Prohormone Thiol Protease and Enkephalin Precursor Processing: Cleavage at Dibasic and Monobasic Sites
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.1992.tb08871.x/fullpdf
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1. PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues.
2. Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo.
3. Primary structure of the human Met- and Leu-enkephalin precursor and its mRNA
4. Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β cell via two distinct site-specific endopeptidases
5. Dynorphin converting enzyme with unusual specificity from rat brain.
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1. Role of glutamine-169 in the substrate recognition of human aminopeptidase B;Biochimica et Biophysica Acta (BBA) - General Subjects;2014-06
2. Prohormone Thiol Protease;Handbook of Proteolytic Enzymes;2013
3. Post-translational Processing of Gastrointestinal Peptides;Physiology of the Gastrointestinal Tract;2012
4. Proteases for Processing Proneuropeptides into Peptide Neurotransmitters and Hormones;Annual Review of Pharmacology and Toxicology;2008-02-01
5. Cathepsin L Expression Is Directed to Secretory Vesicles for Enkephalin Neuropeptide Biosynthesis and Secretion;Journal of Biological Chemistry;2007-03
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