Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue. - Wikidata - wikimedia - TriplyDB

Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue.

Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue.

http://www.wikidata.org/entity/Q53207590

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Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory Biomarkers of Alzheimer's disease Cerebrospinal fluid and blood biomarkers in Alzheimer's disease Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution.Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity.Alzheimer disease models and human neuropathology: similarities and differences Amyloid and lipids in the pathology of Alzheimer disease.Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders Despite its role in assembly, methionine 35 is not necessary for amyloid beta-protein toxicity Potential therapeutic strategies for Alzheimer's disease targeting or beyond β-amyloid: insights from clinical trials Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.The biochemical aftermath of anti-amyloid immunotherapy.Secretases as therapeutic targets for the treatment of Alzheimer's disease.A distinct subfraction of Aβ is responsible for the high-affinity Pittsburgh compound B-binding site in Alzheimer's disease brain The pathogenic aβ43 is enriched in familial and sporadic Alzheimer disease Isolation and characterization of antibody fragments selective for toxic oligomeric tau Biochemical and morphological characterization of the AβPP/PS/tau triple transgenic mouse model and its relevance to sporadic Alzheimer's disease.Intracerebral Injection of Metal-Binding Domain of Aβ Comprising the Isomerized Asp7 Increases the Amyloid Burden in Transgenic Mice.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Advances on the understanding of the origins of synaptic pathology in AD.Amyloid precursor protein transgenic mouse models and Alzheimer's disease: understanding the paradigms, limitations, and contributions.Antibody responses, amyloid-beta peptide remnants and clinical effects of AN-1792 immunization in patients with AD in an interrupted trial.APP transgenic mice: their use and limitations.Aβ oligomer-induced synapse degeneration in Alzheimer's disease.Treatment strategies targeting amyloid β-protein.Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Effects of the amyloid precursor protein Glu693-->Gln 'Dutch' mutation on the production and stability of amyloid beta-protein.Diversity of Amyloid-beta Proteoforms in the Alzheimer's Disease Brain.Comparative pathobiology of β-amyloid and the unique susceptibility of humans to Alzheimer's disease Immunocytochemical evidence that the beta-protein precursor is an integral component of neurofibrillary tangles of Alzheimer's disease.Distribution and fluidizing action of soluble and aggregated amyloid beta-peptide in rat synaptic plasma membranes.The HHQK domain of beta-amyloid provides a structural basis for the immunopathology of Alzheimer's disease.Regional Multiple Pathology Scores Are Associated with Cognitive Decline in Lewy Body Dementias.Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease.Autoantibodies to redox-modified oligomeric Abeta are attenuated in the plasma of Alzheimer's disease patients.Amyloid-β Increases Activity of Proteasomes Capped with 19S and 11S Regulators.Slow degradation of aggregates of the Alzheimer's disease amyloid beta-protein by microglial cells.A sulfated proteoglycan aggregation factor mediates amyloid-beta peptide fibril formation and neurotoxicity.Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides.

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Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue.

http://www.wikidata.org/entity/Q53207590

description

1993 nî lūn-bûn

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1993年の論文

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1993年学术文章

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1993年学术文章

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1993年学术文章

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1993年学术文章

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1993年學術文章

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1993年學術文章

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name

Morphological and biochemical ...... lzheimer disease brain tissue.

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Morphological and biochemical ...... lzheimer disease brain tissue.

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Morphological and biochemical ...... lzheimer disease brain tissue.

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Morphological and biochemical ...... lzheimer disease brain tissue.

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Morphological and biochemical ...... lzheimer disease brain tissue.

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Morphological and biochemical ...... lzheimer disease brain tissue.

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J.1471-4159.1993.TB09834.X

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Journal of Neurochemistry

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Morphological and biochemical ...... lzheimer disease brain tissue.

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Ball MJ

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Greenberg BD

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Palmer KC

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Roher AE

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Yurewicz EC

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P2860

Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease

Senile plaque neurites in Alzheimer disease accumulate amyloid precursor protein

Amyloid plaque core protein in Alzheimer disease and Down syndrome

Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain

Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein.

Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease.

Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport.

Defined neurofilament, tau, and beta-amyloid precursor protein epitopes distinguish Alzheimer from non-Alzheimer senile plaques.

Cationic dyes reveal proteoglycans structurally integrated within the characteristic lesions of Alzheimer's disease.

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