Presenilin-1

[1]. Dieter Edbauer, et al. Reconstitution of gamma-secretase activity. Nat Cell Biol. 2003 May;5(5):486-8. [Content Brief]

[2]. Xiao-Chen Bai, et al. An atomic structure of human γ-secretase. Nature. 2015 Sep 10;525(7568):212-217. [Content Brief]

[3]. Peilong Lu, et al. Three-dimensional structure of human γ-secretase. Nature. 2014 Aug 14;512(7513):166-170. [Content Brief]

[4]. M Murayama, et al. Direct association of presenilin-1 with beta-catenin. FEBS Lett. 1998 Aug 14;433(1-2):73-7. [Content Brief]

[5]. Guanghui Yang, et al. Structural basis of Notch recognition by human γ-secretase. Nature. 2019 Jan;565(7738):192-197. [Content Brief]

[6]. Rui Zhou, et al. Recognition of the amyloid precursor protein by human γ-secretase. Science. 2019 Feb 15;363(6428):eaaw0930. [Content Brief]

[7]. Patrick C Fraering, et al. Purification and characterization of the human gamma-secretase complex. Biochemistry. 2004 Aug 3;43(30):9774-89. [Content Brief]

[8]. W J Ray, et al. Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch. J Biol Chem. 1999 Dec 17;274(51):36801-7. [Content Brief]

[9]. Jun Wang, et al. C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation. J Neurochem. 2006 Jan;96(1):218-27. [Content Brief]

[10]. Huiping Tu, et al. Presenilins form ER Ca2+ leak channels, a function disrupted by familial Alzheimer's disease-linked mutations. Cell. 2006 Sep 8;126(5):981-93. [Content Brief]

[11]. H Steiner, et al. Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis. Biochemistry. 1999 Nov 2;38(44):14600-5. [Content Brief]

[12]. L Kulic, et al. Separation of presenilin function in amyloid beta-peptide generation and endoproteolysis of Notch. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5913-8. [Content Brief]

[13]. M S Wolfe, et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 1999 Apr 8;398(6727):513-7. [Content Brief]

[14]. W Taylor Kimberly, et al. Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6382-7. [Content Brief]

[15]. Claudia Litterst, et al. Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor. J Biol Chem. 2007 Jun 1;282(22):16155-63. [Content Brief]

[16]. Wei-Ting Chen, et al. G206D Mutation of Presenilin-1 Reduces Pen2 Interaction, Increases Aβ42/Aβ40 Ratio and Elevates ER Ca(2+) Accumulation. Mol Neurobiol. 2015 Dec;52(3):1835-1849. [Content Brief]

[17]. Philippe Marambaud, et al. A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 2002 Apr 15;21(8):1948-56. [Content Brief]

[18]. Jonathan D J Wrigley, et al. Conserved residues within the putative active site of gamma-secretase differentially influence enzyme activity and inhibitor binding. J Neurochem. 2004 Sep;90(6):1312-20. [Content Brief]

[19]. Jing Dong, et al. A Novel PSEN1 K311R Mutation Discovered in Chinese Families with Late-Onset Alzheimer's Disease Affects Amyloid-β Production and Tau Phosphorylation. J Alzheimers Dis. 2017;57(2):613-623. [Content Brief]

[20]. Elizabeth A Heilig, et al. A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activity. J Biol Chem. 2010 Jul 16;285(29):22350-9. [Content Brief]

[21]. O Berezovska, et al. Aspartate mutations in presenilin and gamma-secretase inhibitors both impair notch1 proteolysis and nuclear translocation with relative preservation of notch1 signaling. J Neurochem. 2000 Aug;75(2):583-93. [Content Brief]

[22]. Wieslaw K Dowjat, et al. A novel highly pathogenic Alzheimer presenilin-1 mutation in codon 117 (Pro117Ser): Comparison of clinical, neuropathological and cell culture phenotypes of Pro117Leu and Pro117Ser mutations. J Alzheimers Dis. 2004 Feb;6(1):31-43. [Content Brief]