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Journal Abstract Search

108 related items for PubMed ID: 8359021

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  • 5. Cloning and expression of Aplysia carboxypeptidase D, a candidate prohormone-processing enzyme.
    Fan X, Qian Y, Fricker LD, Akalal DB, Nagle GT.
    DNA Cell Biol; 1999 Feb; 18(2):121-32. PubMed ID: 10073571
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  • 6. The function and differential sorting of a family of aplysia prohormone processing enzymes.
    Chun JY, Korner J, Kreiner T, Scheller RH, Axel R.
    Neuron; 1994 Apr; 12(4):831-44. PubMed ID: 8161455
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  • 7. 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
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  • 13. Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA.
    Bloomquist BT, Eipper BA, Mains RE.
    Mol Endocrinol; 1991 Dec 25; 5(12):2014-24. PubMed ID: 1791845
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  • 14. Neuropeptide amidation: cloning of a bifunctional alpha-amidating enzyme from Aplysia.
    Fan X, Spijker S, Akalal DB, Nagle GT.
    Brain Res Mol Brain Res; 2000 Oct 20; 82(1-2):25-34. PubMed ID: 11042355
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  • 15. Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2.
    Smeekens SP, Steiner DF.
    J Biol Chem; 1990 Feb 25; 265(6):2997-3000. PubMed ID: 2154467
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  • 16. 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
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  • 17. Furin: the prototype mammalian subtilisin-like proprotein-processing enzyme. Endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway.
    Van de Ven WJ, Creemers JW, Roebroek AJ.
    Enzyme; 1991 Dec 23; 45(5-6):257-70. PubMed ID: 1843280
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  • 18. PC8 [corrected], a new member of the convertase family.
    Bruzzaniti A, Goodge K, Jay P, Taviaux SA, Lam MH, Berta P, Martin TJ, Moseley JM, Gillespie MT.
    Biochem J; 1996 Mar 15; 314 ( Pt 3)(Pt 3):727-31. PubMed ID: 8615762
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  • 19. Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarity to PACE4.
    Nakagawa T, Hosaka M, Torii S, Watanabe T, Murakami K, Nakayama K.
    J Biochem; 1993 Feb 15; 113(2):132-5. PubMed ID: 8468318
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  • 20. Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. Its testis-specific expression.
    Nakayama K, Kim WS, Torii S, Hosaka M, Nakagawa T, Ikemizu J, Baba T, Murakami K.
    J Biol Chem; 1992 Mar 25; 267(9):5897-900. PubMed ID: 1372895
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