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cDNA structure, tissue distribution and chromosomal localization of rat PC7: A novel mammalian proprotein convertase closest to yeast kexin-like proteinases
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Seidah NG, Hamelin J, Mamarbachi M, Dong W, Tadros H, Mbikay M, Chrétien M, Day R: cDNA structure, tissue distribution and chromosomal localization of rat PC7: a novel mammalian proprotein convertase closest to yeast kexin-like proteinases. Proc Natl Acad Sci USA 1996, 93:342-355. This paper describes cloning of the cDNA sequence of PC7 and analysis of its tissue expression. This report also revealed that both PC7 and furin exhibit a widespread tissue distribution.
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Implication of the RRGD sequence of the proprotein convertase PC1 in zymogen processing and cellular trafficking
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Lusson J, Benjannet S, Hamelin J, Savaria D, Lazure C, Chrétien M, Seidah NG: Implication of the RRGD sequence of the proprotein convertase PC1 in zymogen processing and cellular trafficking. Biochem J 1997, 326:737-744. This is the first indication ever that the RGD motif in convertases has functional significance in terms of stability and intracellular routing of PC1.
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A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease
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The isoforms of the proprotein convertase 5 are sorted to different subcellular compartments
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De Bie I, Marcinkiewicz M, Malide D, Lazure C, Nakayama K, Bendayan M, Seidah NG: The isoforms of the proprotein convertase 5 are sorted to different subcellular compartments. J Cell Biol 1996, 135:1261-1275. This is the first known case where from a single gene, via alternative splicing of the derived heteronuclear RNA, one can generate two isoforms which are sorted to different subcellular compartments. Furthermore, in the case of PC5, within the cell, the two isoforms PC5-A and PC5-B should process different precursor proteins.
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Comparative biosynthesis, post-translational modifications and efficiency of prosegment cleavage of the pro-hormone convertases PC1 and PC2: Glycosylation, sulfation and identification of the intracellular site of prosegment cleavage of PC1 and PC2
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Benjannet S, Rondeau N, Paquet L, Boudreault A, Lazure C, Chrétien M, Seidah NG: Comparative biosynthesis, post-translational modifications and efficiency of prosegment cleavage of the pro-hormone convertases PC1 and PC2: glycosylation, sulfation and identification of the intracellular site of prosegment cleavage of PC1 and PC2. Biochem J 1993, 294:735-743.
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Munzer JS, Basak A, Zhong M, Mamarbachi M, Hamelin J, Savaria D, Lazure C, Benjannet S, Chrétien M, Seidah NG: In Vitro characterization of the novel proprotein convertase PC7. J Biol Chem 1997, 272:19672-19681. The first report on the in vitro properties of recombinant PC7 which provided evidence for a carboxy-terminally extended P domain as compared to kexin and furin.
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Electron microscopic immunocytochemical evidence for the involvement of the convertases PC1 and PC2 in the processing of proinsulin in pancreatic β-cells
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Jean F, Basak A, DiMaio J, Seidah NG, Lazure C: An internally quenched fluorogenic substrate of prohormone convertase 1 and furin leads to a potent prohormone convertase inhibitor. Biochem J 1995, 307:689-695.
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Ayoubi TAY, Meulemans SMP, Roebroek AJM, Van de Ven WJM: Production of recombinant proteins in chinese hamster ovary cells overexpressing the subtilisin-like proprotein converting enzyme furin. Mol Biol Rep 1996, 23:87-95. This is the first report to deal with the advantage of cellular overexpression of both a convertase and its substrate in order to produce large quantities of bioactive von Willebrand factor ex vivo.
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