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Yuan-Hao Hsu
Researcher at Tunghai University
Publications - 17
Citations - 1382
Yuan-Hao Hsu is an academic researcher from Tunghai University. The author has contributed to research in topics: Hydrogen–deuterium exchange & Cardiolipin. The author has an hindex of 12, co-authored 16 publications receiving 1186 citations. Previous affiliations of Yuan-Hao Hsu include University of California, San Diego & University of California, Riverside.
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Journal ArticleDOI
Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.
TL;DR: The phospholipase A2 (PLA2) superfamily traces its roots to the identification of lytic actions of snake venom at the end of the 19th century and to the late 1980’s when PLA2-like activities were reported in mammalian cells in contrast to extracellular secreted activities from venom and pancreas.
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Potent and Selective Fluoroketone Inhibitors of Group VIA Calcium-Independent Phospholipase A2
George Kokotos,Yuan-Hao Hsu,John E. Burke,Constantinos Baskakis,Christoforos G. Kokotos,Victoria Magrioti,Edward A. Dennis +6 more
TL;DR: The structure-activity relationship between fluoroketones and GVIA iPLA(2) inhibition proved to be of paramount importance with the presence of a naphthyl group, and hexa- and octafluoro ketones were also found to be potent inhibitors.
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Localizing the membrane binding region of Group VIA Ca2+-independent phospholipase A2 using peptide amide hydrogen/deuterium exchange mass spectrometry.
TL;DR: A computational homology model based on homologous structures was constructed and combined with the deuterium exchange results in the presence of lipid substrate have allowed the first structural model of GVIA-2 iPLA2 as well as the interfacial lipid binding region to be proposed.
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Assessing Phospholipase A2 Activity toward Cardiolipin by Mass Spectrometry
TL;DR: It is demonstrated that cardiolipin is a substrate for s PLA2, cPLA2 and iPLA2, but not for Lp-PLA1, and that none of these PLA2s have significant PLA1 activities toward dilyso-cardiolipIn.
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A Phospholipid Substrate Molecule Residing in the Membrane Surface Mediates Opening of the Lid Region in Group IVA Cytosolic Phospholipase A2
TL;DR: Using the GIVA phospholipase A2 irreversible inhibitor methyl-arachidonyl fluorophosphonate, this enzyme was able to isolate structural changes caused only by pseudo-substrate binding, implying that most of the changes seen in the catalytic domain are due to a substrate-mediated, not interface- mediated, lid opening, which exposes the active site to water.