Heterologous Expression, Purification, Refolding, and Structural-Functional Characterization of EP-B2, a Self-Activating Barley Cysteine Endoprotease

This publication has 48 references indexed in Scilit:

• Fermentation, purification, formulation, and pharmacological evaluation of a prolyl endopeptidase from Myxococcus xanthus: Implications for Celiac Sprue therapy
  Biotechnology & Bioengineering, 2005
• Prolyl Endopeptidase-Mediated Destruction of T Cell Epitopes in Whole Gluten: Chemical and Immunological Characterization
  The Journal of Pharmacology and Experimental Therapeutics, 2005
• Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue
  Biochemical Journal, 2004
• The 2.0Å Crystal Structure and Substrate Specificity of the KDEL-tailed Cysteine Endopeptidase Functioning in Programmed Cell Death of Ricinus communis Endosperm
  Journal of Molecular Biology, 2004
• Structural Basis for Gluten Intolerance in Celiac Sprue
  Science, 2002
• Maturation of barley cysteine endopeptidase expressed inTrichoderma reeseiis distorted by incomplete processing
  Canadian Journal of Microbiology, 2002
• Electrostatics of nanosystems: Application to microtubules and the ribosome
  Proceedings of the National Academy of Sciences, 2001
• Potency and Selectivity of the Cathepsin L Propeptide as an Inhibitor of Cysteine Proteases
  Biochemistry, 1996
• Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers.
  Plant Cell, 1990
• Gibberellic Acid-Induced Synthesis of Protease by Isolated Aleurone Layers of Barley
  Plant Physiology, 1967