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Lixin Zhang

Researcher at East China University of Science and Technology

Publications -  716
Citations -  28752

Lixin Zhang is an academic researcher from East China University of Science and Technology. The author has contributed to research in topics: Cache & Chemistry. The author has an hindex of 78, co-authored 659 publications receiving 23737 citations. Previous affiliations of Lixin Zhang include Chinese Academy of Sciences & University of Science and Technology of China.

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Chemical preparation, biological evaluation and 3D-QSAR of ethoxysulfuron derivatives as novel antifungal agents targeting acetohydroxyacid synthase.

TL;DR: 68 novel ethoxysulfulron derivatives are designed and synthesized and evaluated their inhibition constants against C. albicans AHAS and cell based minimum inhibitory concentration values and indicated that some ES derivatives should be considered as promising hits to develop antifungal drugs with novel biological target.
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A novel signal transduction system for development of uric acid biosensors

TL;DR: A novel signal transduction system for the development of UA biosensors with the characteristics of stability and ease-of-use is presented, which hold great potential for clinical application.
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The Key Role of van der Waals Interactions in MPc/Au(111) (M = Co, Fe, H2) Systems Based on First-Principles Calculations

TL;DR: In this paper, first principles calculations for metal-phthalocyanines (MPc, M = Co, Fe, H2) adsorbed on Au(111) surfaces with LDA, PW91, and optB86b-vdW functionals are performed.
Proceedings ArticleDOI

RAGuard: A Hardware Based Mechanism for Backward-Edge Control-Flow Integrity

TL;DR: This work proposes a novel hardware-assisted mechanism (RAGuard) that binds a message authentication code to each return address and enhances security via a physical unclonable function and a hardware hash function.
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Fluorescence and Fourier-transform infrared spectroscopic studies on the role of disulfide bond in the calcium binding in the 33 kDa protein of Photosystem II.

TL;DR: Fluorescence and Fourier-transform infrared spectroscopic studies indicate that the conformation of the 33 kDa protein is altered upon reduction, while the reduced protein still retains the secondary structure, and may suggest that the disulfide bridge is not essential for calcium binding.