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1 d not affect the amyloidogenic processing of amyloid beta protein precursor.
2 ical beta-secretase cleavage site within the amyloid beta-protein precursor.
3 the Kunitz-type protease inhibitor domain of amyloid beta-protein precursor.
5 he familial Alzheimer's disease gene product amyloid beta protein precursor (A beta PP) is sequential
6 or IXa and Factor XIa (ie, protease nexin-2/ amyloid beta-protein precursor, A beta PP) in the organi
10 ed increase in the levels of cell-associated amyloid beta-protein precursor (AbetaPP) and cell death.
14 ease-causing mutations in the genes encoding amyloid beta protein precursor and presenilins, raising
16 nal presenilins and cleaves substrates (e.g. amyloid beta-protein precursor and Notch) with very loos
17 I integral membrane proteins, including the amyloid beta-protein precursor and the Notch receptor, a
18 ns of a variety of substrates, including the amyloid beta-protein precursor and the Notch receptor.
19 I integral membrane proteins, including the amyloid beta-protein precursor and the Notch receptor.
20 eta1-40 or Abeta1-42 in the absence of human amyloid beta protein precursor (APP) overexpression.
21 were then tested in acute dosing studies in amyloid beta protein precursor (APP) transgenic mice, an
22 en shown to influence limited proteolysis of amyloid beta protein precursor (APP), Notch and ErbB4, a
24 vidence suggests that dysregulated levels of amyloid beta-protein precursor (APP) and its catabolites
25 rous type I membrane proteins, including the amyloid beta-protein precursor (APP) and the Notch recep
26 se A beta is produced from the processing of amyloid beta-protein precursor (APP) by beta- and gamma-
28 protein (Abeta) is released from the larger amyloid beta-protein precursor (APP) by unidentified enz
29 Protease nexin-2 (PN-2), a soluble form of amyloid beta-protein precursor (APP) containing a Kunin
31 nic mouse models that coexpress human PS and amyloid beta-protein precursor (APP) genes and analyzed
32 idation of the proteolytic processing of the amyloid beta-protein precursor (APP) has revealed that o
33 e presenilin 1 (PS1), presenilin 2 (PS2) and amyloid beta-protein precursor (APP) mutations linked to
34 ated with Alzheimer disease, is derived from amyloid beta-protein precursor (APP) through sequential
36 own to attenuate amyloidogenic processing of amyloid-beta protein precursor (APP) in cell culture stu
39 ther LRP ligands, APOE and APP (encoding the amyloid beta-protein precursor), have now all been genet
41 nd able to produce amyloid beta-peptides and amyloid beta-protein precursor intracellular domain.
43 is of a variety of substrates, including the amyloid beta-protein precursor of Alzheimer's disease an
44 agulant protein, an aprotinin mutant (6L15), amyloid beta-protein precursor, or tissue factor pathway
45 , the Abeta parent molecule protease nexin-2/amyloid beta-protein precursor (PN-2/AbetaPP), which is
48 peptide inhibitors and designed to mimic the amyloid beta-protein precursor substrate bind specifical
49 s of presenilin familial AD mutations on the amyloid beta-protein precursor, the presenilins themselv
51 ate the possibility that caspase cleavage of amyloid beta-protein precursor with the generation of C3
52 mice, an AD mouse model overexpressing human amyloid beta-protein precursor with the Swedish double m
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