The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain.
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A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize ironAlzheimer's disease as homeostatic responses to age-related myelin breakdownQuantitative modelling of amyloidogenic processing and its influence by SORLA in Alzheimer's diseaseIron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's diseaseHomo- and heterodimerization of APP family members promotes intercellular adhesion.The amyloid-beta precursor protein: integrating structure with biological functionStructure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor proteinThe amyloid precursor protein: beyond amyloidAmyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta poresThe Neuroprotective Properties of the Amyloid Precursor Protein Following Traumatic Brain InjuryCaenorhabditis elegans as a model organism to study APP functionAlzheimer's disease--a panorama glimpseAmyloid β precursor protein as a molecular target for amyloid β--induced neuronal degeneration in Alzheimer's diseaseThe Crystal Structure of the Heparin-Binding Reelin-N Domain of F-SpondinStructural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding SiteThe E2 Domains of APP and APLP1 Share a Conserved Mode of DimerizationCrystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose OctasulfateCrystal structure of amyloid precursor-like protein 1 and heparin complex suggests a dual role of heparin in E2 dimerizationStructural aspects and physiological consequences of APP/APLP trans-dimerization.APP processing in Alzheimer's diseaseProteolytic processing of Alzheimer's β-amyloid precursor proteinPeptides of presenilin-1 bind the amyloid precursor protein ectodomain and offer a novel and specific therapeutic approach to reduce ß-amyloid in Alzheimer's diseaseNeuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers.Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics.GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.The structural biology of the amyloid precursor protein APP - a complex puzzle reveals its multi-domain architecture.Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GxxxG motif.Amyloid precursor protein mediates a tyrosine kinase-dependent activation response in endothelial cells.ADAM10 missense mutations potentiate β-amyloid accumulation by impairing prodomain chaperone functionWhat is the role of amyloid precursor protein dimerization?Copper binding to the Alzheimer's disease amyloid precursor proteinAmyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization.Altering APP proteolysis: increasing sAPPalpha production by targeting dimerization of the APP ectodomainLowering of amyloid beta peptide production with a small molecule inhibitor of amyloid-β precursor protein dimerizationThe "CPC clip motif": a conserved structural signature for heparin-binding proteins.Brain endothelial cells produce amyloid {beta} from amyloid precursor protein 770 and preferentially secrete the O-glycosylated formPresynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis.Analysis of the overall structure of the multi-domain amyloid precursor protein (APP).The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation.
P2860
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P2860
The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain.
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The X-ray structure of an anti ...... d precursor protein E2 domain.
@ast
The X-ray structure of an anti ...... d precursor protein E2 domain.
@en
The X-ray structure of an anti ...... d precursor protein E2 domain.
@nl
type
label
The X-ray structure of an anti ...... d precursor protein E2 domain.
@ast
The X-ray structure of an anti ...... d precursor protein E2 domain.
@en
The X-ray structure of an anti ...... d precursor protein E2 domain.
@nl
prefLabel
The X-ray structure of an anti ...... d precursor protein E2 domain.
@ast
The X-ray structure of an anti ...... d precursor protein E2 domain.
@en
The X-ray structure of an anti ...... d precursor protein E2 domain.
@nl
P1433
P1476
The X-ray structure of an anti ...... d precursor protein E2 domain.
@en
P2093
P304
P356
10.1016/J.MOLCEL.2004.06.037
P577
2004-08-01T00:00:00Z