 HIV Protease
"HIV Protease" 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.
Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus of the pol gene.
| Descriptor ID |
D016333
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| MeSH Number(s) |
D08.811.277.656.074.500.340 D08.811.277.656.300.048.340 D12.776.964.775.375.545.750
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| Concept/Terms |
HIV Protease- HIV Protease
- Protease, HIV
- p16 pol gene product, HIV
- p16 protease, HIV
- HIV p16 protease
- HIV Proteinase
- HTLV-III Protease
- HTLV III Protease
- Protease, HTLV-III
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Below are MeSH descriptors whose meaning is more general than "HIV Protease".
Below are MeSH descriptors whose meaning is more specific than "HIV Protease".
This graph shows the total number of publications written about "HIV Protease" by people in this website by year, and whether "HIV Protease" 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 |
|---|
| 1993 | 1 | 0 | 1 | | 2007 | 2 | 0 | 2 | | 2009 | 1 | 0 | 1 | | 2011 | 1 | 0 | 1 | | 2012 | 2 | 0 | 2 | | 2018 | 1 | 0 | 1 | | 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "HIV Protease" by people in Profiles.
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Jurczyszak D, Zhang W, Terry SN, Kehrer T, Bermúdez González MC, McGregor E, Mulder LCF, Eckwahl MJ, Pan T, Simon V. HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle. PLoS Pathog. 2020 02; 16(2):e1008305.
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Natesampillai S, Cummins NW, Nie Z, Sampath R, Baker JV, Henry K, Pinzone M, O'Doherty U, Polley EC, Bren GD, Katzmann DJ, Badley AD. HIV Protease-Generated Casp8p41, When Bound and Inactivated by Bcl2, Is Degraded by the Proteasome. J Virol. 2018 07 01; 92(13).
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Hall BA, Wright DW, Jha S, Coveney PV. Quantized water access to the HIV-1 protease active site as a proposed mechanism for cooperative mutations in drug affinity. Biochemistry. 2012 Aug 21; 51(33):6487-9.
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Torbeev VY, Kent SB. Ionization state of the catalytic dyad Asp25/25' in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis. Org Biomol Chem. 2012 Aug 14; 10(30):5887-91.
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Torbeev VY, Raghuraman H, Hamelberg D, Tonelli M, Westler WM, Perozo E, Kent SB. Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc Natl Acad Sci U S A. 2011 Dec 27; 108(52):20982-7.
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Torbeev VY, Raghuraman H, Mandal K, Senapati S, Perozo E, Kent SB. Dynamics of "flap" structures in three HIV-1 protease/inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopy. J Am Chem Soc. 2009 Jan 28; 131(3):884-5.
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Torbeev VY, Mandal K, Terechko VA, Kent SB. Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site. Bioorg Med Chem Lett. 2008 Aug 15; 18(16):4554-7.
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Johnson EC, Malito E, Shen Y, Rich D, Tang WJ, Kent SB. Modular total chemical synthesis of a human immunodeficiency virus type 1 protease. J Am Chem Soc. 2007 Sep 19; 129(37):11480-90.
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Johnson EC, Malito E, Shen Y, Pentelute B, Rich D, Florián J, Tang WJ, Kent SB. Insights from atomic-resolution X-ray structures of chemically synthesized HIV-1 protease in complex with inhibitors. J Mol Biol. 2007 Oct 26; 373(3):573-86.
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Becker Y. Computer simulations to predict the availability of peptides with known HLA class I motifs possibly generated by proteolysis of HIV-1 proteins in infected cells. Virus Genes. 1995; 10(3):227-37.
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