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1 radation of the APP-cleaving beta-secretase, beta-site APP-cleaving enzyme.
2 beta (C99), generated by cleavage of APP by beta-site APP cleaving enzyme 1 (BACE-1), is the primary
3 ge of the amyloid precursor protein (APP) by beta-site APP cleaving enzyme 1 (BACE1) and gamma-secret
6 elective small molecule (SR3677), suppressed beta-site APP cleaving enzyme 1 (BACE1) enzymatic action
7 r AD drug development.SIGNIFICANCE STATEMENT beta-site APP cleaving enzyme 1 (BACE1) is essential for
11 dence for modulations in axonal transport or beta-site APP cleaving enzyme 1 protein levels and activ
15 expression of AD-related genes [APP, BACE1 (beta-site APP cleaving enzyme 1)] as well as their trans
18 (APP) by the beta- and gamma-secretases, and beta-site APP-cleaving enzyme 1 (BACE1) is the beta-secr
19 eased protein levels, but not mRNA levels of beta-site APP-Cleaving Enzyme 1 (BACE1), a key enzyme in
21 ma- and beta-secretases, the latter known as beta-site APP-cleaving enzyme 1 (BACE1, or herein BACE).
24 of the promoters of betaAPP, beta-secretase (beta-site APP-cleaving enzyme 1, BACE1), and of the four
29 f amyloid precursor protein (APP) by BACE-1 (beta-site APP cleaving enzyme-1) is the rate-limiting st
30 eal that GGA1 is necessary for both LR11 and beta-site APP-cleaving enzyme-1 (BACE1) modulation of AP
31 otein (APP) is processed sequentially by the beta-site APP cleaving enzyme and gamma-secretase to gen
34 genetic approach, we show that reduction of beta-site APP cleaving enzyme (BACE) in these ArcTau mic
37 tide from amyloid precursor protein (APP) by beta-site APP cleaving enzyme (BACE)1 and gamma-secretas
39 nce that heparan sulfate (HS) interacts with beta-site APP-cleaving enzyme (BACE) 1 and regulates its
40 pe amyloid precursor protein (APP) and human beta-site APP-cleaving enzyme (BACE) and found that they
44 oid precursor protein (APP), Abeta peptides, beta-site APP-cleaving enzyme (BACE), presenilin-1 (PS-1
45 A tail construct inhibited APP cleavage in a beta-site APP-cleaving enzyme (BACE)-dependent manner.
48 an aspartyl protease as the beta-secretase (beta-site APP cleaving enzyme, BACE) involved in APP pro
50 of beta C-terminal fragments, the product of beta-site APP cleaving enzyme (BACE1) processing of amyl
51 droxyethyl amine (HEA) derived inhibitors of beta-site APP cleaving enzyme (BACE1) was optimized to a
55 ype I transmembrane aspartyl protease, BACE (beta-site APP cleaving enzyme), has been identified to b
57 xpression of this protease, termed BACE (for beta-site APP-cleaving enzyme) increased the amount of b
59 el transmembrane aspartic protease BACE (for Beta-site APP Cleaving Enzyme) is the beta-secretase tha
61 ntly, a type I membrane protein termed BACE (beta-site APP cleaving enzyme) with characteristics of a
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