2012
Resource Use, Costs, and Utility Estimates for Patients with Cystic Fibrosis with Mild Impairment in Lung Function: Analysis of Data Collected Alongside a 48-Week Multicenter Clinical Trial
DeWitt EM, Grussemeyer CA, Friedman JY, Dinan MA, Lin L, Schulman KA, Reed SD. Resource Use, Costs, and Utility Estimates for Patients with Cystic Fibrosis with Mild Impairment in Lung Function: Analysis of Data Collected Alongside a 48-Week Multicenter Clinical Trial. Value In Health 2012, 15: 277-283. PMID: 22433759, DOI: 10.1016/j.jval.2011.11.027.Peer-Reviewed Original ResearchConceptsLung functionMild impairmentCystic fibrosisClinical trialsAeruginosa colonizationHealth Utilities Index Mark 2/3Study case report formsPrimary end pointNationwide Inpatient SampleDirect medical costsMulticenter clinical trialP. aeruginosa colonizationPseudomonas aeruginosa colonizationMean annual costCase report formsLong-term useUtility estimatesEmergency visitsHospital admissionDornase alfaMedication costsRandomized trialsMean ageFemale sexInpatient Sample
2005
Base Selectivity Is Impaired by Mutants that Perturb Hydrogen Bonding Networks in the RB69 DNA Polymerase Active Site †
Yang G, Wang J, Konigsberg W. Base Selectivity Is Impaired by Mutants that Perturb Hydrogen Bonding Networks in the RB69 DNA Polymerase Active Site †. Biochemistry 2005, 44: 3338-3346. PMID: 15736944, DOI: 10.1021/bi047921x.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBase Pair MismatchBinding SitesDeoxyadenine NucleotidesDeoxycytosine NucleotidesDeoxyguanine NucleotidesDNA-Directed DNA PolymeraseEnterobacterHydrogen BondingKineticsNucleotidesPhenylalanineSubstrate SpecificityThymine NucleotidesTolueneTyrosineViral ProteinsConceptsRB69 polRapid chemical quenchHydrogen bonding networkSet of mutantsStopped-flow fluorescencePutative conformational changesPhosphoryl transfer reactionsPolymerase active siteRB69 DNA polymeraseDNA polymerase active siteChemical quenchMolecular basisBonding networkNoncomplementary dNTPsMutantsTransfer reactionsExo enzymesState kinetic parametersConformational changesMismatched basesActive siteExo formCrystal structureDNA polymeraseNucleoside triphosphates
2004
Relationship between Antiviral Activity and Host Toxicity: Comparison of the Incorporation Efficiencies of 2′,3′-Dideoxy-5-Fluoro-3′-Thiacytidine-Triphosphate Analogs by Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Human Mitochondrial DNA Polymerase
Feng J, Murakami E, Zorca S, Johnson A, Johnson K, Schinazi R, Furman P, Anderson K. Relationship between Antiviral Activity and Host Toxicity: Comparison of the Incorporation Efficiencies of 2′,3′-Dideoxy-5-Fluoro-3′-Thiacytidine-Triphosphate Analogs by Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Human Mitochondrial DNA Polymerase. Antimicrobial Agents And Chemotherapy 2004, 48: 1300-1306. PMID: 15047533, PMCID: PMC375312, DOI: 10.1128/aac.48.4.1300-1306.2004.Peer-Reviewed Original ResearchConceptsHuman mitochondrial DNA polymeraseMitochondrial DNA polymeraseDNA-DNAPolymerase gammaHuman immunodeficiency virusDNA polymerasePrimer-templateHuman mitochondrial DNA polymerase gammaPre-steady-state kinetic analysisMitochondrial DNA polymerase gammaDNA polymerase gammaMolecular mechanism of inhibitionHIV-1Treatment of human immunodeficiency virusExonuclease activityDNA-RNAReverse transcriptaseFood and Drug AdministrationClinical trial studyMolecular mechanismsMechanism of inhibitionHuman immunodeficiency virus type 1 reverse transcriptaseEnzymatic assayImmunodeficiency virusPolymerase
2001
Insights into the Molecular Mechanism of Mitochondrial Toxicity by AIDS Drugs*
