Characterization of dynorphin A-converting enzyme in human spinal cord. An endoprotease related to a distinct conversion pathway for the opioid heptadecapeptide?

This publication has 23 references indexed in Scilit:

• Dynorphin converting enzyme in the rat spinal cord. decreased activities during acute phase of adjuvant induced arthritis
  Life Sciences, 1992
• Consensus sequence for processing of peptide precursors at monobasic sites
  FEBS Letters, 1991
• Fast atom bombardment mass spectrometric analysis of arginine-containing neuropeptides
  Journal of Mass Spectrometry, 1990
• Highly efficient proteinase assay with chromogenic substrates and its application in a study of enzyme inhibitors
  Analytica Chimica Acta, 1990
• Application of high performance liquid chromatography combined with diode‐array detection for analysis of proteins and peptides in human cerebrospinal fluid
  Biomedical Chromatography, 1989
• Characterization of Cysteine Proteases Functioning in Degradation of Dynorphin in Neuroblastoma Cells: Evidence for the Presence of a Novel Enzyme with Strict Specificity Toward Paired Basic Residues
  Journal of Neurochemistry, 1989
• Role of peptide substrate structure in the selective processing of peptide prohormones at basic amino acid pairs by endoproteases
  FEBS Letters, 1988
• Synaptosomal Membrane‐Bound Form of Endopeptidase‐24.15 Generates Leu‐Enkephalin from Dynorphin _1‐8, α‐ and β‐Neoendorphin, and Met‐Enkephalin from Met‐Enkephalin‐Arg⁶‐Gly⁷‐Leu
  Journal of Neurochemistry, 1987
• Endopeptidase in human cerebrospinal fluid which cleaves proenkephalin B opioid peptides at consecutive basic amino acids
  Biochemical and Biophysical Research Communications, 1985
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976