Multiple tachykinins are produced and secreted upon post-translational processing of the three substance P precursor proteins, α-, β-, and γ-preprotachykinin

This publication has 45 references indexed in Scilit:

• Heterogeneity of tachykinin-like immunoreactive peptides in rat spinal cord and dorsal root ganglia
  Peptides, 1989
• Multiple neuropeptides derived from a common precursor are differentially packaged and transported
  Cell, 1988
• Pharmacological receptors for substance P and neurokinins
  Life Sciences, 1987
• Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sites
  FEBS Letters, 1986
• The processing of peptide precursors
  FEBS Letters, 1986
• Neuropeptide K: Isolation, structure and biological activities of a novel brain tachykinin
  Biochemical and Biophysical Research Communications, 1985
• Tissue-specific generation of two preprotachykinin mRNAs from one gene by alternative RNA splicing
  Nature, 1984
• An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N‐terminal arginine from β‐lipotropin_60–65
  FEBS Letters, 1984
• The development and application of a novel N-terminal directed substance P antiserum
  Life Sciences, 1980
• Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
  Journal of Molecular Biology, 1978