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152 related items for PubMed ID: 8995723

  • 1. Prorenin activation and prohormone convertases in the mouse As4.1 cell line.
    Laframboise M, Reudelhuber TL, Jutras I, Brechler V, Seidah NG, Day R, Gross KW, Deschepper CF.
    Kidney Int; 1997 Jan; 51(1):104-9. PubMed ID: 8995723
    [Abstract] [Full Text] [Related]

  • 2. Human lactase-phlorizin hydrolase is not processed by furin, PC1/PC3, PC2, PACE4 and PC5/PC6A of the family of subtilisin-like proprotein processing proteases.
    Wüthrich M, Creemers JW, van de Ven WJ, Sterchi EE.
    Biochim Biophys Acta; 1996 May 28; 1311(3):199-203. PubMed ID: 8664347
    [Abstract] [Full Text] [Related]

  • 3. Proteolytic processing of human prorenin in renal and non-renal tissues.
    Reudelhuber TL, Ramla D, Chiu L, Mercure C, Seidah NG.
    Kidney Int; 1994 Dec 28; 46(6):1522-4. PubMed ID: 7699995
    [Abstract] [Full Text] [Related]

  • 4. Structure and expression of mouse furin, a yeast Kex2-related protease. Lack of processing of coexpressed prorenin in GH4C1 cells.
    Hatsuzawa K, Hosaka M, Nakagawa T, Nagase M, Shoda A, Murakami K, Nakayama K.
    J Biol Chem; 1990 Dec 25; 265(36):22075-8. PubMed ID: 2266110
    [Abstract] [Full Text] [Related]

  • 5. Proprotein conversion is determined by a multiplicity of factors including convertase processing, substrate specificity, and intracellular environment. Cell type-specific processing of human prorenin by the convertase PC1.
    Benjannet S, Reudelhuber T, Mercure C, Rondeau N, Chrétien M, Seidah NG.
    J Biol Chem; 1992 Jun 05; 267(16):11417-23. PubMed ID: 1597471
    [Abstract] [Full Text] [Related]

  • 6. Cathepsin B is a prorenin processing enzyme.
    Neves FA, Duncan KG, Baxter JD.
    Hypertension; 1996 Mar 05; 27(3 Pt 2):514-7. PubMed ID: 8613195
    [Abstract] [Full Text] [Related]

  • 7. Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex.
    Mercure C, Jutras I, Day R, Seidah NG, Reudelhuber TL.
    Hypertension; 1996 Nov 05; 28(5):840-6. PubMed ID: 8901832
    [Abstract] [Full Text] [Related]

  • 8. Endoproteolytic processing of integrin pro-alpha subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7.
    Lissitzky JC, Luis J, Munzer JS, Benjannet S, Parat F, Chrétien M, Marvaldi J, Seidah NG.
    Biochem J; 2000 Feb 15; 346 Pt 1(Pt 1):133-8. PubMed ID: 10657249
    [Abstract] [Full Text] [Related]

  • 9. Cellular processing of the neurotrophin precursors of NT3 and BDNF by the mammalian proprotein convertases.
    Seidah NG, Benjannet S, Pareek S, Chrétien M, Murphy RA.
    FEBS Lett; 1996 Feb 05; 379(3):247-50. PubMed ID: 8603699
    [Abstract] [Full Text] [Related]

  • 10. The regulated cell surface zymogen activation of the proprotein convertase PC5A directs the processing of its secretory substrates.
    Mayer G, Hamelin J, Asselin MC, Pasquato A, Marcinkiewicz E, Tang M, Tabibzadeh S, Seidah NG.
    J Biol Chem; 2008 Jan 25; 283(4):2373-84. PubMed ID: 18039650
    [Abstract] [Full Text] [Related]

  • 11. Pro-protein convertases (PCs) other than PC6 are not tightly regulated for implantation in the human endometrium.
    Freyer C, Kilpatrick LM, Salamonsen LA, Nie G.
    Reproduction; 2007 Jun 25; 133(6):1189-97. PubMed ID: 17636173
    [Abstract] [Full Text] [Related]

  • 12. A targeting sequence for dense secretory granules resides in the active renin protein moiety of human preprorenin.
    Chu WN, Baxter JD, Reudelhuber TL.
    Mol Endocrinol; 1990 Dec 25; 4(12):1905-13. PubMed ID: 2082189
    [Abstract] [Full Text] [Related]

  • 13. Distinct mRNA expression of the highly homologous convertases PC5 and PACE4 in the rat brain and pituitary.
    Dong W, Marcinkiewicz M, Vieau D, Chrétien M, Seidah NG, Day R.
    J Neurosci; 1995 Mar 25; 15(3 Pt 1):1778-96. PubMed ID: 7891135
    [Abstract] [Full Text] [Related]

  • 14. Role of prohormone convertases in pro-neuropeptide Y processing: coexpression and in vitro kinetic investigations.
    Brakch N, Rist B, Beck-Sickinger AG, Goenaga J, Wittek R, Bürger E, Brunner HR, Grouzmann E.
    Biochemistry; 1997 Dec 23; 36(51):16309-20. PubMed ID: 9405066
    [Abstract] [Full Text] [Related]

  • 15. Comparative proteolytic processing of rat prosomatostatin by the convertases PC1, PC2, furin, PACE4 and PC5 in constitutive and regulated secretory pathways.
    Brakch N, Galanopoulou AS, Patel YC, Boileau G, Seidah NG.
    FEBS Lett; 1995 Apr 03; 362(2):143-6. PubMed ID: 7720860
    [Abstract] [Full Text] [Related]

  • 16. Subtilisin-like proprotein convertases, PACE4 and PC8, as well as furin, are endogenous proalbumin convertases in HepG2 cells.
    Mori K, Imamaki A, Nagata K, Yonetomi Y, Kiyokage-Yoshimoto R, Martin TJ, Gillespie MT, Nagahama M, Tsuji A, Matsuda Y.
    J Biochem; 1999 Mar 03; 125(3):627-33. PubMed ID: 10050053
    [Abstract] [Full Text] [Related]

  • 17. Increased proteolytic processing of protein tyrosine phosphatase mu in confluent vascular endothelial cells: the role of PC5, a member of the subtilisin family.
    Campan M, Yoshizumi M, Seidah NG, Lee ME, Bianchi C, Haber E.
    Biochemistry; 1996 Mar 26; 35(12):3797-802. PubMed ID: 8620001
    [Abstract] [Full Text] [Related]

  • 18. cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells.
    Lusson J, Vieau D, Hamelin J, Day R, Chrétien M, Seidah NG.
    Proc Natl Acad Sci U S A; 1993 Jul 15; 90(14):6691-5. PubMed ID: 8341687
    [Abstract] [Full Text] [Related]

  • 19. Highly regulated expression of subtilisin-like proprotein convertase PACE4 (SPC4) during dentinogenesis.
    Akamatsu T, Matsuda Y, Tsumura K, Tada J, Parvin MN, Wei W, Kanamori N, Hosoi K.
    Biochem Biophys Res Commun; 2000 Jun 07; 272(2):410-5. PubMed ID: 10833428
    [Abstract] [Full Text] [Related]

  • 20. Differential regulation of cathepsin B and prorenin gene expression in renal juxtaglomerular cells.
    Todorov V, Müller M, Kurtz A.
    Kidney Blood Press Res; 2001 Jun 07; 24(2):75-8. PubMed ID: 11435737
    [Abstract] [Full Text] [Related]

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