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Cellular Activities of SARS-CoV-2 Main Protease Inhibitors Reveal Their Unique Characteristics

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/cbic.202000047openalex-snapshot
Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019‐nCoV
inferredcites →https://doi.org/10.1002/cmdc.202000924openalex-snapshot
A Quick Route to Multiple Highly Potent SARS‐CoV‐2 Main Protease Inhibitors**
inferredcites →https://doi.org/10.1002/prot.26042openalex-snapshot
Human SARS CoV ‐2 spike protein mutations
inferredcites →https://doi.org/10.1016/j.bmcl.2008.08.082openalex-snapshot
Design, synthesis and antiviral efficacy of a series of potent chloropyridyl ester-derived SARS-CoV 3CLpro inhibitors
inferredcites →https://doi.org/10.1016/j.cell.2020.02.052openalex-snapshot
SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
inferredcites →https://doi.org/10.1016/j.celrep.2020.108254openalex-snapshot
Furin Inhibitors Block SARS-CoV-2 Spike Protein Cleavage to Suppress Virus Production and Cytopathic Effects
inferredcites →https://doi.org/10.1016/j.chembiol.2005.12.008openalex-snapshot
Stable Benzotriazole Esters as Mechanism-Based Inactivators of the Severe Acute Respiratory Syndrome 3CL Protease
inferredcites →https://doi.org/10.1016/j.chembiol.2008.04.011openalex-snapshot
A Structural View of the Inactivation of the SARS Coronavirus Main Proteinase by Benzotriazole Esters
inferredcites →https://doi.org/10.1016/s2666-5247(21)00068-9openalex-snapshot
SARS-CoV-2 spike E484K mutation reduces antibody neutralisation
inferredcites →https://doi.org/10.1021/acs.jmedchem.0c01063openalex-snapshot
Discovery of Ketone-Based Covalent Inhibitors of Coronavirus 3CL Proteases for the Potential Therapeutic Treatment of COVID-19
inferredcites →https://doi.org/10.1021/acs.jmedchem.5b01461openalex-snapshot
An Overview of Severe Acute Respiratory Syndrome–Coronavirus (SARS-CoV) 3CL Protease Inhibitors: Peptidomimetics and Small Molecule Chemotherapy
inferredcites →https://doi.org/10.1021/acschembio.0c00875openalex-snapshot
A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells
inferredcites →https://doi.org/10.1021/cb5009734openalex-snapshot
A Genetically Encoded FRET Sensor for Intracellular Heme
inferredcites →https://doi.org/10.1038/s41392-021-00558-8openalex-snapshot
Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development
inferredcites →https://doi.org/10.1038/s41418-020-00720-9openalex-snapshot
COVID-19 vaccines: where we stand and challenges ahead
inferredcites →https://doi.org/10.1038/s41422-020-0356-zopenalex-snapshot
Boceprevir, GC-376, and calpain inhibitors II, XII inhibit SARS-CoV-2 viral replication by targeting the viral main protease
inferredcites →https://doi.org/10.1038/s41467-020-18233-xopenalex-snapshot
Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease
inferredcites →https://doi.org/10.1038/s41586-020-2180-5openalex-snapshot
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
inferredcites →https://doi.org/10.1038/s41586-020-2223-yopenalex-snapshot
Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors
inferredcites →https://doi.org/10.1038/s41594-020-0440-6openalex-snapshot
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
inferredcites →https://doi.org/10.1073/pnas.2010470117openalex-snapshot
Identify potent SARS-CoV-2 main protease inhibitors via accelerated free energy perturbation-based virtual screening of existing drugs
inferredcites →https://doi.org/10.1073/pnas.2012201118openalex-snapshot
Bepridil is potent against SARS-CoV-2 in vitro
inferredcites →https://doi.org/10.1073/pnas.2024420118openalex-snapshot
Dipyridamole, chloroquine, montelukast sodium, candesartan, oxytetracycline, and atazanavir are not SARS-CoV-2 main protease inhibitors
