Benilova et al., 2012 - Google Patents
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothesBenilova et al., 2012
- Document ID
- 9351137792106899267
- Author
- Benilova I
- Karran E
- De Strooper B
- Publication year
- Publication venue
- Nature neuroscience
External Links
Snippet
The'toxic Aβ oligomer'hypothesis has attracted considerable attention among Alzheimer's disease researchers as a way of resolving the lack of correlation between deposited amyloid- β (Aβ) in amyloid plaques—in terms of both amount and location—and cognitive impairment …
- 206010001897 Alzheimer's disease 0 title abstract description 56
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2821—Alzheimer
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2828—Prion diseases
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
- G01N33/558—Immunoassay; Biospecific binding assay using diffusion or migration of antigen or antibody
- G01N33/561—Immunoelectrophoresis
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2835—Movement disorders, e.g. Parkinson, Huntington, Tourette
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Benilova et al. | The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes | |
| Lau et al. | α-Synuclein strains target distinct brain regions and cell types | |
| Aoyagi et al. | Aβ and tau prion-like activities decline with longevity in the Alzheimer’s disease human brain | |
| Fujita et al. | HMGB1, a pathogenic molecule that induces neurite degeneration via TLR4-MARCKS, is a potential therapeutic target for Alzheimer’s disease | |
| Morozova et al. | Conformational features of tau fibrils from Alzheimer’s disease brain are faithfully propagated by unmodified recombinant protein | |
| Altay et al. | Prominent astrocytic alpha-synuclein pathology with unique post-translational modification signatures unveiled across Lewy body disorders | |
| Sakono et al. | Amyloid oligomers: formation and toxicity of Aβ oligomers | |
| Thibaudeau et al. | A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers | |
| Mok et al. | Mapping interactions with the chaperone network reveals factors that protect against tau aggregation | |
| Oikawa et al. | α-Synuclein fibrils exhibit gain of toxic function, promoting tau aggregation and inhibiting microtubule assembly | |
| Jin et al. | Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration | |
| Jayaraman et al. | Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties | |
| Hong et al. | Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes | |
| Musunuri et al. | Quantification of the brain proteome in Alzheimer’s disease using multiplexed mass spectrometry | |
| Verghese et al. | ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions | |
| Gilbert | Republished: the role of amyloid β in the pathogenesis of Alzheimer’s disease | |
| Tseng et al. | The deacetylase HDAC6 mediates endogenous neuritic tau pathology | |
| Pradeepkiran et al. | Amyloid-β and phosphorylated tau are the key biomarkers and predictors of Alzheimer’s disease | |
| Dinkel et al. | Variations in filament conformation dictate seeding barrier between three-and four-repeat tau | |
| Velasco et al. | Synapse-binding subpopulations of Aβ oligomers sensitive to peptide assembly blockers and scFv antibodies | |
| Vosough et al. | Characterization of homogeneous and heterogeneous amyloid-β42 oligomer preparations with biochemical methods and infrared spectroscopy reveals a correlation between infrared spectrum and oligomer size | |
| Szczepankiewicz et al. | N-terminal extensions retard Aβ42 fibril formation but allow cross-seeding and coaggregation with Aβ42 | |
| Amijee et al. | The N-methylated peptide SEN304 powerfully inhibits Aβ (1–42) toxicity by perturbing oligomer formation | |
| Vadukul et al. | α-Synuclein aggregation is triggered by oligomeric amyloid-β 42 via heterogeneous primary nucleation | |
| Sergeant et al. | Progressive decrease of amyloid precursor protein carboxy terminal fragments (APP‐CTFs), associated with tau pathology stages, in Alzheimer's disease |