BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper.
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Disturbed copper bioavailability in Alzheimer's diseaseCopper metallochaperonesDeficiency of the copper chaperone for superoxide dismutase increases amyloid-β productionCalsyntenin-1 shelters APP from proteolytic processing during anterograde axonal transport.Copper regulates cyclic-AMP-dependent lipolysis"Pulling the plug" on cellular copper: the role of mitochondria in copper export.Metals and cholesterol: two sides of the same coin in Alzheimer's disease pathology.Chronic copper exposure exacerbates both amyloid and tau pathology and selectively dysregulates cdk5 in a mouse model of ADCopper binding to the Alzheimer's disease amyloid precursor proteinBeta-secretase: structure, function, and evolution.The risks of copper toxicity contributing to cognitive decline in the aging population and to Alzheimer's disease.Presenilins promote the cellular uptake of copper and zinc and maintain copper chaperone of SOD1-dependent copper/zinc superoxide dismutase activity.SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer diseaseThe Alzheimer's disease beta-secretase enzyme, BACE1.Amyloid precursor protein and BACE function as oligomers.Links between copper and cholesterol in Alzheimer's disease.The Basic Biology of BACE1: A Key Therapeutic Target for Alzheimer's Disease.Therapeutics for Alzheimer's disease based on the metal hypothesisTrientine reduces BACE1 activity and mitigates amyloidosis via the AGE/RAGE/NF-κB pathway in a transgenic mouse model of Alzheimer's disease.X11beta rescues memory and long-term potentiation deficits in Alzheimer's disease APPswe Tg2576 mice.The consequences of mitochondrial amyloid beta-peptide in Alzheimer's disease.The role of metallobiology and amyloid-β peptides in Alzheimer's disease.Biological metals and metal-targeting compounds in major neurodegenerative diseases.RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of beta-secretase BACE1 in vitro.The secret life of extracellular vesicles in metal homeostasis and neurodegeneration.Potentiating role of copper on spatial memory deficit induced by beta amyloid and evaluation of mitochondrial function markers in the hippocampus of rats.The Mechanisms of Action of Curcumin in Alzheimer's Disease.Orchestration of dynamic copper navigation - new and missing pieces.Down-regulation of endogenous amyloid precursor protein processing due to cellular aging.Phosphorylation of FE65 Ser610 by serum- and glucocorticoid-induced kinase 1 modulates Alzheimer's disease amyloid precursor protein processing.Effect of Metal Chelators on γ-Secretase Indicates That Calcium and Magnesium Ions Facilitate Cleavage of Alzheimer Amyloid Precursor Substrate.Spectroscopic characterization of copper(I) binding to apo and metal-reconstituted zinc finger peptides.The influence of protein folding on the copper affinities of trafficking and target sites.GULP1/CED-6 ameliorates amyloid-β toxicity in a Drosophila model of Alzheimer's disease.Full-length cellular β-secretase has a trimeric subunit stoichiometry, and its sulfur-rich transmembrane interaction site modulates cytosolic copper compartmentalization.Characterization of the role of metallothionein-3 in an animal model of Alzheimer's disease.GULP1 is a novel APP-interacting protein that alters APP processing.O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.Toxicity of Alzheimer's disease-associated Aβ peptide is ameliorated in a Drosophila model by tight control of zinc and copper availability.Role of amyloid-β–metal interactions in Alzheimer’s disease
P2860
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P2860
BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
BACE1 cytoplasmic domain inter ...... dismutase-1 and binds copper.
@en
BACE1 cytoplasmic domain inter ...... dismutase-1 and binds copper.
@nl
type
label
BACE1 cytoplasmic domain inter ...... dismutase-1 and binds copper.
@en
BACE1 cytoplasmic domain inter ...... dismutase-1 and binds copper.
@nl
prefLabel
BACE1 cytoplasmic domain inter ...... dismutase-1 and binds copper.
@en
BACE1 cytoplasmic domain inter ...... dismutase-1 and binds copper.
@nl
P2093
P2860
P50
P356
P1476
BACE1 cytoplasmic domain inter ...... e dismutase-1 and binds copper
@en
P2093
Barbara Angeletti
Christopher Dennison
Colin Dingwall
Hinayana Bawagan
Ishrut Hussain
Katie B Freeman
Maria E Tennant
P2860
P304
17930-17937
P356
10.1074/JBC.M412034200
P407
P577
2005-02-18T00:00:00Z