Functional and Structural Characterization of Synthetic HIV-1 Vpr That Transduces Cells, Localizes to the Nucleus, and Induces G2 Cell Cycle Arrest

This publication has 58 references indexed in Scilit:

• In Vivo Protein Transduction: Delivery of a Biologically Active Protein into the Mouse
  Science, 1999
• NMR structure of the (52–96) C-terminal domain of the HIV-1 regulatory protein vpr: molecular insights into its biological functions
  Journal of Molecular Biology, 1999
• Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration
  Nature Medicine, 1998
• Structure, biological functions and inhibition of the HIV-1 proteins V pr and NCp7
  Biochimie, 1997
• HIV-1, Vpr and the cell cycle
  Current Biology, 1996
• Interaction of Virion Protein Vpr of Human Immunodeficiency Virus Type 1 with Cellular Transcription Factor Sp1 and trans-Activation of Viral Long Terminal Repeat
  Journal of Biological Chemistry, 1995
• Solution structure of the hydrophilic region of HIV‐1 encoded virus protein U (Vpu) by CD and ^lH NMR spectroscopy
  International Journal of Peptide and Protein Research, 1995
• A synthetic protein corresponding to the entire vpr gene product from the human immunodeficiency virus HIV‐1 is recognized by antibodies from HIV‐infected patients
  International Journal of Peptide and Protein Research, 1990
• Cellular uptake of the tat protein from human immunodeficiency virus
  Cell, 1988
• Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
  Cell, 1988