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- W1963997188 abstract "Molecular modeling studies of adefovir diphosphate with the wild type and the mutant HBV polymerase–DNA complex demonstrated that the increase in adefovir sensitivity toward HBV polymerase mutants (rtL180M, rtM204V/I, rtL180M-M204V/I) is a result of increased van der Waals interaction and is supplemented by the decreased affinity of natural substrate toward the mutant HBV polymerase. In the case of rtN236T mutant, loss of two hydrogen bonds accompanied by significant decrease in electrostatic interactions is observed, which explains the observed decrease in drug sensitivity and binding affinity of adefovir diphosphate toward the rtN236T mutant HBV polymerase." @default.
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- W1963997188 title "Molecular mechanisms of adefovir sensitivity and resistance in HBV polymerase mutants: a molecular dynamics study" @default.
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- W1963997188 doi "https://doi.org/10.1016/j.bmcl.2004.05.075" @default.
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