scholarly journals In a pre‐pivotal diagnostic study, β‐amyloid plaque detection in the lens of the eye in MCI and mild AD patients was used to classify subjects as normal, MCI, and mild AD using Sapphire II

2020 ◽  
Vol 16 (S5) ◽  
Author(s):  
Newman Knowlton ◽  
Suzanne B. Hendrix ◽  
Susanne Wilke ◽  
Dennis Nilan
Keyword(s):  
Amyloid Plaque ◽  
Diagnostic Study ◽  
Β Amyloid ◽  
Plaque Detection

scholarly journals Radioiodinated aza-diphenylacetylenes as potential SPECT imaging agents for β-amyloid plaque detection

2007 ◽  
Vol 17 (13) ◽  
pp. 3581-3584 ◽  
Author(s):  
Wenchao Qu ◽  
Mei-Ping Kung ◽  
Catherine Hou ◽  
Lee-Way Jin ◽  
Hank F. Kung
Keyword(s):  
Amyloid Plaque ◽  
Spect Imaging ◽  
Imaging Agents ◽  
Β Amyloid ◽  
Plaque Detection

Novel imaging agents for β-amyloid plaque based on the N-benzoylindole core

2011 ◽  
Vol 21 (18) ◽  
pp. 5594-5597 ◽  
Author(s):  
Yang Yang ◽  
Xin-Hong Duan ◽  
Jun-Yuan Deng ◽  
Bing Jin ◽  
Hong-Mei Jia ◽  
...  
Keyword(s):  
Amyloid Plaque ◽  
Imaging Agents ◽  
Β Amyloid

scholarly journals New Biochemical Insights to Unravel the Pathogenesis of Alzheimer's Lesions

1991 ◽  
Vol 18 (S3) ◽  
pp. 408-410 ◽  
Author(s):  
Alex E. Roher ◽  
Kenneth C. Palmer ◽  
John Capodilupo ◽  
Arun R. Wakade ◽  
Melvyn J. Ball
Keyword(s):  
Amyloid Plaque ◽  
Extracellular Proteins ◽  
High Yield ◽  
Chemical Fractionation ◽  
Core Proteins ◽  
Β Amyloid ◽  
Neuritic Sprouting

ABSTRACT:Purification of amyloid plaque core proteins (APCP) from Alzheimer's disease brains to complete homogeneity and in high yield permitted its chemical fractionation and characterization of its components. APCP is mainly made of β-amyloid (βA) and an assortment of glycoproteins (accounting for 20%) rich in carbohydrates compatible with N-and O-linked saccharides. When added to tissue culture of sympathetic and sensory neurons APCP and βA inhibited neuritic sprouting, a reversible phenomenon at low doses. Higher concentrations of both substances kill the neurons in culture. APCP is significantly more toxic than βA, suggesting the minor components may play an important role in increasing the toxicity of βA. If the observed toxic effects of APCP in situ are occurring in vivo during the course of AD, then the accumulation of these extracellular proteins could be largely responsible for some of the neuronal death observed in this neuropathology.

Targeted Intraparenchymal Delivery of Human NGF by Gene Transfer to the Primate Basal Forebrain for 3 Months Does Not Accelerate β-Amyloid Plaque Deposition

1998 ◽  
Vol 154 (2) ◽  
pp. 573-582 ◽  
Author(s):  
Mark H. Tuszynski ◽  
David E. Smith ◽  
Jeffrey Roberts ◽  
Heather McKay ◽  
Elliott Mufson
Keyword(s):  
Gene Transfer ◽  
Basal Forebrain ◽  
Amyloid Plaque ◽  
Plaque Deposition ◽  
Β Amyloid

scholarly journals Soluble P-tau217 reflects amyloid and tau pathology and mediates the association of amyloid with tau

2021 ◽  
Author(s):  
Niklas Mattsson-Carlgren ◽  
Shorena Janelidze ◽  
Randall Bateman ◽  
Ruben Smith ◽  
Erik Stomrud ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Medial Temporal Lobe ◽  
Amyloid Plaques ◽  
Amyloid Plaque ◽  
Amyloid Pet ◽  
Tau Pathology ◽  
Β Amyloid ◽  
Tau Pet ◽  
Disease Stages

Abstract Alzheimer’s disease is characterized by β-amyloid plaques and tau tangles. Plasma levels of phospho-tau217 (P-tau217) accurately differentiate Alzheimer’s disease dementia from other dementias, but it is unclear to what degree this reflects β-amyloid plaque accumulation, tau tangle accumulation, or both. In a cohort with post-mortem neuropathological data (N=88), both plaque and tangle density contributed independently to higher P-tau217. Several findings were replicated in a cohort with PET imaging (“BioFINDER-2”, N=426), where β-amyloid and tau PET were independently associated to P-tau217. P-tau217 correlated with β-amyloid PET (but not tau PET) in early disease stages, and with both β-amyloid and (more strongly) tau PET in late disease stages. Finally, P-tau217 mediated the association between β-amyloid and tau in both cohorts, especially for tau outside of the medial temporal lobe. These findings support the hypothesis that plasma P-tau217 is increased by both β-amyloid plaques and tau tangles and is congruent with the hypothesis that P-tau is involved in β-amyloid-dependent formation of neocortical tau tangles.

Does β-amyloid plaque formation cause structural injury to neuronal processes?

2005 ◽  
Vol 7 (1-2) ◽  
pp. 5-15 ◽  
Author(s):  
Adele Woodhouse ◽  
Adrian K. West ◽  
Jyoti A. Chuckowree ◽  
James C. Vickers ◽  
Tracey C. Dickson
Keyword(s):  
Amyloid Plaque ◽  
Plaque Formation ◽  
Neuronal Processes ◽  
Β Amyloid ◽  
Structural Injury

scholarly journals P2-245: A PRE-PIVOTAL STUDY: B-AMYLOID PLAQUE DETECTION IN THE LENS OF THE EYE IN MCI AND MILD AD - CORRELATON WITH AMYLOID PET SCANNING

2019 ◽  
Vol 15 ◽  
pp. P677-P677
Author(s):  
Carl H. Sadowsky ◽  
Daniel R. Vlock ◽  
Tersea Villena ◽  
Dennis Nilan ◽  
Richard Gill ◽  
...  
Keyword(s):  
Amyloid Plaque ◽  
Amyloid Pet ◽  
Pet Scanning ◽  
Pivotal Study ◽  
Plaque Detection

Novel anilinophthalimide derivatives as potential probes for β-amyloid plaque in the brain

2010 ◽  
Vol 18 (3) ◽  
pp. 1337-1343 ◽  
Author(s):  
Xin-Hong Duan ◽  
Jin-Ping Qiao ◽  
Yang Yang ◽  
Meng-Chao Cui ◽  
Jiang-Ning Zhou ◽  
...  
Keyword(s):  
Amyloid Plaque ◽  
Β Amyloid ◽  
The Brain
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