B
Bing Xu
Researcher at Brandeis University
Publications - 373
Citations - 29970
Bing Xu is an academic researcher from Brandeis University. The author has contributed to research in topics: Self-healing hydrogels & Cancer cell. The author has an hindex of 83, co-authored 357 publications receiving 26713 citations. Previous affiliations of Bing Xu include University of Pennsylvania & University of Hong Kong.
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Introducing D-amino acid or simple glycoside into small peptides to enable supramolecular hydrogelators to resist proteolysis.
TL;DR: This work suggests that the inclusion of a simple glycogen in hydrogelators is a useful approach to increase their biostability, and the gained understanding from the work may ultimately lead to development of hydrogels of functional peptides for biomedical applications that require long-termBiostability.
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Using Enzymes to Control Molecular Hydrogelation
Zhimou Yang,Bing Xu +1 more
TL;DR: Using an enzymatic reaction to convert a precursor into a Hydrogelator or vice versa, one can control the delivery, functions, and responses of a hydrogel according to a specific biological condition or environment, thus providing an accessible route to creating sophisticated soft materials for potential biomedical applications.
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Silver Surface Iodination for Enhancing the Conductivity of Conductive Composites
TL;DR: In this paper, the electrical conductivity of a silver microflake-filled conductive composites is dramatically improved after a filler surface treatment, and the reliability of the printed thin film resistors is evaluated by both the 85 °C/85% relative humidity moisture exposure and the −40 ∼ 125 °C thermal cycling exposure.
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Using matrix metalloprotease-9 (MMP-9) to trigger supramolecular hydrogelation
TL;DR: This work reports the first example of using MMP-9 to catalyze the formation and self-assembly of a supramolecular hydrogelator and subsequenthydrogelation.
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Regulating the Rate of Molecular Self-Assembly for Targeting Cancer Cells.
Jie Zhou,Xuewen Du,Bing Xu +2 more
TL;DR: A simple molecular design of the substrates of phosphatases-tailoring the number of phosphates on peptidic substrates-is able to regulate the rate of molecular self-assembly of the enzyme reaction product, which allows selective inhibition of osteosarcoma cells over hepatocytes.