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Gadi Borkow

Researcher at Jewish General Hospital

Publications -  24
Citations -  1512

Gadi Borkow is an academic researcher from Jewish General Hospital. The author has contributed to research in topics: Reverse transcriptase & DNA polymerase. The author has an hindex of 14, co-authored 24 publications receiving 1480 citations. Previous affiliations of Gadi Borkow include McGill University.

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Phenotypic mechanism of HIV-1 resistance to 3'-azido-3'-deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase.

TL;DR: It is proposed that HIV-1 resistance to AZT results from the selectively decreased binding of AZTTP and the increased pyroph phosphorolytic cleavage of chain-terminated viral DNA by the mutant RT at physiological pyrophosphate levels, resulting in a net decrease in chain termination.
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Enhanced fidelity of 3TC-selected mutant HIV-1 reverse transcriptase.

TL;DR: Despite resulting drug resistance, treatment for more than 48 weeks is associated with a lower plasma viral burden than that at baseline, and there was an increase in fidelity of nucleotide insertion by the M184V mutant compared with wild-type enzyme.
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Chemical barriers to human immunodeficiency virus type 1 (HIV-1) infection: retrovirucidal activity of UC781, a thiocarboxanilide nonnucleoside inhibitor of HIV-1 reverse transcriptase.

TL;DR: Preincubation of uninfected MT2 cells with UC781 rendered these cells refractory to subsequent HIV infection in the absence of extracellular drug, an effect that persisted for several days following removal of exogenous drug.
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Inhibition of the ribonuclease h and dna polymerase activities of hiv-1 reverse transcriptase by n-(4-tert-butylbenzoyl)-2-hydroxy- 1 -naphthaldehyde hydrazone

TL;DR: It is concluded that N-(4-tert-Butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone may bind to two sites on HIV-1 RT, one of which may be the polymerase non-nucleoside inhibitor binding site and the second may be located in the RNase H domain.