Research graph
References from Distinct Mechanisms for Inhibition of SARS-CoV-2 Main Protease: Dimerization Promoted by Peptidomimetic Inhibitors and Disrupted by Ebselen. Local targets link to admitted publications; unresolved targets remain external evidence.
Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
10.1038/s41467-021-23313-7 · 2021 · External reference
Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation
10.1074/jbc.m500135200 · 2005 · External reference
Ebselen, a promising antioxidant drug: mechanisms of action and targets of biological pathways
10.1007/s11033-014-3417-x · 2014 · External reference
Structural basis for the inhibition of the SARS-CoV-2 main protease by the anti-HCV drug narlaprevir
10.1038/s41392-021-00468-9 · 2021 · External reference
Characterization of an unusual SARS-CoV-2 main protease natural variant exhibiting resistance to nirmatrelvir and ensitrelvir
10.1038/s42003-025-08487-w · 2025 · External reference
AmberTools
10.1021/acs.jcim.3c01153 · 2023 · External reference
Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease
10.1021/bi0490237 · 2004 · External reference
Regulation of the dimerization and activity of SARS-CoV-2 main protease through reversible glutathionylation of cysteine 300
10.1128/mbio.02094-21 · 2021 · External reference
Discovery of a nasal spray steroid, tixocortol, as an inhibitor of SARS-CoV-2 main protease and viral replication
10.1039/d4md00454j · 2024 · External reference
Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease
10.1016/j.str.2021.06.002 · 2021 · External reference
Allosteric inhibition of the SARS-CoV-2 Main protease: insights from mass spectrometry based assays
10.1002/anie.202010316 · 2020 · External reference
Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease
10.1038/s41467-020-18233-x · 2020 · External reference
Structural biology of SARS-CoV-1/SARS-CoV-2 main protease
10.1080/0889311x.2023.2222275 · 2023 · External reference
Targeting the dimerization of the main protease of coronaviruses: a potential broad-spectrum therapeutic strategy
10.1021/acscombsci.0c00058 · 2020 · External reference
Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants
10.1016/j.jbc.2022.101972 · 2022 · External reference
X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease
10.1126/science.abf7945 · 2021 · External reference
Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir
10.1073/pnas.1400027111 · 2014 · External reference
Identification of SARS-CoV-2 Mpro inhibitors containing P1’4-fluorobenzothiazole moiety highly active against SARS-CoV-2
10.1038/s41467-023-36729-0 · 2023 · External reference
Discovery of ketone-based covalent inhibitors of coronavirus 3CL proteases for the potential therapeutic treatment of COVID-19
10.1021/acs.jmedchem.0c01063 · 2020 · External reference
Conformational dynamics of the helix 10 region as an allosteric site in class A β-lactamase inhibitory binding
10.1021/jacs.0c04088 · External reference
Interdomain flexibility and interfacial integrity of β-lactamase inhibitory protein (BLIP) modulate its binding to class A β-lactamases
10.1016/j.jbc.2021.100980 · 2021 · External reference
Conformational Dynamics of the Helix 10 Region as an Allosteric Site in Class A β-Lactamase Inhibitory Binding
10.1021/jacs.0c04088 · External reference
Protein dynamics revealed by hydrogen/deuterium exchange mass spectrometry: Correlation between experiments and simulation
10.1002/rcm.8307 · 2019 · External reference
Inhibitor-Dependent Tolerance of New Delhi Metallo-β-Lactamase Driven by Single Mutation-Induced Conformational Changes
10.1021/jacs.5c05669 · 2025 · External reference
Cys44 of SARS-CoV-2 3CLpro affects its catalytic activity
10.1016/j.ijbiomac.2025.139590 · 2025 · External reference
Advances in hydrogen/deuterium exchange mass spectrometry and the pursuit of challenging biological systems
10.1021/acs.chemrev.1c00279 · 2021 · External reference
Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors
10.1038/s41586-020-2223-y · External reference
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
10.1038/s41594-020-0440-6 · External reference
The Substitutions L50F, E166A, and L167F in SARS-CoV-2 3CLpro Are Selected by a Protease Inhibitor In Vitro and Confer Resistance To Nirmatrelvir
10.1128/mbio.02815-22 · 2023 · External reference
Safety and efficacy of ebselen for the prevention of noise-induced hearing loss: a randomised, double-blind, placebo-controlled, phase 2 trial
10.1016/s0140-6736(17)31791-9 · 2017 · External reference
