X-ray Structures of Human Neutrophil Collagenase Complexed with Peptide Hydroxamate and Peptide Thiol Inhibitors. Implications for Substrate Binding and Rational Drug Design

This publication has 38 references indexed in Scilit:

• Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor
  Nature Structural & Molecular Biology, 1994
• Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases
  FEBS Letters, 1994
• Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’
  FEBS Letters, 1993
• Fragmentation of human polymorphonuclear-leucocyte collagenase
  Biochemical Journal, 1993
• The Recombinant Catalytic Domain of Human Neutrophil Collagenase Lacks Type I Collagen Substrate Specificity
  Biochemical and Biophysical Research Communications, 1993
• The Matrix Metalloproteinases and Their Inhibitors
  American Journal of Respiratory Cell and Molecular Biology, 1992
• Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases
  Nature, 1992
• Accurate bond and angle parameters for X-ray protein structure refinement
  Acta Crystallographica Section A Foundations of Crystallography, 1991
• Metalloproteinases and their inhibitors in matrix remodeling
  Trends in Genetics, 1990
• Crystallographic refinement by simulated annealing: application to crambin
  Acta Crystallographica Section A Foundations of Crystallography, 1989