The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.
about
Amyloid-β Receptors: The Good, the Bad, and the Prion ProteinInnate Immunity Fights Alzheimer's DiseaseThe Neurobiology and Age-Related Prevalence of the ε4 Allele of Apolipoprotein E in Alzheimer's Disease Cohorts.Neutral Sphingomyelinase-2 Deficiency Ameliorates Alzheimer's Disease Pathology and Improves Cognition in the 5XFAD MouseCerebrospinal fluid-induced retardation of amyloid β aggregation correlates with Alzheimer's disease and the APOE ε4 allele.Sortilin Fragments Deposit at Senile Plaques in Human CerebrumCSF beta-amyloid 1-42 - what are we measuring in Alzheimer's disease?APOE4 enhances age-dependent decline in cognitive function by down-regulating an NMDA receptor pathway in EFAD-Tg mice.ApoE4-specific Misfolded Intermediate Identified by Molecular Dynamics Simulations.Differential interaction of Apolipoprotein-E isoforms with insulin receptors modulates brain insulin signaling in mutant human amyloid precursor protein transgenic miceAntibiotic-induced perturbations in gut microbial diversity influences neuro-inflammation and amyloidosis in a murine model of Alzheimer's disease.The Alzheimer's disease risk factors apolipoprotein E and TREM2 are linked in a receptor signaling pathwayStudy of Exosomes Shed New Light on Physiology of Amyloidogenesis.Apolipoprotein E and Alzheimer's disease: the influence of apolipoprotein E on amyloid-β and other amyloidogenic proteins.Apolipoprotein E, Receptors, and Modulation of Alzheimer's Disease.Targeting Apolipoprotein E/Amyloid β Binding by Peptoid CPO_Aβ17-21 P Ameliorates Alzheimer's Disease Related Pathology and Cognitive Decline.The role of histidines in amyloid β fibril assembly.ApoE: the role of conserved residues in defining functionHelical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry.Ligand-Receptor Interaction Modulates the Energy Landscape of Enzyme-Instructed Self-Assembly of Small Molecules.Atomistic Insights into Structural Differences between E3 and E4 Isoforms of Apolipoprotein E.Cerebrospinal Fluid Proteins as Regulators of Beta-amyloid Aggregation and Toxicity.Hidden heterogeneity in Alzheimer's disease: Insights from genetic association studies and other analyses.Molecular Mechanisms of the R61T Mutation in Apolipoprotein E4: A Dynamic Rescue.Self-assembled lipoprotein based gold nanoparticles for detection and photothermal disaggregation of β-amyloid aggregates.Quantitative Characterization of Metastability and Heterogeneity of Amyloid Aggregates.The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.
P2860
Q26771532-26FDACC3-2CA9-4132-A971-3B306CE0793EQ28081826-FB6E2117-914B-4612-8B3E-6F50923DCAACQ30248596-D03C51C9-EA0C-4A19-8B3B-957F15155F4CQ30363059-03C769C5-BD92-4E1A-AC43-26BADF6DCCE7Q33363912-8E77F688-CA4D-4358-9955-48BC13CD8A95Q33770251-F75102AA-4C2B-439A-8755-7ADF5F283883Q35115904-25A2863E-99A6-4A3D-88C7-459781257A34Q35337169-52F5094F-BE09-4CCD-AA51-78A800B28E84Q35823248-95B00A3E-BCA7-4C6B-9871-C071D1A69E72Q36034035-27EC82F2-2840-4742-8646-F0848678FE3EQ37116609-46C9BEFA-7230-47DB-B5A7-3102FBD4CB1EQ38711499-0B623530-A12B-4C37-9E6A-DC0F73A309E8Q38777380-A55EF41B-0F85-4F48-A83E-44A71DA6EA51Q39155261-3F7288F8-0411-4A88-97FD-71DF033146CEQ39257249-5695184B-B8A6-42C8-A90C-C7E94B4A85FCQ41387476-B49DE7B1-657B-4E77-B5C2-9ACED905E4E5Q42090533-96A1C3B4-33F7-485E-B709-76DB8E8EEA42Q42185078-51FCEA22-3A12-48E5-939F-BAB7DE7EF960Q42323951-507398A4-DC19-4D22-84B3-A01FCDB7DDEEQ42972601-D3649D0B-17A9-40F7-885A-262AB558F379Q47270627-FDA2F526-5B4D-414B-A3E5-9B7FD51328F0Q47356578-FF3EEB78-8B99-44B9-8175-CBBA908A7A8FQ47625969-475C7FEC-C258-49AB-8A49-5BBD3185608FQ47794190-680ED994-0844-4DB1-89A5-AE9CD5AEBBAFQ48341341-655EFB44-4059-479F-8976-BD939F9E3DDCQ51766678-13731AFB-B6A7-44D5-91CC-A551EB73C5F2Q54977832-0B9ACA27-A86D-4B45-87E4-279FD7DA2843
P2860
The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.
description
2014 nî lūn-bûn
@nan
2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The binding of apolipoprotein ...... netics of amyloid aggregation.
@ast
The binding of apolipoprotein ...... netics of amyloid aggregation.
@en
type
label
The binding of apolipoprotein ...... netics of amyloid aggregation.
@ast
The binding of apolipoprotein ...... netics of amyloid aggregation.
@en
prefLabel
The binding of apolipoprotein ...... netics of amyloid aggregation.
@ast
The binding of apolipoprotein ...... netics of amyloid aggregation.
@en
P2093
P2860
P3181
P356
P1433
P1476
The binding of apolipoprotein ...... netics of amyloid aggregation.
@en
P2093
Berevan Baban
Carl Frieden
Kanchan Garai
Philip B Verghese
P2860
P304
P3181
P356
10.1021/BI5008172
P407
P577
2014-09-25T00:00:00Z