The production ratios of AICDε51 and Aβ42 by intramembrane proteolysis of βAPP do not always change in parallel.
about
Structural biology of presenilin 1 complexesAlzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Evidence of a novel mechanism for partial γ-secretase inhibition induced paradoxical increase in secreted amyloid β proteinγ-Secretase Modulators and APH1 Isoforms Modulate γ-Secretase Cleavage but Not Position of ε-Cleavage of the Amyloid Precursor Protein (APP).Major carboxyl terminal fragments generated by γ-secretase processing of the Alzheimer amyloid precursor are 50 and 51 amino acids long.Elderly depression and diffusion tensor imaging.Biomarkers and Alzheimer spectrum.New drugs for Alzheimer's disease in Japan.
P2860
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P2860
The production ratios of AICDε51 and Aβ42 by intramembrane proteolysis of βAPP do not always change in parallel.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh-hant
name
The production ratios of AICDε ...... not always change in parallel.
@en
The production ratios of AICDε ...... not always change in parallel.
@nl
type
label
The production ratios of AICDε ...... not always change in parallel.
@en
The production ratios of AICDε ...... not always change in parallel.
@nl
prefLabel
The production ratios of AICDε ...... not always change in parallel.
@en
The production ratios of AICDε ...... not always change in parallel.
@nl
P2093
P50
P1476
The production ratios of AICDε ...... not always change in parallel
@en
P2093
Hitoshi Tanimukai
Kana Fujii
Kanta Yanagida
Masatoshi Takeda
Satoru Funamoto
Shin-ichi Tatsumi
Shinji Tagami
Taisuke Nakayama
Takashi Kudo
Takashi Morihara
P304
P356
10.1111/J.1479-8301.2010.00330.X
P577
2010-09-01T00:00:00Z