Proteolytic events in the post-translational processing of polypeptide hormone precursors
- 28 February 1987
- Vol. 69 (2) , 87-89
- https://doi.org/10.1016/0300-9084(87)90239-2
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sitesFEBS Letters, 1986
- An endopeptidase associated with bovine neurohypophysis secretory granules cleaves pro-ocytocin/neurophysin peptide at paired basic residuesBiochemical and Biophysical Research Communications, 1986
- Pathways of Protein Secretion in EukaryotesScience, 1985
- The somatostatin-28 convertase of rat brain cortex generates both somatostatin-14 and somatostatin-28 (1–12)Biochemical and Biophysical Research Communications, 1985
- Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factorCell, 1984
- A novel protease from yeast with specificity towards paired basic residuesNature, 1984
- Vasopressin and oxytocin are expressed as polyproteinsTrends in Biochemical Sciences, 1983
- Regional distribution of the Mr 15,000 somatostatin precursor, somatostatin-28 and somatostatin-14 in the rat brain suggests a differential intracellular processing of the high molecular weight speciesBiochemical and Biophysical Research Communications, 1983
- Post-Translational Proteolysis in Polypeptide Hormone BiosynthesisAnnual Review of Physiology, 1982
- Porcine Proinsulin: Characterization and Amino Acid SequenceScience, 1968