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

128 related items for PubMed ID: 9631452

  • 1. Caspase-mediated cleavage is not required for the activity of presenilins in amyloidogenesis and NOTCH signaling.
    Brockhaus M, Grünberg J, Röhrig S, Loetscher H, Wittenburg N, Baumeister R, Jacobsen H, Haass C.
    Neuroreport; 1998 May 11; 9(7):1481-6. PubMed ID: 9631452
    [Abstract] [Full Text] [Related]

  • 2. Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family.
    Grunberg J, Walter J, Loetscher H, Deuschle U, Jacobsen H, Haass C.
    Biochemistry; 1998 Feb 24; 37(8):2263-70. PubMed ID: 9485372
    [Abstract] [Full Text] [Related]

  • 3. Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing.
    Baumeister R, Leimer U, Zweckbronner I, Jakubek C, Grünberg J, Haass C.
    Genes Funct; 1997 Apr 24; 1(2):149-59. PubMed ID: 9680315
    [Abstract] [Full Text] [Related]

  • 4. The nonconserved hydrophilic loop domain of presenilin (PS) is not required for PS endoproteolysis or enhanced abeta 42 production mediated by familial early onset Alzheimer's disease-linked PS variants.
    Saura CA, Tomita T, Soriano S, Takahashi M, Leem JY, Honda T, Koo EH, Iwatsubo T, Thinakaran G.
    J Biol Chem; 2000 Jun 02; 275(22):17136-42. PubMed ID: 10748144
    [Abstract] [Full Text] [Related]

  • 5.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

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

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

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

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

  • 10. The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on abeta42 amyloid peptide formation.
    Jacobsen H, Reinhardt D, Brockhaus M, Bur D, Kocyba C, Kurt H, Grim MG, Baumeister R, Loetscher H.
    J Biol Chem; 1999 Dec 03; 274(49):35233-9. PubMed ID: 10575009
    [Abstract] [Full Text] [Related]

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

  • 12.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 13. Presenilin function and gamma-secretase activity.
    Brunkan AL, Goate AM.
    J Neurochem; 2005 May 03; 93(4):769-92. PubMed ID: 15857382
    [Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15. Presenilins are processed by caspase-type proteases.
    Loetscher H, Deuschle U, Brockhaus M, Reinhardt D, Nelboeck P, Mous J, Grünberg J, Haass C, Jacobsen H.
    J Biol Chem; 1997 Aug 15; 272(33):20655-9. PubMed ID: 9252383
    [Abstract] [Full Text] [Related]

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

  • 17. Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.
    Okochi M, Steiner H, Fukumori A, Tanii H, Tomita T, Tanaka T, Iwatsubo T, Kudo T, Takeda M, Haass C.
    EMBO J; 2002 Oct 15; 21(20):5408-16. PubMed ID: 12374741
    [Abstract] [Full Text] [Related]

  • 18. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation.
    Steiner H, Capell A, Pesold B, Citron M, Kloetzel PM, Selkoe DJ, Romig H, Mendla K, Haass C.
    J Biol Chem; 1998 Nov 27; 273(48):32322-31. PubMed ID: 9822712
    [Abstract] [Full Text] [Related]

  • 19. Proteolytic processing and degradation of Alzheimer's disease relevant proteins.
    Steiner H, Capell A, Haass C.
    Biochem Soc Trans; 1999 Feb 27; 27(2):234-42. PubMed ID: 10093740
    [No Abstract] [Full Text] [Related]

  • 20. The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum.
    Walter J, Capell A, Grünberg J, Pesold B, Schindzielorz A, Prior R, Podlisny MB, Fraser P, Hyslop PS, Selkoe DJ, Haass C.
    Mol Med; 1996 Nov 27; 2(6):673-91. PubMed ID: 8972483
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 7.