Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. - Wikidata - wikimedia - TriplyDB

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.

http://www.wikidata.org/entity/Q36178075

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Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway Pro-inflammatory S100A8 and S100A9 proteins: self-assembly into multifunctional native and amyloid complexes The ER stress factor XBP1s prevents amyloid-beta neurotoxicity Immunization with amyloid-beta attenuates inclusion body myositis-like myopathology and motor impairment in a transgenic mouse model Overview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds Amyloid-β Receptors: The Good, the Bad, and the Prion Protein Insights into Mechanisms of Chronic Neurodegeneration Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics Microbial amyloids--functions and interactions within the host Alzheimer's therapeutics: translation of preclinical science to clinical drug development Diversity, biogenesis and function of microbial amyloids Dietary DHA supplementation in an APP/PS1 transgenic rat model of AD reduces behavioral and Aβ pathology and modulates Aβ oligomerization Hydrogen sulfide inhibits amyloid formation Crystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomers Atomic View of a Toxic Amyloid Small Oligomer REST and stress resistance in ageing and Alzheimer's disease Distinct α-synuclein strains differentially promote tau inclusions in neurons Coffee and caffeine potentiate the antiamyloidogenic activity of melatonin via inhibition of Aβ oligomerization and modulation of the Tau-mediated pathway in N2a/APP cells In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms Xanthene food dye, as a modulator of Alzheimer's disease amyloid-beta peptide aggregation and the associated impaired neuronal cell function.A foldamer-dendrimer conjugate neutralizes synaptotoxic β-amyloid oligomers Halogenation generates effective modulators of amyloid-Beta aggregation and neurotoxicity.Amyloid-β protofibrils: size, morphology and synaptotoxicity of an engineered mimic Loss of alpha7 nicotinic receptors enhances beta-amyloid oligomer accumulation, exacerbating early-stage cognitive decline and septohippocampal pathology in a mouse model of Alzheimer's disease.Large aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugation Extracellular and intraneuronal HMW-AbetaOs represent a molecular basis of memory loss in Alzheimer's disease model mouse Aβ40 oligomers identified as a potential biomarker for the diagnosis of Alzheimer's disease Formulation of a medical food cocktail for Alzheimer's disease: beneficial effects on cognition and neuropathology in a mouse model of the disease Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1 Monoclonal antibodies against Aβ42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain.Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Curcumin Pyrazole and its derivative (N-(3-Nitrophenylpyrazole) Curcumin inhibit aggregation, disrupt fibrils and modulate toxicity of Wild type and Mutant α-Synuclein Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living Cells A safe, blood-brain barrier permeable triphenylmethane dye inhibits amyloid-β neurotoxicity by generating nontoxic aggregates Structural classification of toxic amyloid oligomers TGF-β induces TIAF1 self-aggregation via type II receptor-independent signaling that leads to generation of amyloid β plaques in Alzheimer's disease.Toxic fibrillar oligomers of amyloid-β have cross-β structure.

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P2860

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.

http://www.wikidata.org/entity/Q36178075

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2007 nî lūn-bûn

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Fibril specific, conformation ...... ent in prefibrillar oligomers.

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Fibril specific, conformation ...... ent in prefibrillar oligomers.

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Molecular Neurodegeneration

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Carl W Cotman

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Charles G Glabe

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Elizabeth Head

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Floyd Sarsoza

http://www.w3.org/2001/XMLSchema#string

Jennifer L Thompson

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Jessica Wu

http://www.w3.org/2001/XMLSchema#string

Lawrence Margol

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Mihaela Necula

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Peter Butler

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Rakez Kayed

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P2860

Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins

Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease

Structural properties of Abeta protofibrils stabilized by a small molecule.

Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease.

Conformational Abs recognizing a generic amyloid fibril epitope.

The pathogenesis of senile plaques.

Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced beta-cell apoptosis in h-IAPP transgenic mice.

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1019247123

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