altered drug effects and/or concentrations by concomitant herbal medicines are yet to be determined.
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Mechanism-based inhibition of cytochrome P450 3A4 by therapeutic drugs.

TL;DR: It appears that the chemical properties of a drug critical to CYP3A4 inactivation include formation of reactive metabolites by CYP isoenzymes, preponderance of CYP inducers and P-glycoprotein (P-gp) substrate, and occurrence of clinically significant pharmacokinetic interactions with coadministered drugs.
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Selection of DNA aptamers against epithelial cell adhesion molecule for cancer cell imaging and circulating tumor cell capture.

TL;DR: DNA aptamers reported here against cancer biomarker EpCAM will facilitate the development of novel targeted cancer therapy, cancer cell imaging, and circulating tumor cell detection.
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Substrates and inhibitors of human multidrug resistance associated proteins and the implications in drug development.

TL;DR: It can be expected that modulation of MRP members may represent a useful approach in the management of anticancer and antimicrobial drug resistance and possibly of inflammatory diseases and other diseases.
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Drug Bioactivation Covalent Binding to Target Proteins and Toxicity Relevance

TL;DR: A number of therapeutic drugs with different structures and mechanisms of action have been reported to undergo metabolic activation by Phase I or Phase II drug-metabolizing enzymes, giving rise to reactive metabolites/intermediates which readily confer covalent binding to various target proteins by nucleophilic substitution and/or Schiff's base mechanism.