The 2.0Å Crystal Structure and Substrate Specificity of the KDEL-tailed Cysteine Endopeptidase Functioning in Programmed Cell Death of Ricinus communis Endosperm

This publication has 32 references indexed in Scilit:

• Proteolytic degradation of cereal prolamins—the problem with proline
  Plant Science, 2001
• The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum
  Proceedings of the National Academy of Sciences, 2001
• Ricinosomes: an organelle for developmentally regulated programmed cell death in senescing plant tissues.
  The Science of Nature, 2001
• Mass Transport of Proform of a Kdel-Tailed Cysteine Proteinase (Sh-EP) to Protein Storage Vacuoles by Endoplasmic Reticulum–Derived Vesicle Is Involved in Protein Mobilization in Germinating Seeds
  The Journal of cell biology, 2000
• Prediction of Protein Cleavage Sites by the Barley Cysteine Endoproteases EP-A and EP-B Based on the Kinetics of Synthetic Peptide Hydrolysis
  Plant Physiology, 2000
• Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes
  Proceedings of the National Academy of Sciences, 1999
• The 2.1 Å Structure of a Cysteine Protease with Proline Specificity from Ginger Rhizome,Zingiberofficinale^,
  Biochemistry, 1999
• A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment
  Planta, 1998
• Fluorescent properties of amino acids labeled withortho-aminobenzoic acid
  Biospectroscopy, 1998
• Programmed senescence of plant organs
  Cell Death & Differentiation, 1997