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Zhigao Du

Researcher at Chinese Academy of Sciences

Publications -  9
Citations -  552

Zhigao Du is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Artemisia annua & Artemisinin. The author has an hindex of 8, co-authored 9 publications receiving 496 citations.

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Isolation and Characterization of AaWRKY1, an Artemisia annua Transcription Factor that Regulates the Amorpha-4,11-diene Synthase Gene, a Key Gene of Artemisinin Biosynthesis

TL;DR: Transient expression experiments in agroinfiltrated Nicotiana benthamiana and A. annua leaves showed that AaWRKY1 protein transactivated the ADSpro2 promoter activity by binding to the W-box of the promoter; disruption of theW-box abolished the activation.
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Metabolic engineering of artemisinin biosynthesis in Artemisia annua L.

TL;DR: In the past decade, an Agrobacterium-mediated transformation system of A. annua is established, and a number of genes related to artemisinin biosynthesis into the plant are transferred, and another promising approach to reduce the price of art Artemisinin-based antimalarial drugs is metabolic engineering of the plant to obtain a higher content of artemisine in transgenic plants.
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Foliar application of chitosan activates artemisinin biosynthesis in Artemisia annua L.

TL;DR: It is shown that foliar application of 100 mg l−1 chitosan improved artemisinin biosynthesis in A. annua and induced the expression of ADS and DBR2, which could explain the increase in level of artemisinic metabolites.
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Artemisinin biosynthesis enhancement in transgenic Artemisia annua plants by downregulation of the β-caryophyllene synthase gene.

TL;DR: It is demonstrated that the inhibition pathway in the precursor competition for artemisinin biosynthesis by anti-sense technology is an effective means of increasing the art Artemisinin content of A. annua plants.
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Biochemical characterization and identification of a cinnamyl alcohol dehydrogenase from Artemisia annua

TL;DR: Functional and enzymatic assays showed that the recombinant enzyme was able to reversibly reduce a variety of common CADs substrates, namely geranial, cinnamyl aldehyde, sinapyl aldhyde, coniferyl aldehydes, and a sesquiterpenoid artemisinic aldechemical respectively.