about
Unified theory of Alzheimer's disease (UTAD): implications for prevention and curative therapyTargeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeuticsAβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.APOE-modulated Aβ-induced neuroinflammation in Alzheimer's disease: current landscape, novel data, and future perspectiveReview of the Evidence that Transcranial Electromagnetic Treatment will be a Safe and Effective Therapeutic Against Alzheimer's DiseaseIs Apolipoprotein E4 an Important Risk Factor for Dementia in Persons with Down Syndrome?Caspase Cleaved Tau in Alzheimer's Disease: A Therapeutic Target Realized.Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.Genetically-controlled Vesicle-Associated Membrane Protein 1 expression may contribute to Alzheimer's pathophysiology and susceptibility.Amyloid β Oligomeric Species Present in the Lag Phase of Amyloid Formation.The keystone of Alzheimer pathogenesis might be sought in Aβ physiologyAmyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?Glycines from the APP GXXXG/GXXXA Transmembrane Motifs Promote Formation of Pathogenic Aβ Oligomers in CellsArabidopsis thaliana extracts optimized for polyphenols production as potential therapeutics for the APOE-modulated neuroinflammation characteristic of Alzheimer's disease in vitroDistinct prion-like strains of amyloid beta implicated in phenotypic diversity of Alzheimer's disease.Rapidly progressive Alzheimer's disease features distinct structures of amyloid-β.Dementia with Lewy Bodies: Molecular Pathology in the Frontal Cortex in Typical and Rapidly Progressive Forms.Yeast Model of Amyloid-β and Tau Aggregation in Alzheimer's Disease.Non-canonical soluble amyloid-beta aggregates and plaque buffering: controversies and future directions for target discovery in Alzheimer's disease.Rosetta Stone for Amyloid Fibrils: The Key Role of Ring-Like Oligomers in Amyloidogenesis.The potential inhibitory effect of β-casein on the aggregation and deposition of Aβ1-42 fibrils in Alzheimer's disease: insight from in-vitro and in-silico studies.Apolipoprotein E Related Co-Morbidities and Alzheimer's Disease.Advantages of Structure-Based Drug design Approaches in Neurological Disorders.Protein-Protein Interface and Disease: Perspective from Biomolecular Networks.Oleuropein aglycone and polyphenols from olive mill waste water ameliorate cognitive deficits and neuropathology.Modulation of the Aβ peptide aggregation pathway by KP1019 limits Aβ-associated neurotoxicity.Protein Phosphorylation is a Key Mechanism in Alzheimer's Disease.Amyloid beta: structure, biology and structure-based therapeutic development.The Polyphenol Oleuropein Aglycone Modulates the PARP1-SIRT1 Interplay: An In Vitro and In Vivo Study.Shear-Induced Amyloid Formation in the Brain: I. Potential Vascular and Parenchymal ProcessesGly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics.Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution.Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins.Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition.Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy.Studies for Improving a Rat Model of Alzheimer's Disease: Icv Administration of Well-Characterized β-Amyloid 1-42 Oligomers Induce Dysfunction in Spatial Memory.A human scFv antibody that targets and neutralizes high molecular weight pathogenic amyloid-β oligomers.Mitochondrial dysfunction in a transgenic mouse model expressing human amyloid precursor protein (APP) with the Arctic mutation.1,2,3,4,6-penta-O-galloyl-β-D-glucopyranose Binds to the N-terminal Metal Binding Region to Inhibit Amyloid β-protein Oligomer and Fibril Formation.
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
Amyloid β-protein oligomers and Alzheimer's disease.
@en
Amyloid β-protein oligomers and Alzheimer's disease.
@nl
type
label
Amyloid β-protein oligomers and Alzheimer's disease.
@en
Amyloid β-protein oligomers and Alzheimer's disease.
@nl
prefLabel
Amyloid β-protein oligomers and Alzheimer's disease.
@en
Amyloid β-protein oligomers and Alzheimer's disease.
@nl
P2860
P356
P1476
Amyloid β-protein oligomers and Alzheimer's disease.
@en
P2093
David B Teplow
P2860
P2888
P356
10.1186/ALZRT226
P407
P50
P577
2013-11-29T00:00:00Z
P5875
P6179
1012255093