Discussion: G48V is associated with V82A in saquinavir resistance and this pair occurs as a mutational cluster together with nonactive-site mutant C95F, which emphasizes the importance of coevolution of mutations at 48 and 82 in drug resistance.
Insights into the mechanism of drug resistance: X-ray structure analysis of G48V/C95F tethered HIV-1 protease dimer/saquinavir complex.
PMID: 20471372
2010
Biochemical and biophysical research communications
Abstract: Recently, G48V mutation is found to co-exist with the mutation C95F in AIDS patients treated with saquinavir.
Abstract: The present structure also provides a rationale for the clinical observation that the resistance mutations C95F/G48V/V82A occur as a cluster in AIDS patients.
Abstract: We report here the three-dimensional crystal structure of G48V/C95F tethered HIV-1 protease/saquinavir complex.
HIV-1 subtype B protease and reverse transcriptase amino acid covariation.
Novel human immunodeficiency virus type 1 protease mutations potentially involved in resistance to protease inhibitors.
PMID: 15855527
2005
Antimicrobial agents and chemotherapy
Abstract: On the other hand, C95F, which was associated with treatment with saquinavir and indinavir, was highly expressed in clusters with either L90M and I93L or V82A and G48V.
1.8A X-ray structure of C95M/C1095F double mutant of tethered HIV-1 protease dimer complexed with acetyl pepstatin.
PMID: 15451428
2004
Biochemical and biophysical research communications
Abstract: In some of the virus isolates from patients undergoing heavy treatment with anti-HIV protease drugs, C95F mutation has appeared.
Abstract: These alterations may be relevant to C95F mutation conferring drug resistance to HIV-1 protease.
HIV mutation literature information.
PMID: 
2019
ACS omega
Browser Board
Co-occurred Entities
Filtrator
ViMRT