Efavirenz Stimulates HIV-1 Reverse Transcriptase RNase H Activity by a Mechanism Involving Increased Substrate Binding and Secondary Cleavage Activity

Lignende værker

• Reverse transcriptase backbone can alter the polymerization and RNase activities of non-nucleoside reverse transcriptase mutants K101E+G190S
  af: Wang, Jiong, et al.
  Udgivet: (2013)
• Nonnucleoside Reverse Transcriptase Inhibitor-Resistant HIV Is Stimulated by Efavirenz during Early Stages of Infection
  af: Wang, Jiong, et al.
  Udgivet: (2011)
• 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
  af: Wang, Jiong, et al.
  Udgivet: (2010)
• Unique progressive cleavage mechanism of HIV reverse transcriptase RNase H
  af: Wisniewski, Michele, et al.
  Udgivet: (2000)
• Determinants of the RNase H cleavage specificity of human immunodeficiency virus reverse transcriptase.
  af: DeStefano, J J, et al.
  Udgivet: (1993)