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Dongming Ma

Researcher at Chinese Academy of Sciences

Publications -  14
Citations -  707

Dongming Ma is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Medicine & Artemisia annua. The author has an hindex of 7, co-authored 7 publications receiving 601 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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Salicylic acid activates artemisinin biosynthesis in Artemisia annua L.

TL;DR: Results suggest that salicylic acid induces artemisinin biosynthesis in Artemisia annua L. annua in at least two ways: by increasing the conversion of dihydroartemisinic acid into artemis inin caused by the burst of ROS, and by up-regulating the expression of genes involved in artemisine biosynthesis.
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Cloning and characterization of AabHLH1, a bHLH transcription factor that positively regulates artemisinin biosynthesis in Artemisia annua

TL;DR: Biochemical analysis demonstrated that the AabHLH1 protein was capable of binding to the E-box cis-elements, present in both ADS and CYP71AV1 promoters, and possessed transactivation activity in yeast, suggesting that Aab HLH1 can positively regulate the biosynthesis of artemisinin.
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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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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.