Transient Structural Dynamics of Glycogen Phosphorylase from Nonequilibrium Hydrogen/Deuterium-Exchange Mass Spectrometry
10.1021/jacs.3c08934 · 2023 · External reference
Room-temperature X-ray crystallography reveals the oxidation and reactivity of cysteine residues in SARS-CoV-2 3CL Mpro: insights into enzyme mechanism and drug design
10.1107/s2052252520012634 · 2020 · External reference
Deuteros 2.0: peptide-level significance testing of data from hydrogen deuterium exchange mass spectrometry
10.1093/bioinformatics/btaa677 · 2021 · External reference
Development of ebselen, a glutathione peroxidase mimic, for the prevention and treatment of noise-induced hearing loss
10.1055/s-0028-1111106 · 2009 · External reference
Ebselen, disulfiram, carmofur, PX-12, tideglusib, and shikonin are nonspecific promiscuous SARS-CoV-2 main protease inhibitors
10.1021/acsptsci.0c00130 · 2020 · External reference
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB
10.1021/acs.jctc.5b00255 · 2015 · External reference
Effects of the potential lithium-mimetic, ebselen, on impulsivity and emotional processing
10.1007/s00213-016-4319-5 · 2016 · External reference
Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments
10.1038/s41592-019-0459-y · 2019 · External reference
Molecular characterization of ebselen binding activity to SARS-CoV-2 main protease
10.1126/sciadv.abd0345 · 2020 · External reference
HDX-MS: an analytical tool to capture protein motion in action
10.3390/biomedicines8070224 · 2020 · External reference
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry
10.1006/jmbi.1998.1937 · 1998 · External reference
An oral SARS-CoV-2 Mpro inhibitor clinical candidate for the treatment of COVID-19
10.1126/science.abl4784 · 2021 · External reference
Stabilization of the dimeric state of SARS-CoV-2 main protease by GC376 and nirmatrelvir
10.3390/ijms24076062 · 2023 · External reference
Inhibition of SARS-CoV-2 main protease: a repurposing study that targets the dimer interface of the protein
10.1080/07391102.2021.1910571 · 2022 · External reference
Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against Mpro and cathepsin L
10.1126/sciadv.abe0751 · 2020 · External reference
Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
10.1074/jbc.m206060200 · 2002 · External reference
Medicinal chemistry strategies towards the development of non-covalent SARS-CoV-2 Mpro inhibitors
10.1016/j.apsb.2023.08.004 · 2024 · External reference
Computational tools for hydrogen–deuterium exchange mass spectrometry data analysis
10.1021/acs.chemrev.4c00438 · 2024 · External reference
SARS-CoV-2 main protease: a molecular dynamics study
10.1021/acs.jcim.0c00575 · 2020 · External reference
An extended conformation of SARS-CoV-2 main protease reveals allosteric targets
10.1073/pnas.2120913119 · 2022 · External reference
Charging of Proteins in Native Mass Spectrometry
10.1007/s13361-016-1517-7 · 2017 · External reference
Allosteric inhibition of SARS-CoV-2 3CL protease by colloidal bismuth subcitrate
10.1039/d1sc03526f · 2021 · External reference
Thermokinetic Analysis of Protein Subunit Exchange by Variable-Temperature Native Mass Spectrometry
10.1021/acs.biochem.9b00911 · 2019 · External reference
Subunit exchange rates in Hepatitis B virus capsids are geometry- and temperature-dependent
10.1039/c0cp00692k · 2010 · External reference
Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication
10.1038/s41467-020-18096-2 · 2020 · External reference
Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro
10.1126/sciadv.add2191 · 2022 · External reference
A review of the latest research on M pro targeting SARS-COV inhibitors
10.1039/d1md00066g · 2021 · External reference
The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
10.1073/pnas.1835675100 · 2003 · External reference
Measurement of rate constants for homodimer subunit exchange using double electron-electron resonance and paramagnetic relaxation enhancements
10.1007/s10858-012-9685-7 · 2013 · External reference
Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors
10.1126/science.abb3405 · 2020 · External reference
An allosteric mechanism for potent inhibition of SARS-CoV-2 main proteinase
10.1016/j.ijbiomac.2024.130644 · 2024 · External reference
Crystal structure of SARS-CoV-2 main protease in complex with protease inhibitor PF-07321332
10.1007/s13238-021-00883-2 · 2022 · External reference
A Novel Coronavirus from Patients with Pneumonia in China, 2019
10.1056/nejmoa2001017 · 2020 · External reference
