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Shi-Zhong Luo

Researcher at Beijing University of Chemical Technology

Publications -  44
Citations -  814

Shi-Zhong Luo is an academic researcher from Beijing University of Chemical Technology. The author has contributed to research in topics: Transmembrane domain & Peptide. The author has an hindex of 15, co-authored 43 publications receiving 610 citations. Previous affiliations of Shi-Zhong Luo include Tsinghua University & University of Texas Health Science Center at Houston.

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An aptamer based surface plasmon resonance biosensor for the detection of ochratoxin A in wine and peanut oil.

TL;DR: A surface plasmon resonance (SPR) biosensor using an anti-OTA aptamer immobilized sensor chip was developed to measure ochratoxin A quantificationally through a straightforward direct binding assay, showing good analytical performances with limits of detection much lower than the maximum residue limit, as well as good reproducibility and stability.
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Role of peptide self-assembly in antimicrobial peptides.

TL;DR: The influences of peptide self‐assembly on the activity and mode of action, and some specific features it introduces to the AMPs, such as particular responsiveness, improved cell selectivity and stability and sustained release are discussed.
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A direct determination of AFBs in vinegar by aptamer-based surface plasmon resonance biosensor.

TL;DR: The developed SPR assay is a simple, fast and sensitive approach for the detection of residual AFBs in agricultural products and foodstuffs like vinegar, and shows high specificity towards AFB1 and AFB2, but hardly bound to other toxins with similar structures.
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Amyloid-Forming Segment Induces Aggregation of FUS-LC Domain from Phase Separation Modulated by Site-Specific Phosphorylation

TL;DR: The RNA-binding protein fused in sarcoma (FUS) forms physiological granules and pathological fibrils, which facilitate RNA functions and cause neurodegenerative diseases, respectively, and Solid-state NMR spectroscopy and computational modeling implied that site-specific phosphorylation at Ser61 plays key roles in FUS assembly by disrupting both intra- and intermolecular interactions that maintain the amyloid core structure.
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Role of the transmembrane domain of glycoprotein IX in assembly of the glycoprotein Ib-IX complex.

TL;DR: The TM domain, rather than the cytoplasmic domain, of GPIX plays an important role in expression and assembly of the GPIb–IX complex by interacting with its counterparts of G PIb.