Soluble Rous Sarcoma Virus Reverse Transcriptases α, αβ, and β Purified from Insect Cells Are Processive DNA Polymerases That Lack an RNase H 3′ → 5′ Directed Processing Activity

This publication has 51 references indexed in Scilit:

• Analysis of the Polymerization Kinetics of Homodimeric EIAV p51/51 Reverse Transcriptase Implies the Formation of a Polymerase Active Site Identical to Heterodimeric EIAV p66/51 Reverse Transcriptase
  Biochemistry, 1998
• Alterations to the Primer Grip of p66 HIV-1 Reverse Transcriptase and Their Consequences for Template-Primer Utilization
  Biochemistry, 1996
• Truncating α-Helix E′ of p66 Human Immunodeficiency Virus Reverse Transcriptase Modulates RNase H Function and Impairs DNA Strand Transfer
  Published by Elsevier ,1995
• Mechanism of DNA Strand Transfer Reactions Catalyzed by HIV-1 Reverse Transcriptase
  Science, 1992
• RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms
  FEBS Letters, 1992
• Interaction of HIV-1 ribonuclease H with polypurine tract containing RNA-DNA hybrids
  Biochemistry, 1990
• Simian immunodeficiency virus reverse transcriptase
  European Journal of Biochemistry, 1990
• Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAV
  Science, 1986
• Mechanism of release of the avian retrovirus tRNATrp primer molecule from viral DNA by ribonuclease H during reverse transcription
  Cell, 1982
• Purification of the DNA polymerase of avian myeloblastosis virus
  Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971