Yuan-Ling Xia on Muck Rack

Yuan-Ling Xia

As seen in: MDPI, Texas Medical Center
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Articles

Computational Insights into SARS-CoV-2 Main Protease Mutations and Nirmatrelvir Efficacy: The Effects of P132H and P132H-A173V

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By Yuan-Ling Xia
| Texas Medical Center
Journal of Chemical Information and Modeling 10.1021/acs.jcim.4c00334 Post-print SARS-CoV-2, Coronavirus 3C Proteases, Mutation, Antiviral Agents, Humans, COVID-19 Drug Treatment, Molecular Dynamics Simulation, Protease Inhibitors, Leucine, Thermodynamics, Sulfonamides, Protein Binding, Succinates, Lactams, Nitriles, Proline yes Xia, Yuan-Ling; Du, Wen-Wen; Li, Yong-Ping; et al., "Computational Insights into SARS-CoV-2 Main Protease Mutations and Nirmatrelvir Efficacy: The Effects of P132H...
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Dissecting the Binding Affinity of Anti-SARS-CoV-2 Compounds to Human Transmembrane Protease, Serine 2: A Computational Study

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By Yue-Hui Shi, Jian-Xin Shen, Yan Tao, Yuan-Ling Xia
| Texas Medical Center
Abstract The human transmembrane protease, serine 2 (TMPRSS2), essential for SARS-CoV-2 entry, is a key antiviral target. Here, we computationally profiled the TMPRSS2-binding affinities of 15 antiviral compounds. Molecular dynamics (MD) simulations for the docked complexes revealed that three compounds exited the substrate-binding cavity (SBC), suggesting noncompetitive inhibition.
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"Mechanistic Origin of Different Binding Affinities of SARS-CoV and SAR" by Zhi-Bi Zhang, Yuan-Ling Xia et al.

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By Zhi-Bi Zhang, Yuan-Ling Xia, Jian-Xin Shen, Wen-Wen Du
| Texas Medical Center
Abstract The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein (RBDCoV2) has a higher binding affinity to the human receptor angiotensin-converting enzyme 2 (ACE2) than the SARS-CoV RBD (RBDCoV).
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