O
Ornjira Aruksakunwong
Researcher at Rangsit University
Publications - 19
Citations - 435
Ornjira Aruksakunwong is an academic researcher from Rangsit University. The author has contributed to research in topics: Hydrogen bond & HIV-1 protease. The author has an hindex of 12, co-authored 19 publications receiving 404 citations. Previous affiliations of Ornjira Aruksakunwong include Chulalongkorn University & University of Vienna.
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Journal ArticleDOI
How amantadine and rimantadine inhibit proton transport in the M2 protein channel.
Pathumwadee Intharathep,Chittima Laohpongspaisan,Thanyada Rungrotmongkol,Arthorn Loisruangsin,Maturos Malaisree,Panita Decha,Ornjira Aruksakunwong,Krit Chuenpennit,Nopphorn Kaiyawet,Pornthep Sompornpisut,Somsak Pianwanit,Supot Hannongbua +11 more
TL;DR: To understand how antiviral drugs inhibit the replication of influenza A virus via the M2 ion channel, molecular dynamics simulations have been applied to the six possible protonation states of the M1 ion channel in free form and its complexes with two commercial drugs in a fully hydrated lipid bilayer.
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Insights into Saquinavir Resistance in the G48V HIV-1 Protease: Quantum Calculations and Molecular Dynamic Simulations
Kitiyaporn Wittayanarakul,Ornjira Aruksakunwong,Suwipa Saen-oon,Wasun Chantratita,Vudhichai Parasuk,Pornthep Sompornpisut,Supot Hannongbua +6 more
TL;DR: Molecular dynamics results combined with the quantum-based and molecular mechanics Poisson-Boltzmann surface area calculations indicated a monoprotonation took place on D25, one of the triad active site residues in the mutant HIV-1 protease complexed with saquinavir.
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Understanding of known drug-target interactions in the catalytic pocket of neuraminidase subtype N1
Maturos Malaisree,Thanyada Rungrotmongkol,Panita Decha,Pathumwadee Intharathep,Ornjira Aruksakunwong,Supot Hannongbua +5 more
TL;DR: To provide detailed information and insight into the drug‐target interaction, structure, solvation, and dynamic and thermodynamic properties, the three known‐neuraminidase inhibitors embedded in the catalytic site of neuraminid enzyme (NA) subtype N1 were studied using molecular dynamics simulations.
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Source of oseltamivir resistance in avian influenza H5N1 virus with the H274Y mutation
Maturos Malaisree,Thanyada Rungrotmongkol,Nadtanet Nunthaboot,Ornjira Aruksakunwong,Pathumwadee Intharathep,Panita Decha,Pornthep Sompornpisut,Supot Hannongbua +7 more
TL;DR: In this paper, molecular dynamics simulations were carried out for the mutant oseltamivir-NA complex, to provide detailed information on the oselto-selvir-resistance resulting from the H274Y mutation in neuraminidase (NA) of avian influenza H5N1 viruses.
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Source of High Pathogenicity of an Avian Influenza Virus H5N1: Why H5 Is Better Cleaved by Furin
Panita Decha,Thanyada Rungrotmongkol,Pathumwadee Intharathep,Maturos Malaisree,Ornjira Aruksakunwong,Chittima Laohpongspaisan,Vudhichai Parasuk,Pornthep Sompornpisut,Somsak Pianwanit,Sirirat Kokpol,Supot Hannongbua +10 more
TL;DR: The simulated data provide a clear answer to the question of why inserted H5 is better cleaved by FR than the other subtypes, explaining the high pathogenicity of avian influenza H5N1.