The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation

The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation

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Homo- and heterodimerization of APP family members promotes intercellular adhesion.Amyloid precursor protein and amyloid precursor-like protein 2 in cancer Platelets and Alzheimer's disease: Potential of APP as a biomarker Structural aspects and physiological consequences of APP/APLP trans-dimerization.Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members The normal and pathologic roles of the Alzheimer's β-secretase, BACE1 BACE1-/- mice exhibit seizure activity that does not correlate with sodium channel level or axonal localization Regulation of amyloid precursor protein processing by the Beclin 1 complex Pharmacological analysis of Drosophila melanogaster gamma-secretase with respect to differential proteolysis of Notch and APP.beta-Secretase cleavage is not required for generation of the intracellular C-terminal domain of the amyloid precursor family of proteins.The secretases: enzymes with therapeutic potential in Alzheimer disease.Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer's disease Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and γ-secretase.Molecular Differences and Similarities Between Alzheimer's Disease and the 5XFAD Transgenic Mouse Model of Amyloidosis.Β-site APP-cleaving enzyme 1 trafficking and Alzheimer's disease pathogenesis.Deletion of the amyloid precursor-like protein 2 (APLP2) does not affect hippocampal neuron morphology or function.PAT1a modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2.Pathological and physiological functions of presenilins.Turnover of amyloid precursor protein family members determines their nuclear signaling capability APP and APLP2 are essential at PNS and CNS synapses for transmission, spatial learning and LTP.An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer's disease.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Abeta induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597-624)An NSAID-like compound, FT-9, preferentially inhibits gamma-secretase cleavage of the amyloid precursor protein compared to its effect on amyloid precursor-like protein 1.The Amyloid Precursor Protein of Alzheimer's Disease Clusters at the Organelle/Microtubule Interface on Organelles that Bind Microtubules in an ATP Dependent Manner.The 28-amino acid form of an APLP1-derived Abeta-like peptide is a surrogate marker for Abeta42 production in the central nervous system.Genetic and molecular aspects of Alzheimer's disease shed light on new mechanisms of transcriptional regulation.Label-free Quantitative Proteomics of Mouse Cerebrospinal Fluid Detects β-Site APP Cleaving Enzyme (BACE1) Protease Substrates In Vivo A correlativity study of plasma APL1β28 and clusterin levels with MMSE/MoCA/CASI in aMCI patients.Second generation γ-secretase modulators exhibit different modulation of Notch β and Aβ production.Development of beta-amyloid-induced neurodegeneration in Alzheimer's disease and novel neuroprotective strategies.Relevance of amyloid precursor-like protein 2 C-terminal fragments in pancreatic cancer cells.The amyloid precursor protein (APP) family members are key players in S-adenosylmethionine formation by MAT2A and modify BACE1 and PSEN1 gene expression-relevance for Alzheimer's disease.APLP1 as a cerebrospinal fluid biomarker for γ-secretase modulator treatment Nicastrin functions to sterically hinder γ-secretase-substrate interactions driven by substrate transmembrane domain A single dose of the γ-secretase inhibitor semagacestat alters the cerebrospinal fluid peptidome in humans.Secreted APP regulates the function of full-length APP in neurite outgrowth through interaction with integrin beta1.Is the amyloid hypothesis of Alzheimer's disease therapeutically relevant?Reduced amyloidogenic processing of the amyloid beta-protein precursor by the small-molecule Differentiation Inducing Factor-1 Structure-activity relationship of memapsin 2: implications on physiological functions and Alzheimer's disease

P2860

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P2860

The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation

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