Unique progressive cleavage mechanism of HIV reverse transcriptase RNase H

Míreanna Comhchosúla

• Determinants of the RNase H cleavage specificity of human immunodeficiency virus reverse transcriptase.
  le: DeStefano, J J, et al.
  Foilsithe: (1993)
• Mutants of Human Immunodeficiency Virus Type 1 (HIV-1) Reverse Transcriptase Resistant to Nonnucleoside Reverse Transcriptase Inhibitors Demonstrate Altered Rates of RNase H Cleavage That Correlate with HIV-1 Replication Fitness in Cell Culture
  le: Archer, Richard H., et al.
  Foilsithe: (2000)
• Efavirenz Stimulates HIV-1 Reverse Transcriptase RNase H Activity by a Mechanism Involving Increased Substrate Binding and Secondary Cleavage Activity
  le: Muchiri, John M, et al.
  Foilsithe: (2013)
• Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo
  le: Julias, John G., et al.
  Foilsithe: (2002)
• Reduced Fitness in Cell Culture of HIV-1 with Nonnucleoside Reverse Transcriptase Inhibitor-Resistant Mutations Correlates with Relative Levels of Reverse Transcriptase Content and RNase H Activity in Virions
  le: Wang, Jiong, et al.
  Foilsithe: (2010)