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

Alzheimer's disease: β-amyloid plaque formation in human brain

Synapse ◽  
2011 ◽  
Vol 65 (12) ◽  
pp. 1289-1297 ◽  
Author(s):  
Philip Seeman ◽  
Neil Seeman
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Human Brain ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Β Amyloid

Prion protein (PrPc) promotes β-amyloid plaque formation

2005 ◽  
Vol 26 (8) ◽  
pp. 1177-1182 ◽  
Author(s):  
Katja Schwarze-Eicker ◽  
Kathy Keyvani ◽  
Nicole Görtz ◽  
David Westaway ◽  
Norbert Sachser ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Β Amyloid

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 Ube3a deficiency inhibits amyloid plaque formation in APPswe/PS1δE9 mouse model of Alzheimer’s disease

2017 ◽  
Vol 26 (20) ◽  
pp. 4042-4054 ◽  
Author(s):  
Brijesh Kumar Singh ◽  
Naman Vatsa ◽  
Vipendra Kumar ◽  
Shashi Shekhar ◽  
Ankit Sharma ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Mouse Model ◽  
Amyloid Plaque ◽  
Plaque Formation ◽  
Model Of Alzheimer’S Disease

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
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