These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

144 related items for PubMed ID: 7790890

  • 1. Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles.
    Song L, Fricker L.
    J Neurochem; 1995 Jul; 65(1):444-53. PubMed ID: 7790890
    [Abstract] [Full Text] [Related]

  • 2. Posttranslational processing of carboxypeptidase E, a neuropeptide-processing enzyme, in AtT-20 cells and bovine pituitary secretory granules.
    Fricker LD, Devi L.
    J Neurochem; 1993 Oct; 61(4):1404-15. PubMed ID: 8376994
    [Abstract] [Full Text] [Related]

  • 3.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 4. The post-translational processing and intracellular sorting of carboxypeptidase H in the islets of Langerhans.
    Guest PC, Arden SD, Rutherford NG, Hutton JC.
    Mol Cell Endocrinol; 1995 Aug 30; 113(1):99-108. PubMed ID: 8674818
    [Abstract] [Full Text] [Related]

  • 5. The pro region is not required for the expression or intracellular routeing of carboxypeptidase E.
    Song L, Fricker LD.
    Biochem J; 1997 Apr 01; 323 ( Pt 1)(Pt 1):265-71. PubMed ID: 9173892
    [Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary.
    Song L, Fricker LD.
    J Biol Chem; 1995 Oct 20; 270(42):25007-13. PubMed ID: 7559630
    [Abstract] [Full Text] [Related]

  • 8.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 9.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 10. 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 20; 18(2):121-32. PubMed ID: 10073571
    [Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12. Processing and secretion of human carboxypeptidase E by C6 glioma cells.
    Manser E, Fernandez D, Lim L.
    Biochem J; 1991 Dec 15; 280 ( Pt 3)(Pt 3):695-701. PubMed ID: 1764034
    [Abstract] [Full Text] [Related]

  • 13. Induced and spontaneous mutations at Ser202 of carboxypeptidase E. Effect on enzyme expression, activity, and intracellular routing.
    Varlamov O, Leiter EH, Fricker L.
    J Biol Chem; 1996 Jun 14; 271(24):13981-6. PubMed ID: 8662840
    [Abstract] [Full Text] [Related]

  • 14. Carboxypeptidase E, a peripheral membrane protein implicated in the targeting of hormones to secretory granules, co-aggregates with granule content proteins at acidic pH.
    Rindler MJ.
    J Biol Chem; 1998 Nov 20; 273(47):31180-5. PubMed ID: 9813022
    [Abstract] [Full Text] [Related]

  • 15. Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary.
    Hook VY, Loh YP.
    Proc Natl Acad Sci U S A; 1984 May 20; 81(9):2776-80. PubMed ID: 6326144
    [Abstract] [Full Text] [Related]

  • 16.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 17. Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10).
    Fricker LD, Das B, Angeletti RH.
    J Biol Chem; 1990 Feb 15; 265(5):2476-82. PubMed ID: 2303412
    [Abstract] [Full Text] [Related]

  • 18. Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice.
    Cool DR, Normant E, Shen F, Chen HC, Pannell L, Zhang Y, Loh YP.
    Cell; 1997 Jan 10; 88(1):73-83. PubMed ID: 9019408
    [Abstract] [Full Text] [Related]

  • 19. Identification of peptides from brain and pituitary of Cpe(fat)/Cpe(fat) mice.
    Che FY, Yan L, Li H, Mzhavia N, Devi LA, Fricker LD.
    Proc Natl Acad Sci U S A; 2001 Aug 14; 98(17):9971-6. PubMed ID: 11481435
    [Abstract] [Full Text] [Related]

  • 20. Comparative biosynthesis, covalent post-translational modifications and efficiency of prosegment cleavage of the prohormone convertases PC1 and PC2: glycosylation, sulphation and identification of the intracellular site of prosegment cleavage of PC1 and PC2.
    Benjannet S, Rondeau N, Paquet L, Boudreault A, Lazure C, Chrétien M, Seidah NG.
    Biochem J; 1993 Sep 15; 294 ( Pt 3)(Pt 3):735-43. PubMed ID: 8397508
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 8.