A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance

Medicine & Life Sciences

• Human immunodeficiency virus 1 p16 protease 100%
• Drug Resistance 61%
• Peptide Hydrolases 40%
• Mutation 37%
• Catalytic Domain 32%
• HIV-1 10%
• Nelfinavir 9%
• Saquinavir 8%
• HIV Protease Inhibitors 8%
• Indinavir 8%
• Mutation Accumulation 8%
• Ritonavir 7%
• Differential Scanning Calorimetry 7%
• Thermodynamics 7%
• Protease Inhibitors 6%
• Drug Interactions 5%
• HIV Infections 5%
• Binding Sites 4%
• Kinetics 4%
• Drug Therapy 3%

Chemical Compounds

• Mutation 56%
• Protease Inhibitor 13%
• Nelfinavir 9%
• Saquinavir 9%
• Indinavir 9%
• Ritonavir 8%
• Resistance 7%
• Molecule 5%
• Kd 4%
• Differential Scanning Calorimetry 4%
• Binding Site 3%
• Thermodynamics 3%