ViMRT
}  
 
Home   
< Docs   

 HIV mutation literature information.


  Resistance of HIV type 1 to proteinase inhibitor Ro 31-8959.
 PMID: 7576926       1995       AIDS research and human retroviruses
Abstract: The primary event (Gly-48 to valine) occurs at the hinge of the flaps of the proteinase, thus hampering entry of the inhibitor to the active center and suggesting steric hindrance.


  Analysis of resistance to human immunodeficiency virus type 1 protease inhibitors by using matched bacterial expression and proviral infection vectors.
 PMID: 7636988       1995       Journal of virology
Abstract: G48V, L90M, and G48V/L90M exhibited successively less processing in vitro than the wild-type enzyme, and the purified enzymes were 220-, 20-, and 720-fold, respectively, less sensitive to Ro 31-8959.
Abstract: The reduced enzyme sensitivity correlated directly with the sensitivities of the matched recombinant viruses, in that individual mutations L90M and G48V conferred 2-fold and 4- to 6-fold increases in 50% inhibitory concentration, respectively, whereas G48V/L90M was 8 to 10 times less sensitive to Ro 31-8959.
Abstract: The utility of this vector system was demonstrated by using protease variants glycine to valine at amino acid 48


  Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959.
 PMID: 7831807       1995       Virology
Abstract: Sequence comparison to wild-type (wt) proteinase demonstrated two amino acid substitutions in the resistant virus, a Gly to Val exchange at position 48 and a Leu to Met exchange at position 90.


  Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase.
 PMID: 7726006       1994       Acta virologica
Abstract: Substitution of glycine by valine at position 48 of the PR protein was found.



Browser Board

 Co-occurred Entities




   Filtrator