Exonuclease removal of dideoxycytidine (zalcitabine) by the human mitochondrial DNA polymerase.

@article{Hanes2008ExonucleaseRO,
  title={Exonuclease removal of dideoxycytidine (zalcitabine) by the human mitochondrial DNA polymerase.},
  author={Jeremiah W Hanes and K A Johnson},
  journal={Antimicrobial agents and chemotherapy},
  year={2008},
  volume={52 1},
  pages={253-8}
}
The toxicity of nucleoside analogs used for the treatment of human immunodeficiency virus infection is due primarily to the inhibition of replication of the mitochondrial genome by the human mitochondrial DNA polymerase (Pol gamma). The severity of clinically observed toxicity correlates with the kinetics of incorporation versus excision of each analog as quantified by a toxicity index, spanning over six orders of magnitude. Here we show that the rate of excision of dideoxycytidine (zalcitabine… CONTINUE READING

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The analogs ddC , stavudine , and ddATP ( a metabolite of didanosine ) each bind more tightly at the polymerase site during incorporation than normal nucleotides , and this tight binding contributes to slower excision by the proofreading exonuclease , leading to increased toxicity toward mitochondrial DNA .
The analogs ddC , stavudine , and ddATP ( a metabolite of didanosine ) each bind more tightly at the polymerase site during incorporation than normal nucleotides , and this tight binding contributes to slower excision by the proofreading exonuclease , leading to increased toxicity toward mitochondrial DNA .
The analogs ddC , stavudine , and ddATP ( a metabolite of didanosine ) each bind more tightly at the polymerase site during incorporation than normal nucleotides , and this tight binding contributes to slower excision by the proofreading exonuclease , leading to increased toxicity toward mitochondrial DNA .
The analogs ddC , stavudine , and ddATP ( a metabolite of didanosine ) each bind more tightly at the polymerase site during incorporation than normal nucleotides , and this tight binding contributes to slower excision by the proofreading exonuclease , leading to increased toxicity toward mitochondrial DNA .
The analogs ddC , stavudine , and ddATP ( a metabolite of didanosine ) each bind more tightly at the polymerase site during incorporation than normal nucleotides , and this tight binding contributes to slower excision by the proofreading exonuclease , leading to increased toxicity toward mitochondrial DNA .
The analogs ddC , stavudine , and ddATP ( a metabolite of didanosine ) each bind more tightly at the polymerase site during incorporation than normal nucleotides , and this tight binding contributes to slower excision by the proofreading exonuclease , leading to increased toxicity toward mitochondrial DNA .
The toxicity of nucleoside analogs used for the treatment of human immunodeficiency virus infection is due primarily to the inhibition of replication of the mitochondrial genome by the human mitochondrial DNA polymerase ( Pol gamma ) .
The toxicity of nucleoside analogs used for the treatment of human immunodeficiency virus infection is due primarily to the inhibition of replication of the mitochondrial genome by the human mitochondrial DNA polymerase ( Pol gamma ) .
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