Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing

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• 作者：Marie Decock^a ; Laetitia El Haylani^a ; Serena Stanga^a ; Ilse Dewachter^a ; Jean-Noë ; l Octave^a ; Steven O. Smith^b ; Stefan N. Constantinescu^c ; Pascal Kienlen-Campard^a ; ^{pascal.kienlen-campard@uclouvain.be" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Aβ ; β-amyloid peptide ; AD ; Alzheimer&rsquo ; s disease ; APP ; amyloid precursor protein ; AICD ; APP intracellular domain ; sAPPα ; soluble APPα ; sAPPβ ; soluble APPβ ; CHO ; chinese hamster ovary ; CTF ; C-terminal fragment ; DAPT ; N-[N-(3 ; 5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester ; DTT ; dithiothreitol ; ECL ; enzymatic chemi-luminescence ; ECLIA ; electro-chemiluminescence immuno-assay ; FBS ; fetal bovine serum ; FRET ; fluorescence resonance energy transfer ; KPI ; Kunitz-type protease inhibitor
• 刊名：FEBS Open Bio
• 出版年：2015
• 出版时间：2015
• 年：2015
• 卷：5
• 期：Complete
• 页码：763-773
• 全文大小：2234 K

文摘

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d="p0005">Amyloid precursor protein (APP) dimerizes more than its C-terminal fragments in cells.

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d="p0010">Mutations of membrane GXXXG motifs affect Aβ production but not APP dimerization.

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d="p0015">Deletion of the APP intracellular domain increases APP dimerization.

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