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Rui-Xue Xu

Researcher at Shandong University

Publications -  11
Citations -  217

Rui-Xue Xu is an academic researcher from Shandong University. The author has contributed to research in topics: O-methyltransferase & Aytoniaceae. The author has an hindex of 7, co-authored 11 publications receiving 152 citations. Previous affiliations of Rui-Xue Xu include Pompeu Fabra University.

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Cloning and functional characterization of a 4-coumarate CoA ligase from liverwort Plagiochasma appendiculatum

TL;DR: Kinetic analysis indicated that the most favorable substrate for Pa4CL1 is p-coumaric acid, and the recombinant protein was heterologously expressed in Escherichia coli and exhibited a high level of 4CL activity.
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Hyperspectral-Enhanced Dark Field Microscopy for Single and Collective Nanoparticle Characterization in Biological Environments.

TL;DR: The morphological evolution of nanoparticles over time and in different biological environments is followed up to better understand and establish a link between the observed nanoparticles’ changes and cellular behaviors.
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Functional characterization of a Plagiochasma appendiculatum flavone synthase I showing flavanone 2-hydroxylase activity

TL;DR: PaFNS I represents a 2‐ODD in which a hydrophobic π‐stacking interaction between the key residue and the naringenin A‐ring determines 2‐hydroxyflavanone formation.
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Functional characterization of a Mg(2+)-dependent O-methyltransferase with coumarin as preferred substrate from the liverwort Plagiochasma appendiculatum

TL;DR: The catalytic capacities of the studied protein suggest that two routes to scopoletin might co-exist in liverworts in that the enzyme involved in the methylation process participates in both paths, but especially the route from esculetin.
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Functional characterization of a plastidal cation-dependent O-methyltransferase from the liverwort Plagiochasma appendiculatum.

TL;DR: Although the substrate selectivity and biochemical feature of PaOMT1 is similar to CCoAOMT-like enzymes, the sequence alignment results indicated PaOMt1 is closer to true CCo aOMT enzymes.