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Max Yen

Researcher at Southern Illinois University Carbondale

Publications -  13
Citations -  1709

Max Yen is an academic researcher from Southern Illinois University Carbondale. The author has contributed to research in topics: Catalysis & Chiral resolution. The author has an hindex of 7, co-authored 13 publications receiving 1637 citations.

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Effect of side-chain substituents on self-assembly of perylene diimide molecules: morphology control.

TL;DR: The aggregate of DD-PTCDI shows a pronounced absorption band at the longer wavelength, whereas the absorption of ND-P TCDI aggregate is not significant in the same wavelength region, and optical spectral observations are reminiscent of the previous theoretical investigation on the side-chain-modulated electronic properties of PTCDI assembly.
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Detection of Explosives with a Fluorescent Nanofibril Film

TL;DR: A new type of fluorescence sensory material has been developed from an alkoxycarbonyl-substituted carbazole-cornered tetracycle, which facilitates long-range exciton migration and favors adsorption and diffusion of gaseous adsorbates within the film.
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Recycling of homogeneous Pd catalysts using superparamagnetic nanoparticles as novel soluble supports for Suzuki, Heck, and Sonogashira cross-coupling reactions

TL;DR: Recycling of homogeneous catalysts could be achieved by using magnetic nanoparticles and solid-phase beads, but nanoparticle-supported catalysis proceeded much faster than its counterpart on resins.
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Nanofibril Self-Assembly of an Arylene Ethynylene Macrocycle

TL;DR: Nanofibril structures have been fabricated from an arylene ethynylene macrocycle, which consists of a square frame corner-joined by four carbazole moieties, with optimal pi-pi stacking in cooperation with the side-chain association.
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Superparamagnetic nanoparticle-supported enzymatic resolution of racemic carboxylates

TL;DR: Candida rugosa lipase immobilized on maghemite nanoparticles demonstrated high stereoselectivity in kinetic resolution of racemic carboxylates and improved long-term stability over its parent free enzyme, allowing the supported enzyme to be repeatedly used for a series of chiral resolution reactions.