In vitro characterization of Pittsburgh compound-B binding to Lewy bodies. (Q46979979)

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8 January 2020

title

In vitro characterization of Pittsburgh compound-B binding to Lewy bodies (English)

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author name string

Michelle T Fodero-Tavoletti

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Paul A Adlard

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Kevin J Barnham

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Lisa E Foster

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Laura Leone

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Keyla Perez

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Mikhalina Cortés

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Janetta G Culvenor

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8 January 2020

Qiao-Xin Li

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Katrina M Laughton

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Christopher C Rowe

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Victor L Villemagne

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Colin L Masters

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language of work or name

English

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publication date

1 September 2007

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8 January 2020

published in

Journal of Neuroscience

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volume

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issue

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page(s)

10365-10371

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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

8 January 2020

cites work

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Non-Abeta component of Alzheimer's disease amyloid (NAC) revisited. NAC and alpha-synuclein are not associated with Abeta amyloid.

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Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid

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Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro

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Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain

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Structure determination of micelle-like intermediates in amyloid beta -protein fibril assembly by using small angle neutron scattering

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A lipophilic thioflavin-T derivative for positron emission tomography (PET) imaging of amyloid in brain

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Visual hallucinations in Lewy body disease relate to Lewy bodies in the temporal lobe

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Qualitative performance characteristics differentiate dementia with Lewy bodies and Alzheimer's disease.

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The binding of 2-(4'-methylaminophenyl)benzothiazole to postmortem brain homogenates is dominated by the amyloid component.

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Synthesis and evaluation of 11C-labeled 6-substituted 2-arylbenzothiazoles as amyloid imaging agents

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Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: a pilot phase 2 clinical trial

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Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound-B

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APP intracellular domain is increased and soluble Abeta is reduced with diet-induced hypercholesterolemia in a transgenic mouse model of Alzheimer disease

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Cytoplasmic domain of the beta-amyloid protein precursor of Alzheimer's disease: function, regulation of proteolysis, and implications for drug development

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Effects of Abeta immunization (AN1792) on MRI measures of cerebral volume in Alzheimer disease.

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Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway

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Molecular, structural, and functional characterization of Alzheimer's disease: evidence for a relationship between default activity, amyloid, and memory

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Binding of the positron emission tomography tracer Pittsburgh compound-B reflects the amount of amyloid-beta in Alzheimer's disease brain but not in transgenic mouse brain.

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Overexpression of Abeta is associated with acceleration of onset of motor impairment and superoxide dismutase 1 aggregation in an amyotrophic lateral sclerosis mouse model

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Diffuse Lewy body disease: light and electron microscopic immunocytochemistry of senile plaques.

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Media from rhabdomyosarcoma and neuroblastoma cell cultures stimulate in vitro aggregation and fibrillization of amyloid beta-protein

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Observation of metastable Abeta amyloid protofibrils by atomic force microscopy

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Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate.

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Consensus recommendations for the postmortem diagnosis of Alzheimer's disease. The National Institute on Aging, and Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer's Disease

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Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.

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Lewy bodies contain altered alpha-synuclein in brains of many familial Alzheimer's disease patients with mutations in presenilin and amyloid precursor protein genes

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10.1523/JNEUROSCI.0630-07.2007

Identifiers

DOI

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8 January 2020

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PubMed publication ID

17898208

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