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Minghua Cui

Researcher at Ewha Womans University

Publications -  28
Citations -  674

Minghua Cui is an academic researcher from Ewha Womans University. The author has contributed to research in topics: TRPV1 & Docking (molecular). The author has an hindex of 13, co-authored 27 publications receiving 495 citations. Previous affiliations of Minghua Cui include Wonkwang University.

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Harnessing the Therapeutic Potential of Capsaicin and Its Analogues in Pain and Other Diseases

TL;DR: This review summarizes the historical background, source, structure and analogues of capsicin, and capsaicin-triggered TRPV1 signaling and desensitization processes and will focus on the therapeutic roles of Capsaicin and its analogues in both normal and pathophysiological conditions.
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Exploring G protein-coupled receptors (GPCRs) ligand space via cheminformatics approaches: Impact on rational drug design

TL;DR: A comprehensive view on the ligand– and structure-based cheminformatics approaches which are best illustrated via GPCR case studies is provided, and an appropriate combination of ligand-based knowledge with structure- based ones, i.e., integrated approach, which is emerging as a promising strategy for chemin Formatics-based G PCR drug design is discussed.
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Transient receptor potential vanilloid type 1 antagonists: a patent review (2011 – 2014)

TL;DR: This review article covers the patents that claim TRPV1 antagonists and were published during 2011 – 2014 and describes the representative chemical entities with important in vitro and in vivo data.
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Transmembrane 4 L Six Family Member 5 Senses Arginine for mTORC1 Signaling

TL;DR: It is proposed that lysosomal TM4SF5 senses and enables arginine efflux for mTORC1/S6K1 activation, and arginin-auxotroph in hepatocellular carcinoma may be targeted by blocking theArginine sensing using anti-TM4 SF5 reagents.
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Discovery of Potent Human Glutaminyl Cyclase Inhibitors as Anti-Alzheimer's Agents Based on Rational Design.

TL;DR: A library of glutamyl cyclase (QC) inhibitors based on the proposed binding mode of the preferred substrate, Aβ3E-42 are designed, resulting in strong interactions with the carboxylate group of Glu327 in the QC binding site and offering useful insights in designing novel QC inhibitors as a potential treatment option for AD.