2015
Human PrimPol: A Novel Mechanism of Antiviral Toxicity
Mislak A, Anderson K. Human PrimPol: A Novel Mechanism of Antiviral Toxicity. The FASEB Journal 2015, 29 DOI: 10.1096/fasebj.29.1_supplement.710.23.Peer-Reviewed Original ResearchNucleoside reverse transcriptase inhibitorsAntiviral toxicityHIV-1HIV-1-infected patientsNRTI-associated mitochondrial toxicityDaily drug regimensHIV-1 infectionLife-long administrationReverse transcriptase inhibitorsReduced viral loadReverse transcriptasePrevent viral transmissionDrug regimensViral loadTranscriptase inhibitorsRelated morbidityInfected patientsSevere mitochondrial dysfunctionSide effectsPatient adherenceViral replicationMechanisms of toxicityMitochondrial toxicityViral transmissionPatients
2014
Recent Findings on the Mechanisms Involved in Tenofovir Resistance
Iyidogan P, Anderson K. Recent Findings on the Mechanisms Involved in Tenofovir Resistance. Antiviral Chemistry And Chemotherapy 2014, 23: 217-222. PMID: 23744599, PMCID: PMC4077986, DOI: 10.3851/imp2628.Peer-Reviewed Original ResearchConceptsReverse transcriptase inhibitorsDrug resistanceResistance mechanismsNon-nucleoside reverse transcriptase inhibitorsHIV-1 infectionLong-term efficacyMechanism of RTSynergistic antiviral effectTenofovir resistanceAntiretroviral agentsCombination therapyTreatment failureAntiviral synergySafety profileTranscriptase inhibitorsHIV-1TenofovirClinical useAntiviral effectTherapyViral sequencesNucleotide analoguesRegimensEfavirenz
2012
Balancing Antiviral Potency and Host Toxicity: Identifying a Nucleotide Inhibitor with an Optimal Kinetic Phenotype for HIV-1 Reverse Transcriptase
Sohl C, Kasiviswanathan R, Kim J, Pradere U, Schinazi R, Copeland W, Mitsuya H, Baba M, Anderson K. Balancing Antiviral Potency and Host Toxicity: Identifying a Nucleotide Inhibitor with an Optimal Kinetic Phenotype for HIV-1 Reverse Transcriptase. Molecular Pharmacology 2012, 82: 125-133. PMID: 22513406, PMCID: PMC3382833, DOI: 10.1124/mol.112.078758.Peer-Reviewed Original ResearchConceptsNucleoside reverse transcriptase inhibitorsHost toxicityClinical trialsReverse transcriptaseTreatment of HIV infectionMinimal host toxicityUnique toxicity profilePhase II clinical trialReverse transcriptase inhibitorsII clinical trialsHIV-1 reverse transcriptaseWild-typeAntiretroviral efficacyHIV infectionToxicity profileTranscriptase inhibitorsHIV-1Molecular mechanismsTreat HIVMechanisms of toxicityMitochondrial toxicityMolecular mechanisms of toxicityAntiviral potencyViral target proteinsThymidine analog
2006
Developing novel nonnucleoside HIV-1 reverse transcriptase inhibitors: beyond the butterfly.
Basavapathruni A, Anderson K. Developing novel nonnucleoside HIV-1 reverse transcriptase inhibitors: beyond the butterfly. Current Pharmaceutical Design 2006, 12: 1857-65. PMID: 16724952, DOI: 10.2174/138161206776873617.Peer-Reviewed Original ResearchConceptsNonnucleoside reverse transcriptase inhibitorsReverse transcriptase inhibitorsTranscriptase inhibitorsHuman immunodeficiency virus type 1 infectionResistance to nonnucleoside reverse transcriptase inhibitorsTreatment of human immunodeficiency virus type 1 infectionType 1 infectionFood and Drug AdministrationU.S. Food and Drug AdministrationCombination therapyDevelopment of resistanceMechanism of actionHIV-1 reverse transcriptase inhibitorsDrug AdministrationNonnucleosideNonnucleoside HIV-1 reverse transcriptase inhibitorNonnucleoside inhibitorsFeatures of inhibitionPotential new inhibitorsInhibitorsAmino acid substitutionsBiochemical featuresMolecular mechanismsNew inhibitorsAcid substitutions
2000
An analysis of the catalytic cycle of HIV-1 reverse transcriptase: opportunities for chemotherapeutic intervention based on enzyme inhibition.
Furman P, Painter G, Anderson K. An analysis of the catalytic cycle of HIV-1 reverse transcriptase: opportunities for chemotherapeutic intervention based on enzyme inhibition. Current Pharmaceutical Design 2000, 6: 547-67. PMID: 10788596, DOI: 10.2174/1381612003400777.Peer-Reviewed Original ResearchConceptsCatalytic cycleIntrinsic binding affinityHIV-1 reverse transcriptaseCatalytic complexChemical catalysisBinding affinityCatalysisMolecular forcesReverse transcriptase inhibitorsAllosteric siteClasses of approved drugsNon-nucleoside reverse transcriptase inhibitorsTranscriptase inhibitorsNucleoside reverse transcriptase inhibitorsSite of inhibitionEnzyme inhibitionReverse transcriptaseAlternative substratesEnzyme