Mechanistic basis for receptor-mediated pathological alpha-synuclein fibril cell-to-cell transmission in Parkinson's disease. | Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease. Zhang S, Liu YQ, Jia C, Lim YJ, Feng G, Xu E, Long H, Kimura Y, Tao Y, Zhao C, Wang C, Liu Z, Hu JJ, Ma MR, Liu Z, Jiang L, Li D, Wang R, Dawson VL, Dawson TM, Li YM, Mao X, Liu C., Free PMC Article | 12/4/2021 |
Loss of all three APP family members during development impairs synaptic function and plasticity, disrupts learning, and causes an autism-like phenotype. | Loss of all three APP family members during development impairs synaptic function and plasticity, disrupts learning, and causes an autism-like phenotype. Steubler V, Erdinger S, Back MK, Ludewig S, Fässler D, Richter M, Han K, Slomianka L, Amrein I, von Engelhardt J, Wolfer DP, Korte M, Müller UC., Free PMC Article | 11/13/2021 |
Mutation in Sodium-Glucose Cotransporter 2 Results in Down-Regulation of Amyloid Beta (A4) Precursor-Like Protein 1 in Young Age, Which May Lead to Poor Memory Retention in Old Age. | Mutation in Sodium-Glucose Cotransporter 2 Results in Down-Regulation of Amyloid Beta (A4) Precursor-Like Protein 1 in Young Age, Which May Lead to Poor Memory Retention in Old Age. Unno K, Takagi Y, Konishi T, Suzuki M, Miyake A, Kurotaki T, Hase T, Meguro S, Shimada A, Hasegawa-Ishii S, Pervin M, Taguchi K, Nakamura Y., Free PMC Article | 02/20/2021 |
APLP1 exhibits synaptogenic activity, involving trans-synaptic dimerization. APLP1 knock-out mice show impaired basal transmission and a reduced mEPSC frequency. | APLP1 Is a Synaptic Cell Adhesion Molecule, Supporting Maintenance of Dendritic Spines and Basal Synaptic Transmission. Schilling S, Mehr A, Ludewig S, Stephan J, Zimmermann M, August A, Strecker P, Korte M, Koo EH, Müller UC, Kins S, Eggert S., Free PMC Article | 07/1/2017 |
Results suggest that APLP1 deficiency on its own does not lead to defects in synaptic plasticity, but affects synaptic transmission and network inhibition in the dentate gyrus | Deletion of the amyloid precursor-like protein 1 (APLP1) enhances excitatory synaptic transmission, reduces network inhibition but does not impair synaptic plasticity in the mouse dentate gyrus. Vnencak M, Paul MH, Hick M, Schwarzacher SW, Del Turco D, Müller UC, Deller T, Jedlicka P. | 02/27/2016 |
[review] A role of APP and its two closely related homologues APLP1 and APLP2 has been determined in various aspects of nervous system development and function, in particular, for synapse formation and function. | Functions of the APP gene family in the nervous system: insights from mouse models. Aydin D, Weyer SW, Müller UC. | 12/22/2012 |
findings demonstrated that NB-2 interacts with APLP and that both NB-2 and APLP1 are localized at presynaptic sites, suggesting that NB-2 associates with APLP1 in a cis manner on the presynaptic membrane | A cis-complex of NB-2/contactin-5 with amyloid precursor-like protein 1 is localized on the presynaptic membrane. Shimoda Y, Koseki F, Itoh M, Toyoshima M, Watanabe K. | 06/30/2012 |
Crystal structure of the E2 domain of amyloid precursor protein-like protein 1 in complex with sucrose octasulfate. | Crystal structure of the E2 domain of amyloid precursor protein-like protein 1 in complex with sucrose octasulfate. Xue Y, Lee S, Wang Y, Ha Y., Free PMC Article | 10/22/2011 |
The results demonstrated that cell viability and neurite outgrowth of N2a cells undergoing knockdown of Aplp1 were significantly reduced, compared with N2a cells undergoing knockdown of either App or Aplp2. | Gene silencing analyses against amyloid precursor protein (APP) gene family by RNA interference. Sakai T, Hohjoh H. | 01/21/2010 |
Cytoplasmic polyadenylation element (CPE) binding factor binds the small intracellular domain (ICD) of APLP1. | Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation. Cao Q, Huang YS, Kan MC, Richter JD., Free PMC Article | 01/21/2010 |
The 5' UTR of the Aplp1 gene lacks any type of CAGA box. This may explain its inability to form amyloid plaques. | Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease. Maloney B, Ge YW, Greig N, Lahiri DK. | 01/21/2010 |