Subtle Alterations of the Native Zinc Finger Structures Have Dramatic Effects on the Nucleic Acid Chaperone Activity of Human Immunodeficiency Virus Type 1 Nucleocapsid Protein

Eitemau Tebyg

• Zinc Finger Structures in the Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Facilitate Efficient Minus- and Plus-Strand Transfer
  gan: Guo, Jianhui, et al.
  Cyhoeddwyd: (2000)
• Specific zinc-finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function
  gan: Williams, Mark C., et al.
  Cyhoeddwyd: (2002)
• Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription
  gan: Wu, Tiyun, et al.
  Cyhoeddwyd: (2014)
• Effects of nucleic acid local structure and magnesium ions on minus-strand transfer mediated by the nucleic acid chaperone activity of HIV-1 nucleocapsid protein
  gan: Wu, Tiyun, et al.
  Cyhoeddwyd: (2007)
• Fundamental differences between the nucleic acid chaperone activities of HIV-1 nucleocapsid protein and Gag or Gag-derived proteins: Biological implications
  gan: Wu, Tiyun, et al.
  Cyhoeddwyd: (2010)