3.4.23.16: HIV-1 retropepsin
This is an abbreviated version!
For detailed information about HIV-1 retropepsin, go to the full flat file.
Word Map on EC 3.4.23.16
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3.4.23.16
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antiretroviral
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ritonavir
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transcriptase
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saquinavir
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indinavir
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nelfinavir
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hiv-infected
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lopinavir
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polyproteins
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flap
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darunavir
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amprenavir
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drug-resistant
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anti-hiv
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atazanavir
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virological
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haart
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gag-pol
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peptidomimetic
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virion
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p-glycoprotein
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lipodystrophy
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non-nucleoside
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integrase
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cross-resistance
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isostere
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nonpeptidic
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zidovudine
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nevirapine
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virus-1
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tipranavir
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cyp3a4
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nnrti
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drug-drug
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treatment-experienced
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lamivudine
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didanosine
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ritonavir-boosted
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autoprocessing
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efavirenz
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protease-inhibitor
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stavudine
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treatment-naive
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analysis
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raltegravir
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zalcitabine
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plasmepsins
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antiretroviral-naive
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pi-based
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pharmacology
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drug development
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medicine
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hiv-rna
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lipoatrophy
- 3.4.23.16
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antiretroviral
- ritonavir
- transcriptase
- saquinavir
- indinavir
- nelfinavir
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hiv-infected
- lopinavir
- polyproteins
- flap
- darunavir
- amprenavir
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drug-resistant
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anti-hiv
- atazanavir
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virological
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haart
- gag-pol
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peptidomimetic
- virion
- p-glycoprotein
- lipodystrophy
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non-nucleoside
-
integrase
-
cross-resistance
- isostere
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nonpeptidic
- zidovudine
- nevirapine
- virus-1
- tipranavir
- cyp3a4
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nnrti
-
drug-drug
-
treatment-experienced
- lamivudine
- didanosine
-
ritonavir-boosted
-
autoprocessing
- efavirenz
-
protease-inhibitor
- stavudine
-
treatment-naive
- analysis
- raltegravir
- zalcitabine
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plasmepsins
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antiretroviral-naive
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pi-based
- pharmacology
- drug development
- medicine
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hiv-rna
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lipoatrophy
Reaction
specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro =
Synonyms
CRF01_AE protease, Gag protease, HIV aspartyl protease, HIV PR, HIV protease, HIV-1 aspartyl protease, HIV-1 PR, HIV-1 protease, HIV-1 proteinase, HIV-1PR, HIV-2 protease, HIVPR, human immunodeficiency virus 1 protease, human immunodeficiency virus 1 retropepsin, human immunodeficiency virus protease, human immunodeficiency virus type 1 protease, human immunodeficiency virus type I protease, More, PR, PR1, PR2, retropepsin, retroproteinase
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analysis
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method for picomolar electrochemical detection of human immunodeficiency virus type-1 protease using ferrocene-pepstatin-modified surfaces studied by cyclic voltammetry and electrochemical impedance spectroscopy. Both gold nanoparticles and thiolated single walled carbon nanotubes/gold nanoparticles electrode materials show enhanced electrochemical responses to increasing concentrations of HIV-1 protease with shifting to higher potentials as well as decrease in the overall signal intensity. The sensing electrode modified with thiolated ingle walled carbon nanotubes/gold nanoparticles shows an estimated detection limit of 0.8 pM
drug development
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the enzyme is a target for drug development
medicine
pharmacology
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the enzyme is responsible for the processing of gag and gag-pol polyprotein precursors to produce structural proteins and enzymes for the mature virus. Hence it is essential for the maturation and infectivity of the virus and is thus a major target for the development of inhibitor drugs
medicine
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HIV-1 protease is the target of some of the most effective antiviral AIDS therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins
medicine
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drugs against protease and reverse transcriptase form the basis for Highly Active Anti-Retroviral Theraphy that has been successful in improving survival rates and quality of life for HIV infected individuals
medicine
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the enzyme is an attractive target for antiviral drugs of HIV-1
medicine
insertions at positions 33 and 35 contribute to the viral resistance to most of the tested protease inhibitors. The structural analysis reveals local structural rearrangements in the flap region and in the substrate binding pockets. The enlargement of the HIV proteinase substrate binding site together with impaired flap dynamics could account for the weaker inhibitor binding by the insertion mutants. Amino acid insertions in the vicinity of the binding cleft represent a mechanism of HIV resistance development
medicine
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construction of chimeric viruses using patient-derived gag-protease sequences amplified from plasma HIV RNA and inserted into an NL4-3 backbone. The chimeric viruses generated from elite controllers display lower replication capacity than viruses from chronic progressors. Human leukocyte antigen system allele HLA-B*57 is associated with lower replication capacity than other alleles in both elite controllers and chronic progressor groups. Chimeric viruses from allele B*57 elite controllers demonstrate lower replication capacity than viruses from allele B*57 chronic progressors. Cytotoxic T-lymphocyte selection pressure on gag-protease alters virus replication capacity, and HIV-specific cytotoxic T-lymphocytes inducing escape mutations with fitness costs in this region may be important for strict viremia control in elite controllers of HIV
medicine
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isolation of subtype G viruses from patients with diverse amino acid combinations at codons 71, 74, 89 and 90. In isolates displaying 89I/V in combination with A71 or T74, a reversal to subtype G wild-type 89M is observed after growth in the absence of protease inhibitor. The presence of 71T in one isolate and 74S in another allows the persistence of 89I. Mutation 90M confers intermediate but significant degrees of drug resistance to ritonavir and nelfinavir in subtype G viruses. The combination of 71T or 74S, 89I and 90M results in higher levels of resistance to those protease inhibitors. 71T or 74S may stabilize 89I in the protease of subtype G
medicine
the HIV proteases are effective therapeutic targets for treating HIV infection because of the essential role in hydrolysing the viral Gag and Gag-Pol precursor polyprotein during infectious viral particle maturation
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the enzyme is a target for drug development active on multidrug-resistant virus
pharmacology
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the enzyme is a target for specific inhibitor development
pharmacology
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mutations in the gag region NC-p1/TFP-p6/p6pol may influence the selection of darunavir resistance mutations. The I437T/V gag mutation that confers resistance to protease inhibitors reduces the selection of such mutations. Virus with L76V in protease or I437T/V in gag may be already resistant to darunavir
pharmacology
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use of suboptimal concentrations of inhibitors atazanavir and lopinavir. Even with high levels of inhibition of viral infectivity, IC90, most of the Gag and Gag-Pol polyproteins are processed, although slight but significant increases in processing intermediates of Gag Are detected. Drug treatments cause a significant increase in the proportion of viruses displaying either immature or aberrant mature morphologies. The aberrant mature particles are characterized by an electron-dense region at the viral periphery and an electron-lucent core structure in the viral center. Drug treatments cause only a slight decrease in overall thermodynamic stability of the viral RNA dimer