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1 th virulence and has a putative action as an endothelin-converting enzyme.
3 ned whether agonist degradation by endosomal endothelin-converting enzyme 1 (ECE-1) controls SSTR2A t
4 etalloendopeptidases, which includes NEP and endothelin-converting enzyme 1 (ECE-1), an enzyme involv
5 ns only 18 genes, among which Ece1, encoding endothelin-converting enzyme 1, stands out as a candidat
6 -1 expression, indicating the presence of an endothelin-converting enzyme 1/endothelin 1-SphK positiv
8 t homology with neutral endopeptidase 24.11, endothelin converting enzyme-1 (ECE-1), and the PEX gene
9 erformed on the gro1, B-factor, adlican, and endothelin converting enzyme-1 genes and confirmed micro
10 lly generated from its inactive precursor by endothelin-converting enzyme-1 (ECE-1) and acts on the e
11 is report, we describe the identification of endothelin-converting enzyme-1 (ECE-1) as a novel Abeta-
12 itro models we have previously characterized endothelin-converting enzyme-1 (ECE-1) as an Abeta-degra
15 d selective non-peptidic inhibitors of human endothelin-converting enzyme-1 (ECE-1) have been designe
17 ported the intracellular localization of the endothelin-converting enzyme-1 (ECE-1) in human umbilica
18 more, we have previously shown that both the endothelin-converting enzyme-1 (ECE-1) inhibitor, phosph
24 eptide is the conversion of its precursor by endothelin-converting enzyme-1 (ECE-1), a metalloproteas
25 ss has been linked to enhanced expression of endothelin-converting enzyme-1 (ECE-1, the enzyme that c
27 To investigate the phosphorylation of human endothelin-converting enzyme-1 (hECE-1) and identify pot
29 t inhibition of SphK leads to suppression of endothelin-converting enzyme-1 expression, indicating th
30 our murine model by using phospharamidon, an endothelin-converting enzyme-1 inhibitor; knocking down
31 converting enzyme-1 inhibitor; knocking down endothelin-converting enzyme-1 mRNA; or blocking the bin
32 red liver led to a decrease in expression of endothelin-converting enzyme-1, a critical regulator of
33 rocessing, such as insulin degrading enzyme, endothelin-converting enzyme-1, neprilysin and alpha-sec
39 a-amyloid in the brain but confirm roles for endothelin-converting enzyme and neprilysin and indicate
40 amyloid levels are significantly elevated in endothelin-converting enzyme and neprilysin knock-out mi
41 increasing the rate of Abeta degradation by endothelin-converting enzyme and not by activating nonam
43 In contrast, phosphoramidon, an inhibitor of endothelin-converting enzyme, did not significantly chan
48 We therefore investigated the effects of endothelin-converting enzyme (ECE) inhibition and endoth
50 he roles of ET(A) and ET(B) receptors and of endothelin-converting enzyme (ECE)-1 in ET-1-induced vas
52 tudies have identified a polymorphism in the endothelin-converting enzyme (ECE)-1b promoter (-338C/A)
54 ngiotensin-converting enzyme, neprilysin and endothelin-converting enzyme function as vasopeptidases
56 est that the combination of low-dose CsA and endothelin-converting enzyme inhibition may prove useful
57 receptor antagonist; and phosporamindon, an endothelin converting enzyme inhibitor in the eyes of di
58 ld be significantly improved by combining an endothelin-converting enzyme inhibitor with low-dose CsA
59 i.m. on day 2), low-dose CsA (25 mg/kg), an endothelin-converting enzyme inhibitor, phosphoramidon (
60 sAbeta-degrading enzymes examined, including endothelin-converting enzyme, insulin-degrading enzyme,
61 a nicotinic receptor (CHRNG, 6 subjects) and endothelin converting enzyme-like 1 (ECEL1, 4 subjects).
62 ltiplex consanguineous family to identify in endothelin-converting enzyme-like 1 (ECEL1) mutations th
63 tor antagonism or inhibition of the specific endothelin-converting enzymes may, therefore, represent
64 f several degradative enzymes, including the endothelin-converting enzymes, neprilysin, insulin-degra
65 nists (BQ123 plus BQ788) or by inhibition of endothelin-converting enzyme (phosphoramidon or SM19712)
67 ty to mammalian metallopeptidases, including endothelin-converting enzyme, which converts a potent va
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