换一批Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.
第一作者：
Johanna,Wanngren
第一单位：
Department of NVS, Center for Alzheimer Research, Karolinska Institutet, Stockholm, Sweden.
作者：
关键词
AD, Alzheimer diseaseAICD, amyloid precursor protein intracellular domainAPP, amyloid precursor proteinAlzheimer diseaseAmyloid β-peptideAβ, amyloid-β peptideBD8, blastocyst-derived embryonic stem cellsBis-Tris, 2-(bis(2-hydroxyethyl)amino)-2-(hydroxymethyl)propane-1,3-diolCHAPSO, 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-1-propanesulfonic acidCRM, column-washed dog pancreas rough microsomesCTF, C-terminal fragmentER, endoplasmic reticulumEndo H, endoglycosidase HFAD, familial ADFLIM/FRET, Fluorescence Lifetime Imaging/ Fluorescence Resonance Energy TransferGCB, γ-secretase inhibitor coupled to biotinGVP, Gal4VP16Lep, leader peptidaseMGD, minimal glycosylation distanceMSD, Meso Scale DiscoveryMembrane integrationNTF, N-terminal fragmentPS, presenilinProtein structureRM, rough microsomesTMD, transmembrane domainsWT, wild typeγ-Secretase
DOI
10.1016/j.fob.2014.04.006
PMID
24918054
发布时间
2021-10-21
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FEBS open bio
393-406页
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