Feng J, Johnson A, Johnson K, Anderson K. Insights into the Molecular Mechanism of Mitochondrial Toxicity by AIDS Drugs*. Journal Of Biological Chemistry 2001, 276: 23832-23837. PMID: 11328813, DOI: 10.1074/jbc.m101156200.Peer-Reviewed Original ResearchMeSH KeywordsAcquired Immunodeficiency SyndromeAnti-HIV AgentsCytidine TriphosphateDeoxycytosine NucleotidesDideoxynucleotidesDNADNA Polymerase gammaDNA ReplicationDNA-Directed DNA PolymeraseDNA, MitochondrialExodeoxyribonucleasesHumansKineticsLamivudineMitochondriaNucleic Acid Synthesis InhibitorsReverse Transcriptase InhibitorsZalcitabineConceptsPol gammaHuman mitochondrial DNA polymeraseHuman pol gammaMitochondrial DNA replicationMitochondrial DNA polymeraseToxicity of nucleoside analogsCytosine analogsMechanism of mitochondrial toxicityExonuclease activityDNA primersDNA replicationDNA polymeraseNucleoside analogsRate of excisionStructure/function relationshipsMolecular mechanismsLong-term administrationToxic inhibitorsExonucleaseTreatment of AIDSPolymeraseClinical toxicityMitochondrial toxicityDNAPol
1999
Initiation of Minus-Strand DNA Synthesis by Human Immunodeficiency Virus Type 1 Reverse Transcriptase †
Vaccaro J, Singh H, Anderson K. Initiation of Minus-Strand DNA Synthesis by Human Immunodeficiency Virus Type 1 Reverse Transcriptase †. Biochemistry 1999, 38: 15978-15985. PMID: 10625465, DOI: 10.1021/bi990945x.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesDeoxycytosine NucleotidesDNA, ViralHIV Reverse TranscriptaseHumansKineticsRNARNA, ViralSubstrate SpecificityTemplates, GeneticConceptsHIV-1 reverse transcriptaseDNA/DNA substratesReverse transcriptaseHuman immunodeficiency virus type 1 reverse transcriptaseType 1 reverse transcriptasePrimer-template substrateDNA synthesisMinus-strand DNA synthesisConcentrations of dCTPDNA/RNADeoxynucleotide incorporationMolecular mechanismsTranscriptaseSteady-state releaseInitiationHigh affinityRNAReleaseStrand DNA synthesisMechanistic Studies Examining the Efficiency and Fidelity of DNA Synthesis by the 3TC-Resistant Mutant (184V) of HIV-1 Reverse Transcriptase †
Feng J, Anderson K. Mechanistic Studies Examining the Efficiency and Fidelity of DNA Synthesis by the 3TC-Resistant Mutant (184V) of HIV-1 Reverse Transcriptase †. Biochemistry 1999, 38: 9440-9448. PMID: 10413520, DOI: 10.1021/bi990709m.Peer-Reviewed Original ResearchConceptsHIV-1 reverse transcriptaseM184V RTHIV-1 virusWild-type HIV-1 reverse transcriptaseReverse transcriptaseDNA-dependent DNA polymerizationStrong antiviral effectRNA-dependent DNA polymerizationCombination therapyAntiviral effectMethionine 184Mutant reverse transcriptaseMutant HIV-1 reverse transcriptaseRT fidelityCorresponding DNA templateSingle amino acid substitutionMolecular mechanismsAmino acid substitutionsVirusDNA synthesisTranscriptaseAcid substitutionsHigh levelsClinicTherapy
1998
Mechanistic Studies Comparing the Incorporation of (+) and (−) Isomers of 3TCTP by HIV-1 Reverse Transcriptase †
Feng J, Anderson K. Mechanistic Studies Comparing the Incorporation of (+) and (−) Isomers of 3TCTP by HIV-1 Reverse Transcriptase †. Biochemistry 1998, 38: 55-63. PMID: 9890882, DOI: 10.1021/bi982340r.Peer-Reviewed Original Research
1997
RNA Dependent DNA Replication Fidelity of HIV-1 Reverse Transcriptase: Evidence of Discrimination between DNA and RNA Substrates †
Kerr S, Anderson K. RNA Dependent DNA Replication Fidelity of HIV-1 Reverse Transcriptase: Evidence of Discrimination between DNA and RNA Substrates †. Biochemistry 1997, 36: 14056-14063. PMID: 9369477, DOI: 10.1021/bi971385+.Peer-Reviewed Original Research
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply