scholarly journals Therapeutic Treatment of Alzheimer's Disease Using Metal Complexing Agents

Author(s):  
Katherine A. Price ◽  
Peter J. Crouch ◽  
Anthony R. White
2009 ◽  
Vol 5 (2) ◽  
pp. 134-142 ◽  
Author(s):  
Laura Bica ◽  
Peter J. Crouch ◽  
Roberto Cappai ◽  
Anthony R. White

2012 ◽  
Vol 8 (4S_Part_11) ◽  
pp. P395-P395
Author(s):  
Kameshwar Ayyasolla ◽  
Shai Rahimipour ◽  
Edmund Miller ◽  
Pravin C. Singhal

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e49468 ◽  
Author(s):  
Neel R. Nabar ◽  
Fang Yuan ◽  
Xiaoyang Lin ◽  
Li Wang ◽  
Ge Bai ◽  
...  

2004 ◽  
Vol 167 (5) ◽  
pp. 809-812 ◽  
Author(s):  
Christoph Kaether ◽  
Christian Haass

Millions of patients suffer from Alzheimer's disease, and intensive efforts to find a cure for this devastating disorder center on the proteases, which release the deadly amyloid β-peptide from its precursor. The cutting procedure is thought to be cholesterol dependent and strategies to lower cholesterol as therapeutic treatment are under intensive investigation. Recent findings suggest that the complete proteolytic machinery required for amyloid β-peptide generation is located within lipid rafts. Data by Dotti and colleagues (Abad-Rodriguez et al., 2004), in this issue, suggest that rafts isolate the cutting machinery away from its deadly substrate. These findings describe a novel mechanism for controlling proteolytic activity by building a lipid boundary between proteases and their substrates.


2019 ◽  
Vol 42 ◽  
Author(s):  
Colleen M. Kelley ◽  
Larry L. Jacoby

Abstract Cognitive control constrains retrieval processing and so restricts what comes to mind as input to the attribution system. We review evidence that older adults, patients with Alzheimer's disease, and people with traumatic brain injury exert less cognitive control during retrieval, and so are susceptible to memory misattributions in the form of dramatic levels of false remembering.


Author(s):  
J. Metuzals ◽  
D. F. Clapin ◽  
V. Montpetit

Information on the conformation of paired helical filaments (PHF) and the neurofilamentous (NF) network is essential for an understanding of the mechanisms involved in the formation of the primary lesions of Alzheimer's disease (AD): tangles and plaques. The structural and chemical relationships between the NF and the PHF have to be clarified in order to discover the etiological factors of this disease. We are investigating by stereo electron microscopic and biochemical techniques frontal lobe biopsies from patients with AD and squid giant axon preparations. The helical nature of the lesion in AD is related to pathological alterations of basic properties of the nervous system due to the helical symmetry that exists at all hierarchic structural levels in the normal brain. Because of this helical symmetry of NF protein assemblies and PHF, the employment of structure reconstruction techniques to determine the conformation, particularly the handedness of these structures, is most promising. Figs. 1-3 are frontal lobe biopsies.


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