Decoding the Root Lignification Mechanism of Angelica sinensis through Genome-wide Methylation Analysis.

Angelica sinensis is a traditional Chinese herbal medicine with significant economic and medicinal value. However, early bolting and flowering can occur during the second year of the vegetative growth period, rendering the roots unviable for medicinal use and resulting in substantial economic losses. Consequently, the growing interest in studying the molecular mechanisms underlying early bolting or increased root lignification in A.

Elucidation of AsANS controlling pigment biosynthesis in Angelica sinensis through hormonal and transcriptomic analysis.

Angelica sinensis, a traditional Chinese medicinal plant, has been primarily reported due to its nutritional value. Pigmentation in this plant is an important appearance trait that directly affects its commercial value. To understand the mechanism controlling purpleness in A.

Study on extraction technology and antioxidant activity of total alkaloids from based on orthogonal design and BP neural network.

In this study, total alkaloids from were extracted and tested for their antioxidant properties. To optimize extraction methods, a single factor experiment was conducted to determine the total alkaloid concentrations of using the L (3) orthogonal design test method and the BP neural network (BPNN), resulting in the optimum extraction conditions for total alkaloids. The optimal conditions for alkaloids extraction with acid water are: HCl concentration is 0.

Site-directed mutagenesis identified the key active site residues of 2,3-oxidosqualene cyclase HcOSC6 responsible for cucurbitacins biosynthesis in .

is a Chinese traditional medicinal plant, containing cucurbitacin IIa (CuIIa) and cucurbitacin IIb (CuIIb), both of which have a wide range of pharmacological effects, including antiallergic, anti-inflammatory, and anticancer properties. However, few studies have been explored on the key enzymes that are involved in cucurbitacins biosynthesis in . Oxidosqualene cyclase (OSC) is a vital enzyme for cyclizing 2,3-oxidosqualene and its analogues.