Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir

Journal of Computer-Aided Molecular Design

Volumn 26, Issue 2, 2012, Pages 215-232

  Kar, Parimal ^a   Knecht, Volker ^a  

^a MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

Author keywords

Amprenavir; Drug resistance; HIV 1 PR; MM PBSA; Normal mode analysis

Indexed keywords

DRUG INTERACTIONS; DRUG THERAPY; FREE ENERGY; PROTONATION; SOLVATION; VAN DER WAALS FORCES;

AMPRENAVIR; BINDING AFFINITIES; DRUG-RESISTANCE; HIGH AFFINITY; HIV-1 PROTEASE; HIV-1 PROTEASE INHIBITORS; MM-PBSA; NORMAL MODE ANALYSIS; PROTONATION STATE; WILD TYPES;

BINDING ENERGY;

AMPRENAVIR; ASPARAGINE; ATAZANAVIR; DARUNAVIR; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; INDINAVIR; LOPINAVIR; NELFINAVIR; RITONAVIR; SAQUINAVIR; TIPRANAVIR;

ARTICLE; BINDING AFFINITY; CATALYSIS; DECOMPOSITION; DIMERIZATION; DRUG STRUCTURE; ENERGY TRANSFER; ENTROPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; HYDROPHOBICITY; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTON TRANSPORT; SOLVATION; STATIC ELECTRICITY; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 84861672533     PISSN: 0920654X     EISSN: 15734951     Source Type: Journal    
DOI: 10.1007/s10822-012-9550-5     Document Type: Article

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