BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate.
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CD74 interacts with APP and suppresses the production of AbetaBRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2APP is cleaved by Bace1 in pre-synaptic vesicles and establishes a pre-synaptic interactome, via its intracellular domain, with molecular complexes that regulate pre-synaptic vesicles functionsMolecular Mechanism for Cellular Response to β-Escin and Its Therapeutic ImplicationsDeletion of the γ-secretase subunits Aph1B/C impairs memory and worsens the deficits of knock-in mice modeling the Alzheimer-like familial Danish dementiaGeneration and initial characterization of FDD knock in miceSpecific chaperones and regulatory domains in control of amyloid formation.APP heterozygosity averts memory deficit in knockin mice expressing the Danish dementia BRI2 mutantModeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease.Identification of novel γ-secretase-associated proteins in detergent-resistant membranes from brain.Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficitsAn intracellular threonine of amyloid-β precursor protein mediates synaptic plasticity deficits and memory loss.Memory deficits due to familial British dementia BRI2 mutation are caused by loss of BRI2 function rather than amyloidosis.Identification of NEEP21 as a ß-amyloid precursor protein-interacting protein in vivo that modulates amyloidogenic processing in vitro.Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10.Memory deficits of British dementia knock-in mice are prevented by Aβ-precursor protein haploinsufficiency.Proteomic characterization of a mouse model of familial Danish dementia.β- but not γ-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia.Lessons from a Rare Familial Dementia: Amyloid and Beyond.Inhibition of γ-secretase worsens memory deficits in a genetically congruous mouse model of Danish dementia.Cerebral amyloidosis: amyloid subunits, mutants and phenotypes.Tyr682 in the Aβ-precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance.Caspase-9 mediates synaptic plasticity and memory deficits of Danish dementia knock-in mice: caspase-9 inhibition provides therapeutic protection.APP and APLP2 interact with the synaptic release machinery and facilitate transmitter release at hippocampal synapses.APP Receptor? To Be or Not To Be.Increased AβPP processing in familial Danish dementia patients.Interaction of ApoE3 and ApoE4 isoforms with an ITM2b/BRI2 mutation linked to the Alzheimer disease-like Danish dementia: Effects on learning and memoryAnimal models of human amyloidoses: are transgenic mice worth the time and trouble?BRI2 interacts with BACE1 and regulates its cellular levels by promoting its degradation and reducing its mRNA levels.BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?Abolishing Tau cleavage by caspases at Aspartate421 causes memory/synaptic plasticity deficits and pre-pathological Tau alterations.BRI2 protein regulates β-amyloid degradation by increasing levels of secreted insulin-degrading enzyme (IDE).The familial dementia gene revisited: a missense mutation revealed by whole-exome sequencing identifies ITM2B as a candidate gene underlying a novel autosomal dominant retinal dystrophy in a large family.A Greek Tragedy: The Growing Complexity of Alzheimer Amyloid Precursor Protein Proteolysis.The ITM2B (BRI2) gene is a target of BCL6 repression: Implications for lymphomas and neurodegenerative diseases.BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Amyloid Precursor Protein (APP) May Act as a Substrate and a Recognition Unit for CRL4CRBN and Stub1 E3 Ligases Facilitating Ubiquitination of Proteins Involved in Presynaptic Functions and NeurodegenerationMaturation of BRI2 generates a specific inhibitor that reduces APP processing at the plasma membrane and in endocytic vesiclesTransthyretin Suppresses Amyloid-β Secretion by Interfering with Processing of the Amyloid-β Protein Precursor
P2860
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P2860
BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
BRI2 inhibits amyloid beta-pep ...... f secretases to the substrate.
@en
BRI2 inhibits amyloid beta-pep ...... f secretases to the substrate.
@nl
type
label
BRI2 inhibits amyloid beta-pep ...... f secretases to the substrate.
@en
BRI2 inhibits amyloid beta-pep ...... f secretases to the substrate.
@nl
prefLabel
BRI2 inhibits amyloid beta-pep ...... f secretases to the substrate.
@en
BRI2 inhibits amyloid beta-pep ...... f secretases to the substrate.
@nl
P2093
P2860
P1476
BRI2 inhibits amyloid beta-pep ...... of secretases to the substrate
@en
P2093
Eileen M McGowan
Luca Giliberto
Shuji Matsuda
Yukiko Matsuda
P2860
P304
P356
10.1523/JNEUROSCI.2094-08.2008
P407
P577
2008-08-01T00:00:00Z