2000
Mechanism of Inhibition of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase by d4TTP: an Equivalent Incorporation Efficiency Relative to the Natural Substrate dTTP
Vaccaro J, Parnell K, Terezakis S, Anderson K. Mechanism of Inhibition of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase by d4TTP: an Equivalent Incorporation Efficiency Relative to the Natural Substrate dTTP. Antimicrobial Agents And Chemotherapy 2000, 44: 217-221. PMID: 10602755, PMCID: PMC89660, DOI: 10.1128/aac.44.1.217-221.2000.Peer-Reviewed Original ResearchConceptsHIV-1HIV-1 RTHuman immunodeficiency virus type 1Immunodeficiency virus type 1Target human immunodeficiency virus type 1Inhibition of HIV-1 RTNatural substrateVirus type 1Pre-steady-state kinetic analysisNucleoside analogue inhibitorsDNA synthesisRNA-dependent DNA synthesisAIDS patientsPrimer-template complexHuman immunodeficiency virus type 1 reverse transcriptaseNucleoside triphosphate analoguesType 1Mechanism of inhibitionD4TTPIncorporation efficiencyDTTPDNATriphosphate analoguesAnalogue inhibitorsInhibition
1999
Mechanistic studies show that (−)‐FTC‐TP is a better inhibitor of HIV‐1 reverse transcriptase than 3TC‐TP
Feng J, Shi J, Schinazi R, Anderson K. Mechanistic studies show that (−)‐FTC‐TP is a better inhibitor of HIV‐1 reverse transcriptase than 3TC‐TP. The FASEB Journal 1999, 13: 1511-1517. PMID: 10463941, DOI: 10.1096/fasebj.13.12.1511.Peer-Reviewed Original ResearchConceptsHIV-1 reverse transcriptaseFTC-TPClinical trialsReverse transcriptaseOngoing clinical trialsTreatment of AIDSAntiretroviral activityClinical potencyViral replicationBeta 2Triphosphate formNucleoside inhibitorsDifferential potencyRNA-dependent DNA synthesisEnhanced potencyTrialsPotencyMolecular mechanismsMechanistic studiesDNA synthesisInhibitorsTranscriptaseFTC