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Yisheng Xu

Researcher at East China University of Science and Technology

Publications -  98
Citations -  2907

Yisheng Xu is an academic researcher from East China University of Science and Technology. The author has contributed to research in topics: Catalysis & Chemistry. The author has an hindex of 23, co-authored 78 publications receiving 2164 citations. Previous affiliations of Yisheng Xu include University of Massachusetts Amherst & University of Science and Technology of China.

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Real-Time Tracking and In Vivo Visualization of β-Galactosidase Activity in Colorectal Tumor with a Ratiometric Near-Infrared Fluorescent Probe.

TL;DR: This work designs an enzyme-activatable ratiometric near-infrared (NIR) probe (DCM-βgal) for the real-time fluorescent quantification and trapping of β-gal activity in vivo and in situ, and provides a potential tool for in vivo real- time tracking enzyme activity in preclinical applications.
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Protein–polyelectrolyte interactions

TL;DR: An ongoing theme is the role of electrostatics, and it is shown how this leads to the variety of physical forms taken by protein–polyelectrolyte complexes, in a review of the literature over the last 8 years.
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Protein Purification by Polyelectrolyte Coacervation: Influence of Protein Charge Anisotropy on Selectivity

TL;DR: High-sensitivity turbidimetric titrations were used to define conditions of complex formation and coacervation of proteins with the cationic polyelectrolyte, poly(diallyldimethylammonium chloride) (PDADMAC), and the resultant phase boundaries are nonmonotonic with respect to ionic strength.
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Mineral-Enhanced Polyacrylic Acid Hydrogel as an Oyster-Inspired Organic–Inorganic Hybrid Adhesive

TL;DR: A novel type of oyster-inspired organic-inorganic adhesive based on a biomineralized polyelectrolyte hydrogel is reported, which consists of polyacrylic acid physically cross-linked by very small amorphous calcium carbonate nanoparticles (<3 nm).
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Electrostatic Selectivity in Protein–nanoparticle Interactions

TL;DR: The binding of bovine serum albumin and β-lactoglobulin to TTMA to BLG was studied by high-resolution turbidimetry, dynamic light scattering, and isothermal titration calorimetry (to measure binding energetics), all as a function of pH and ionic strength.