Synthesis and processing of pro-ocytocin in bovine corpus luteum and granulosa cells
Author:
Publisher
Elsevier BV
Subject
Endocrinology,Molecular Biology,Biochemistry
Reference27 articles.
1. Processing Endoprotease Recognizes a Structural Feature at the Cleavage Site of Peptide Prohormones
2. Hormonal Interactions at the Molecular Level. A Study of Oxytocin and Vasopressin Binding to Bovine Neurophysins
3. An endopeptidase associated with bovine neurohypophysis secretory granules cleaves pro-ocytocin/neurophysin peptide at paired basic residues
4. C-Terminally extended ocytocin and pro-ocytocin: Neurophysin peptide converting enzyme in bovine corpus luteum
5. Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving prooxytocin/neurophysin peptides at the basic amino acid doublet
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1. Magnolysin;Handbook of Proteolytic Enzymes;2013
2. Role of Amino Acid Sequences Flanking Dibasic Cleavage Sites in Precursor Proteolytic Processing;European Journal of Biochemistry;2008-06-28
3. Magnolysin;Handbook of Proteolytic Enzymes;2004
4. Peptides as tools for studying propeptide and proprotein processing;Analytica Chimica Acta;1997-10
5. Role of Amino Acid Sequences Flanking Dibasic Cleavage Sites in Precursor Proteolytic Processing. The Importance of the First Residue C-Terminal of the Cleavage Site;European Journal of Biochemistry;1995-02
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