Abstract: Certain reverse transcriptase mutations such as M184V/I, K70R, V108I, and protease mutations such as L33FIV, M84V, and M36I were associated with reduced viral load.
Patterns of point mutations associated with antiretroviral drug treatment failure in CRF01_AE (subtype E) infection differ from subtype B infection.
PMID: 12843744
2003
Journal of acquired immune deficiency syndromes (1999)
Abstract: The mutations T69N and V75M in reverse transcriptase and L10F, K20I, L33I, and N88S in protease were seen more frequently in patients infected with CRF01_AE than in patients with subtype B.
Comparative study of some energetic and steric parameters of the wild type and mutants HIV-1 protease: a way to explain the viral resistance.
PMID: 12169210
2002
Journal of cellular and molecular medicine
Abstract: Because, in vivo, the HIV-1 PR ( HIV-1 protease) present a high mutation rate we performed a comparative study of the energetic behaviors of the wild type HIV-1 PR and four type of mutants: Val82/Asn; Val82/Asp; Gln7/Lys, Leu33/Ile, Leu63/Ile; Ala71/Thr, Val82/Ala.
Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH.
Abstract: An autolysis-resistant mutant, Q7K/L33I/L63I, was used to facilitate sedimentation equilibrium studies at neutral pH where the wild-type enzyme is typically unstable in the absence of bound inhibitor.
Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration.
PMID: 8621402
1996
The Journal of biological chemistry
Abstract: The structural basis of this effect has been explored by several independent methods by using both the wild-type enzyme and its triple mutant (Q7K/L33I/L63I) (Mildner, A.
The HIV-1 protease as enzyme and substrate: mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties.
Abstract: Q7K/L33I/L63I should find useful application as a stable surrogate of the HIV-1 protease.
Abstract: However, one of the mutant proteases, Q7K/L33I/L63I, was highly resistant to autolysis, while retaining the physical properties, specificity, and susceptibility to inhibition of the wild-type enzyme.
HIV mutation literature information.
PMID: 
2006
Journal of medical virology
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