inferredcites →https://doi.org/10.1093/cid/ciaa237openalex-snapshot
In Vitro Antiviral Activity and Projection of Optimized Dosing Design of Hydroxychloroquine for the Treatment of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2)
inferredcites →https://doi.org/10.1093/infdis/jiy332openalex-snapshot
The Calcium Channel Blocker Bepridil Demonstrates Efficacy in the Murine Model of Marburg Virus Disease
inferredcites →https://doi.org/10.1101/2020.08.29.272864openalex-snapshot
A simplified cell-based assay to identify coronavirus 3CL protease inhibitors
inferredcites →https://doi.org/10.1126/sciadv.abe0751openalex-snapshot
Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against M pro and cathepsin L
inferredcites →https://doi.org/10.1126/science.abb3405openalex-snapshot
Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors
inferredcites →https://doi.org/10.1126/science.abb4489openalex-snapshot
Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease
inferredcites →https://doi.org/10.1126/science.abf1611openalex-snapshot
SARS-CoV-2 M pro inhibitors with antiviral activity in a transgenic mouse model
inferredcites →https://doi.org/10.1126/science.abf7945openalex-snapshot
X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease
inferredcites →https://doi.org/10.1128/jvi.01348-12openalex-snapshot
Broad-Spectrum Antivirals against 3C or 3C-Like Proteases of Picornaviruses, Noroviruses, and Coronaviruses
inferredcites →https://doi.org/10.1371/journal.pone.0245962openalex-snapshot
A drug repurposing screen identifies hepatitis C antivirals as inhibitors of the SARS-CoV2 main protease
inferredcites →https://doi.org/10.1371/journal.ppat.1009013openalex-snapshot
The role of cysteine peptidases in coronavirus cell entry and replication: The therapeutic potential of cathepsin inhibitors
inferredcites →https://doi.org/10.1371/journal.ppat.1009212openalex-snapshot
Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/cmdc.202100456openalex-snapshot
MPI8 is Potent against SARS‐CoV‐2 by Inhibiting Dually and Selectively the SARS‐CoV‐2 Main Protease and the Host Cathepsin L**
inferred← citeshttps://doi.org/10.1016/b978-0-443-36518-8.00023-0openalex-snapshot
Targeting 3CLpro for broad-spectrum antiviral therapy: Structural insights, inhibitor development, and the future of PROTACs
inferred← citeshttps://doi.org/10.1016/j.apsb.2021.10.026openalex-snapshot
Validation and invalidation of SARS-CoV-2 main protease inhibitors using the Flip-GFP and Protease-Glo luciferase assays
inferred← citeshttps://doi.org/10.1016/j.ejmech.2023.115979openalex-snapshot
Development of de-novo coronavirus 3-chymotrypsin-like protease (3CLpro) inhibitors since COVID-19 outbreak: A strategy to tackle challenges of persistent virus infection
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c01037openalex-snapshot
Structure-Guided Design of Potent Inhibitors of SARS-CoV-2 3CL Protease: Structural, Biochemical, and Cell-Based Studies
inferred← citeshttps://doi.org/10.1021/acsptsci.1c00240openalex-snapshot
Validation and Invalidation of SARS-CoV-2 Papain-like Protease Inhibitors
inferred← citeshttps://doi.org/10.1101/2021.12.18.473326openalex-snapshot
The P3 O - Tert -Butyl-Threonine is Key to High Cellular and Antiviral Potency for Aldehyde-Based SARS-CoV-2 Main Protease Inhibitors
inferred← citeshttps://doi.org/10.1101/2021.12.18.473330openalex-snapshot
The N -Terminal Carbamate is Key to High Cellular and Antiviral Potency for Boceprevir-Based SARS-CoV-2 Main Protease Inhibitors
inferred← citeshttps://doi.org/10.3390/ijms222111779openalex-snapshot
Structural and Biochemical Analysis of the Dual Inhibition of MG-132 against SARS-CoV-2 Main Protease (Mpro/3CLpro) and Human Cathepsin-L
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