Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia
about
CLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXVRegulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2bThe α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b)The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta productionBRI2 interacts with amyloid precursor protein (APP) and regulates amyloid beta (Abeta) productionBRI2 (ITM2b) inhibits Abeta deposition in vivoBeta-amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furinFurin at the cutting edge: from protein traffic to embryogenesis and diseaseA decamer duplication in the 3' region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindredEvidence that assembly of an active gamma-secretase complex occurs in the early compartments of the secretory pathwayRegional distribution of amyloid-Bri deposition and its association with neurofibrillary degeneration in familial British dementiaGeneration and initial characterization of FDD knock in miceSystemic amyloid deposits in familial British dementia.Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation.Modeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease.Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilizationAmyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins.Chromosome 13 dementia syndromes as models of neurodegeneration.PYROGLUTAMATE FORMATION AT THE N-TERMINI OF ABRI MOLECULES IN FAMILIAL BRITISH DEMENTIA IS NOT RESTRICTED TO THE CENTRAL NERVOUS SYSTEM.Genetic alterations of the BRI2 gene: familial British and Danish dementias.Increased tau phosphorylation and tau truncation, and decreased synaptophysin levels in mutant BRI2/tau transgenic mice.Therapeutic strategies for human amyloid diseases.Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10.Furin-mediated processing in the early secretory pathway: sequential cleavage and degradation of misfolded insulin receptors.Mitochondrial dysfunction induced by a post-translationally modified amyloid linked to a familial mutation in an alternative model of neurodegeneration.The Familial British Dementia Mutation Promotes Formation of Neurotoxic Cystine Cross-linked Amyloid Bri (ABri) OligomersNeurodegeneration caused by proteins with an aberrant carboxyl-terminus.Lessons from a Rare Familial Dementia: Amyloid and Beyond.The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function.Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis.Oxidative stress and mitochondria-mediated cell death mechanisms triggered by the familial Danish dementia ADan amyloidModeling familial British dementia in transgenic mice.Abundant pyroglutamate-modified ABri and ADan peptides in extracellular and vascular amyloid deposits in familial British and Danish dementias.Cerebral amyloid angiopathy and parenchymal amyloid deposition in transgenic mice expressing the Danish mutant form of human BRI2.Amyloidogenesis of natively unfolded proteins.BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate.BRI2 homodimerizes with the involvement of intermolecular disulfide bonds.Expression of BRI2 mRNA and protein in normal human brain and familial British dementia: its relevance to the pathogenesis of diseaseBRI2 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?
P2860
Q24292980-04E84832-90E5-4155-BA94-ACC23E96CAFFQ24298773-31BEDA53-24C0-4718-9B22-6F06D092C732Q24300479-892B503D-6109-49AA-9937-AB0A36540AA5Q24306233-1B2E0E47-24EB-4EA8-BC27-F2F9F95629BFQ24308675-AFAD77FA-D53A-49F5-ABA8-2A0345102849Q24319041-F34D5E92-CFB8-41F3-ABC5-1584449B3CBBQ24323262-94140E31-65DF-4610-99F7-C8F49AB357AEQ24670432-3F0D11D9-5F40-4AC2-81C4-E3E867144055Q24675956-AFC659DF-92FD-40B7-B0D4-EB7EB7088620Q28285387-4701563D-724F-402F-A157-11C67587A0FBQ28346149-5594F5EA-3C89-44D4-8C5A-34A7EC2907ADQ28750248-2FB1D4EA-61DB-42E6-804E-18AC0DA618F2Q30718374-86E286E6-CECC-4E1F-8BCF-ACC5E13E0183Q31807323-542B31B5-AF66-4822-8FB8-5BDDAB702955Q33842635-A133F549-B459-472E-9A1A-D888ADD540BEQ34078036-C5FAAA0A-3245-4751-92C3-91615D747C1DQ34083143-F0FFE5FE-AE84-4A1C-9CAA-B8B556F80647Q34109391-D8D8863D-EB7B-483C-8763-DFD8EB901561Q34243914-AF48365A-BF58-46C7-A5F6-B296080142B3Q34513577-170C04F4-93D0-4C5E-A5E6-B2EB32727B87Q34590082-8B1C8AA2-ECDE-48FC-BEEB-DC1E217ECFFDQ34743288-DB186DFB-D1FB-41F7-BF10-F77DF97AC0A2Q35197818-11A8DC68-49F2-4A1F-93F1-9C6F024A6A3BQ35346533-7C2E83EF-C5AF-4EF5-BDB8-C9E8BC811B12Q35679473-A7C3C2C7-E283-4D24-BF74-A3E764CD2880Q35860467-443B36F1-C41A-4DD5-94BD-94FA53E61DA7Q35871644-EF14EBFF-2026-4C20-8622-AE491EF5FCF5Q36082628-569917C5-1C7F-4DCC-8E67-CB5A23913B0AQ36257261-C724EE0E-F4E8-4B54-A587-2F6991C630F4Q36323476-52EDE5B5-FEE5-49DE-B438-94AE0603A62CQ36396174-6909E38B-20C1-41C1-A525-14681CD8EE02Q36448525-7D9D8710-7EDD-4F31-9943-3F3392697FECQ36605288-AF939121-04F9-4D0C-8562-C1DAE71C265CQ37019428-9AA80574-9CBE-43CC-B7DD-6FE0F4B877F8Q37184755-73063772-9CDA-40B6-90C0-FC1222180F21Q37352319-4C42B263-A169-4D8F-AAFD-6772A8771CB6Q37440201-16D8145E-179C-4D02-AD7C-088E3D2F69F8Q37481580-60326241-1E4C-4A28-9976-E53DA47BC8D9Q37638750-090C5956-6C23-4453-B515-A7F48DF1CEE3Q37888775-1A53E6BA-5CD6-4C63-8970-636AC745AF05
P2860
Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Furin mediates enhanced produc ...... s in familial British dementia
@ast
Furin mediates enhanced produc ...... s in familial British dementia
@en
Furin mediates enhanced produc ...... s in familial British dementia
@en-gb
Furin mediates enhanced produc ...... s in familial British dementia
@nl
type
label
Furin mediates enhanced produc ...... s in familial British dementia
@ast
Furin mediates enhanced produc ...... s in familial British dementia
@en
Furin mediates enhanced produc ...... s in familial British dementia
@en-gb
Furin mediates enhanced produc ...... s in familial British dementia
@nl
prefLabel
Furin mediates enhanced produc ...... s in familial British dementia
@ast
Furin mediates enhanced produc ...... s in familial British dementia
@en
Furin mediates enhanced produc ...... s in familial British dementia
@en-gb
Furin mediates enhanced produc ...... s in familial British dementia
@nl
P2093
P921
P356
P1433
P1476
Furin mediates enhanced produc ...... s in familial British dementia
@en
P2093
D F Steiner
G Thinakaran
S C Meredith
S S Sisodia
P2888
P304
P356
10.1038/14783
P407
P577
1999-11-01T00:00:00Z
P5875
P6179
1006022144