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The new enzymology of precursor processing endoproteases
1992
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Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles
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Kinetic studies on the processing of human beta-lipotropin by bovine pituitary intermediate lobe pro-opiomelanocortin-converting enzyme
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Generation of Lys-gamma 3-melanotropin from pro-opiomelanocortin 1-77 by a bovine intermediate lobe secretory vesicle membrane-associated aspartic protease and purified pro-opiomelanocortin converting enzyme
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Purification and characterization of a paired basic residue-specific prohormone-converting enzyme from bovine pituitary neural lobe secretory vesicles
1986
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Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme
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PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues
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Characterization of pro-opiocortin-converting activity in purified secretory granules from rat pituitary neurointermediate lobe
1982
Loh, Y.P.; Gainer, H.
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Chromaffin granule aspartic proteinase processes recombinant proopiomelanocortin (POMC)
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Azaryan, A.V.; Schiller, M.R.; Hook, V.Y.H.
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Pro-opiomelanocortin and pro-vasopressin converting enzyme in pituitary secretory vesicles
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Loh, Y.P.; Birch, N.P.; Castro, M.G.
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Regulation of prohormone convertase 1 (PC1) by gp130-related cytokines
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Yapsin A
2004
Loh, Y.P.; Cawley, N.X.
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
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Cysteine cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimers disease
2012
Hook, V.; Funkelstein, L.; Wegrzyn, J.; Bark, S.; Kindy, M.; Hook, G.
Biochim. Biophys. Acta
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Biosynthesis, trafficking, and secretion of pro-opiomelanocortin-derived peptides
2016
Cawley, N.; Li, Z.; Loh, Y.
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