Allosteric inhibition of the SARS-CoV-2 Main protease: insights from mass spectrometry based assays
10.1002/anie.202010316 · ExternalCitation · doi-reference
Protein dynamics revealed by hydrogen/deuterium exchange mass spectrometry: Correlation between experiments and simulation
10.1002/rcm.8307 · ExternalCitation · doi-reference
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry
10.1006/jmbi.1998.1937 · ExternalCitation · doi-reference
Effects of the potential lithium-mimetic, ebselen, on impulsivity and emotional processing
10.1007/s00213-016-4319-5 · ExternalCitation · doi-reference
Measurement of rate constants for homodimer subunit exchange using double electron-electron resonance and paramagnetic relaxation enhancements
10.1007/s10858-012-9685-7 · ExternalCitation · doi-reference
Ebselen, a promising antioxidant drug: mechanisms of action and targets of biological pathways
10.1007/s11033-014-3417-x · ExternalCitation · doi-reference
Crystal structure of SARS-CoV-2 main protease in complex with protease inhibitor PF-07321332
10.1007/s13238-021-00883-2 · ExternalCitation · doi-reference
Charging of Proteins in Native Mass Spectrometry
10.1007/s13361-016-1517-7 · ExternalCitation · doi-reference
Medicinal chemistry strategies towards the development of non-covalent SARS-CoV-2 Mpro inhibitors
10.1016/j.apsb.2023.08.004 · ExternalCitation · doi-reference
An allosteric mechanism for potent inhibition of SARS-CoV-2 main proteinase
10.1016/j.ijbiomac.2024.130644 · ExternalCitation · doi-reference
Cys44 of SARS-CoV-2 3CLpro affects its catalytic activity
10.1016/j.ijbiomac.2025.139590 · ExternalCitation · doi-reference
Interdomain flexibility and interfacial integrity of β-lactamase inhibitory protein (BLIP) modulate its binding to class A β-lactamases
10.1016/j.jbc.2021.100980 · ExternalCitation · doi-reference
Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants
10.1016/j.jbc.2022.101972 · ExternalCitation · doi-reference
Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease
10.1016/j.str.2021.06.002 · ExternalCitation · doi-reference
Safety and efficacy of ebselen for the prevention of noise-induced hearing loss: a randomised, double-blind, placebo-controlled, phase 2 trial
10.1016/s0140-6736(17)31791-9 · ExternalCitation · doi-reference
Thermokinetic Analysis of Protein Subunit Exchange by Variable-Temperature Native Mass Spectrometry
10.1021/acs.biochem.9b00911 · ExternalCitation · doi-reference
Advances in hydrogen/deuterium exchange mass spectrometry and the pursuit of challenging biological systems
10.1021/acs.chemrev.1c00279 · ExternalCitation · doi-reference
Computational tools for hydrogen–deuterium exchange mass spectrometry data analysis
10.1021/acs.chemrev.4c00438 · ExternalCitation · doi-reference
SARS-CoV-2 main protease: a molecular dynamics study
10.1021/acs.jcim.0c00575 · ExternalCitation · doi-reference
AmberTools
10.1021/acs.jcim.3c01153 · ExternalCitation · doi-reference
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB
10.1021/acs.jctc.5b00255 · ExternalCitation · doi-reference
Discovery of ketone-based covalent inhibitors of coronavirus 3CL proteases for the potential therapeutic treatment of COVID-19
10.1021/acs.jmedchem.0c01063 · ExternalCitation · doi-reference
Targeting the dimerization of the main protease of coronaviruses: a potential broad-spectrum therapeutic strategy
10.1021/acscombsci.0c00058 · ExternalCitation · doi-reference
Ebselen, disulfiram, carmofur, PX-12, tideglusib, and shikonin are nonspecific promiscuous SARS-CoV-2 main protease inhibitors
10.1021/acsptsci.0c00130 · ExternalCitation · doi-reference
Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease
10.1021/bi0490237 · ExternalCitation · doi-reference
Conformational Dynamics of the Helix 10 Region as an Allosteric Site in Class A β-Lactamase Inhibitory Binding
10.1021/jacs.0c04088 · ExternalCitation · doi-reference
Transient Structural Dynamics of Glycogen Phosphorylase from Nonequilibrium Hydrogen/Deuterium-Exchange Mass Spectrometry
10.1021/jacs.3c08934 · ExternalCitation · doi-reference
Inhibitor-Dependent Tolerance of New Delhi Metallo-β-Lactamase Driven by Single Mutation-Induced Conformational Changes
10.1021/jacs.5c05669 · ExternalCitation · doi-reference
Structural basis for the inhibition of the SARS-CoV-2 main protease by the anti-HCV drug narlaprevir
10.1038/s41392-021-00468-9 · ExternalCitation · doi-reference
Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication
10.1038/s41467-020-18096-2 · ExternalCitation · doi-reference
Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease
10.1038/s41467-020-18233-x · ExternalCitation · doi-reference
Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
10.1038/s41467-021-23313-7 · ExternalCitation · doi-reference
Identification of SARS-CoV-2 Mpro inhibitors containing P1’4-fluorobenzothiazole moiety highly active against SARS-CoV-2
10.1038/s41467-023-36729-0 · ExternalCitation · doi-reference
Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors
10.1038/s41586-020-2223-y · ExternalCitation · doi-reference
Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments
10.1038/s41592-019-0459-y · ExternalCitation · doi-reference
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
10.1038/s41594-020-0440-6 · ExternalCitation · doi-reference
Characterization of an unusual SARS-CoV-2 main protease natural variant exhibiting resistance to nirmatrelvir and ensitrelvir
10.1038/s42003-025-08487-w · ExternalCitation · doi-reference
Subunit exchange rates in Hepatitis B virus capsids are geometry- and temperature-dependent
10.1039/c0cp00692k · ExternalCitation · doi-reference
A review of the latest research on M pro targeting SARS-COV inhibitors
10.1039/d1md00066g · ExternalCitation · doi-reference
Allosteric inhibition of SARS-CoV-2 3CL protease by colloidal bismuth subcitrate
10.1039/d1sc03526f · ExternalCitation · doi-reference
Discovery of a nasal spray steroid, tixocortol, as an inhibitor of SARS-CoV-2 main protease and viral replication
10.1039/d4md00454j · ExternalCitation · doi-reference
Development of ebselen, a glutathione peroxidase mimic, for the prevention and treatment of noise-induced hearing loss
10.1055/s-0028-1111106 · ExternalCitation · doi-reference
A Novel Coronavirus from Patients with Pneumonia in China, 2019
10.1056/nejmoa2001017 · ExternalCitation · doi-reference
Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir
10.1073/pnas.1400027111 · ExternalCitation · doi-reference
The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
10.1073/pnas.1835675100 · ExternalCitation · doi-reference
An extended conformation of SARS-CoV-2 main protease reveals allosteric targets
10.1073/pnas.2120913119 · ExternalCitation · doi-reference
Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
10.1074/jbc.m206060200 · ExternalCitation · doi-reference
Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation
10.1074/jbc.m500135200 · ExternalCitation · doi-reference
Inhibition of SARS-CoV-2 main protease: a repurposing study that targets the dimer interface of the protein
10.1080/07391102.2021.1910571 · ExternalCitation · doi-reference
Structural biology of SARS-CoV-1/SARS-CoV-2 main protease
10.1080/0889311x.2023.2222275 · ExternalCitation · doi-reference
Deuteros 2.0: peptide-level significance testing of data from hydrogen deuterium exchange mass spectrometry
10.1093/bioinformatics/btaa677 · ExternalCitation · doi-reference
Room-temperature X-ray crystallography reveals the oxidation and reactivity of cysteine residues in SARS-CoV-2 3CL Mpro: insights into enzyme mechanism and drug design
10.1107/s2052252520012634 · ExternalCitation · doi-reference
Molecular characterization of ebselen binding activity to SARS-CoV-2 main protease
10.1126/sciadv.abd0345 · ExternalCitation · doi-reference
Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against Mpro and cathepsin L
10.1126/sciadv.abe0751 · ExternalCitation · doi-reference
Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro
10.1126/sciadv.add2191 · ExternalCitation · doi-reference
Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors
10.1126/science.abb3405 · ExternalCitation · doi-reference
X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease
10.1126/science.abf7945 · ExternalCitation · doi-reference
An oral SARS-CoV-2 Mpro inhibitor clinical candidate for the treatment of COVID-19
10.1126/science.abl4784 · ExternalCitation · doi-reference
Regulation of the dimerization and activity of SARS-CoV-2 main protease through reversible glutathionylation of cysteine 300
10.1128/mbio.02094-21 · ExternalCitation · doi-reference
The Substitutions L50F, E166A, and L167F in SARS-CoV-2 3CLpro Are Selected by a Protease Inhibitor In Vitro and Confer Resistance To Nirmatrelvir
10.1128/mbio.02815-22 · ExternalCitation · doi-reference
HDX-MS: an analytical tool to capture protein motion in action
10.3390/biomedicines8070224 · ExternalCitation · doi-reference
Stabilization of the dimeric state of SARS-CoV-2 main protease by GC376 and nirmatrelvir
10.3390/ijms24076062 · ExternalCitation · doi-reference
