"Protease Inhibitors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Descriptor ID |
D011480
|
MeSH Number(s) |
D27.505.519.389.745
|
Concept/Terms |
Protease Inhibitors- Protease Inhibitors
- Inhibitors, Protease
- Endopeptidase Inhibitors
- Inhibitors, Endopeptidase
- Protease Inhibitor
- Inhibitor, Protease
- Peptide Hydrolase Inhibitors
- Hydrolase Inhibitors, Peptide
- Inhibitors, Peptide Hydrolase
- Peptide Peptidohydrolase Inhibitors
- Inhibitors, Peptide Peptidohydrolase
- Peptidohydrolase Inhibitors, Peptide
- Protease Antagonists
- Antagonists, Protease
- Antiproteases
- Peptidase Inhibitors
- Inhibitors, Peptidase
|
Below are MeSH descriptors whose meaning is more general than "Protease Inhibitors".
Below are MeSH descriptors whose meaning is more specific than "Protease Inhibitors".
This graph shows the total number of publications written about "Protease Inhibitors" by people in this website by year, and whether "Protease Inhibitors" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
Year | Major Topic | Minor Topic | Total |
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1995 | 0 | 1 | 1 |
1996 | 1 | 0 | 1 |
1998 | 1 | 1 | 2 |
1999 | 2 | 0 | 2 |
2002 | 0 | 2 | 2 |
2003 | 1 | 1 | 2 |
2004 | 2 | 2 | 4 |
2005 | 1 | 0 | 1 |
2006 | 1 | 3 | 4 |
2007 | 0 | 2 | 2 |
2009 | 1 | 0 | 1 |
2010 | 0 | 4 | 4 |
2011 | 1 | 1 | 2 |
2012 | 2 | 0 | 2 |
2013 | 3 | 2 | 5 |
2014 | 2 | 0 | 2 |
2015 | 1 | 0 | 1 |
2016 | 1 | 0 | 1 |
2017 | 1 | 1 | 2 |
2019 | 2 | 0 | 2 |
2020 | 1 | 0 | 1 |
2021 | 4 | 2 | 6 |
2022 | 1 | 2 | 3 |
2023 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protease Inhibitors" by people in Profiles.
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Persistence of an Infectious Form of SARS-CoV-2 After Protease Inhibitor Treatment of Permissive Cells In Vitro. J Infect Dis. 2025 Feb 04; 231(1):e68-e76.
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Glycyrrhizic acid conjugates with amino acid methyl esters target the main protease, exhibiting antiviral activity against wild-type and nirmatrelvir-resistant SARS-CoV-2 variants. Antiviral Res. 2024 07; 227:105920.
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Transmissible SARS-CoV-2 variants with resistance to clinical protease inhibitors. Sci Adv. 2023 03 29; 9(13):eade8778.
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Global 5'-UTR RNA structure regulates translation of a SERPINA1 mRNA. Nucleic Acids Res. 2022 09 23; 50(17):9689-9704.
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Functional map of SARS-CoV-2 3CL protease reveals tolerant and immutable sites. Cell Host Microbe. 2022 10 12; 30(10):1354-1362.e6.
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Gain-of-Signal Assays for Probing Inhibition of SARS-CoV-2 Mpro/3CLpro in Living Cells. mBio. 2022 06 28; 13(3):e0078422.
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Development of optimized drug-like small molecule inhibitors of the SARS-CoV-2 3CL protease for treatment of COVID-19. Nat Commun. 2022 04 07; 13(1):1891.
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Biochemical Screening of Potent Zika Virus Protease Inhibitors. ChemMedChem. 2022 04 20; 17(8):e202100695.
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Tafenoquine and its derivatives as inhibitors for the severe acute respiratory syndrome coronavirus 2. J Biol Chem. 2022 03; 298(3):101658.
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Norovirus Protease Structure and Antivirals Development. Viruses. 2021 10 14; 13(10).