Secreted alpha amidating enzymes are generated by specific posttranslational processing of precursors containing transmembrane domains

This publication has 28 references indexed in Scilit:

• Cloning of cDNA encoding a new peptide C-terminal α-amidating enzyme having a putative membrane-spanning domain from Xenopuslaevis skin
  Biochemical and Biophysical Research Communications, 1988
• Purification of a peptidylglycine α-amidating enzyme from transplantable rat medullary thyroid carcinomas
  Archives of Biochemistry and Biophysics, 1988
• Structure of the Precursor to an Enzyme Mediating COOH-Terminal Amidation in Peptide Biosynthesis
  Molecular Endocrinology, 1987
• Cloning and sequence of cDNA encoding a peptide C-terminal α-amidating enzyme from Xenopuslaevis
  Biochemical and Biophysical Research Communications, 1987
• Alteration of the cytoplasmic domain of the membrane-spanning glycoprotein p62 of Semliki Forest virus does not affect its polar distribution in established lines of Madin-Darby canine kidney cells.
  The Journal of cell biology, 1986
• NEUROPEPTIDES: MULTIPLE MOLECULAR FORMS, METABOLIC PATHWAYS, AND RECEPTORS
  Annual Review of Biochemistry, 1986
• Purification and Characterization of a Peptidyl Glycine Monooxygenase from Porcine Pituitary*
  Endocrinology, 1986
• Peptide C-terminal α-amidating enzyme purified to homogeneity from Xenopuslaevis skin
  Biochemical and Biophysical Research Communications, 1986
• POLYPROTEIN GENE EXPRESSION: Generation of Diversity of Neuroendocrine Peptides
  Annual Review of Biochemistry, 1984
• Mechanism of C-terminal amide formation by pituitary enzymes
  Nature, 1982