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Presentation . 2022
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Presentation . 2022
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The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature

Authors: Fraser, James;

The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature

Abstract

James Fraser's presentation at the monthly [virtual] Antiviral Drug Discovery (AViDD) Open Science Forum on 19 October 2022. His talk focuses on finding new ligands to the SARS CoV 2 Macrodomain using Fragments, Neutrons, and Entropy. Public datasets Identifying new ligands for the SARS-CoV-2 Macrodomain by Fragment Screening and Multi-temperature Crystallography [Interactively explore on Fragalysis] Preprints and papers Iterative computational design and crystallographic screening identifies potent inhibitors targeting the Nsp3 Macrodomain of SARS-CoV-2 [DOI] Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking [DOI] The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature [DOI] Of problems and opportunities—How to treat and how to not treat crystallographic fragment screening data [DOI] Tutorials Multi-state models from PanDDA Inspecting PanDDA event maps deposited in the Protein Data Bank Software Fragmentstein X-ray fragment merging ligand design tools You can find a recording of his talk on the AViDD Open Science Forum Youtube page James Fraser is a member of the QBI Coronavirus Research Group (QCRG) AViDD Center.

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Keywords

Antiviral Drug Discovery, QBI Coronavirus Research Group (QCRG) AViDD Center, AViDD, Open Science Forum, open science, Antiviral Drug Discovery Open Science Forum, AViDD Open Science Forum

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This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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