2018
APOBEC as an Endogenous Mutagen in Cancers of the Head and Neck
Sasaki T, Issaeva N, Yarbrough W, Anderson K. APOBEC as an Endogenous Mutagen in Cancers of the Head and Neck. Current Cancer Research 2018, 275-292. DOI: 10.1007/978-3-319-78762-6_10.Peer-Reviewed Original ResearchDiverse physiological processesFamily of cytidineApolipoprotein B mRNA-editing enzyme catalytic polypeptideEnzyme catalytic polypeptideU conversionBioinformatics studiesEndogenous mutagensAPOBEC3 functionGenomic DNAPhysiological processesCatalytic polypeptideEditing mechanismBioinformatics dataAPOBEC activityHuman cancersTarget nucleotidesProduction of neoantigensAPOBEC3 proteinsDiverse cancersSquamous cell carcinomaHuman papillomavirus expressionTherapeutic avenuesProteinStructural evidenceDNA
2010
102 Yeast homologues of disease mutations in DNA polymerase gamma cause mtDNA depletion and mutagenesis
Stumpf J, Spell D, Stillwagon M, Anderson K, Copeland W. 102 Yeast homologues of disease mutations in DNA polymerase gamma cause mtDNA depletion and mutagenesis. Mitochondrion 2010, 10: 228. DOI: 10.1016/j.mito.2009.12.094.Peer-Reviewed Original Research
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, MitochondrialDNA-Directed DNA PolymeraseExodeoxyribonucleasesHumansKineticsLamivudineMitochondriaNucleic 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
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