Real time NMR monitoring of local unfolding of HIV-1 protease tethered dimer driven by autolysis.

This publication has 16 references indexed in Scilit:

• 1.9 x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR
  Proteins-Structure Function and Bioinformatics, 2001
• The HIV-1 Protease as Enzyme and Substrate: Mutagenesis of Autolysis Sites and Generation of a Stable Mutant with Retained Kinetic Properties
  Biochemistry, 1994
• Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor
  Nature Structural & Molecular Biology, 1994
• Secondary structure and signal assignments of human‐immunodeficiency‐virus‐1 protease complexed to a novel, structure‐based inhibitor
  European Journal of Biochemistry, 1994
• STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASE
  Annual Review of Biochemistry, 1993
• Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases
  Biochemistry, 1992
• Stability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer.
  Proceedings of the National Academy of Sciences, 1990
• The Structure and Function of the Aspartic Proteinases
  Annual Review of Biophysics, 1990
• Active human immunodeficiency virus protease is required for viral infectivity.
  Proceedings of the National Academy of Sciences, 1988
• Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
  Chemical Physics Letters, 1980