An online nano-LC-ESI-FTICR-MS method for comprehensive characterization of endogenous fragments from amyloid β and amyloid precursor protein in human and cat cerebrospinal fluid

2012 ◽  
Vol 47 (5) ◽  
pp. 591-603 ◽  
Author(s):  
Gunnar Brinkmalm ◽  
Erik Portelius ◽  
Annika Öhrfelt ◽  
Niklas Mattsson ◽  
Rita Persson ◽  
...  
2013 ◽  
Vol 56 (8) ◽  
pp. 3379-3403 ◽  
Author(s):  
Kevin W. Hunt ◽  
Adam W. Cook ◽  
Ryan J. Watts ◽  
Christopher T. Clark ◽  
Guy Vigers ◽  
...  

1995 ◽  
Vol 199 (3) ◽  
pp. 203-206 ◽  
Author(s):  
Lars Lannfelt ◽  
Hans Basun ◽  
Carmen Vigo-Pelfrey ◽  
Lars-Olof Wahlund ◽  
Bengt Winblad ◽  
...  

2013 ◽  
Vol 5 (194) ◽  
pp. 194re2-194re2 ◽  
Author(s):  
L. F. Maia ◽  
S. A. Kaeser ◽  
J. Reichwald ◽  
M. Hruscha ◽  
P. Martus ◽  
...  

2019 ◽  
Vol 141 (3) ◽  
Author(s):  
I. A. Kuznetsov ◽  
A. V. Kuznetsov

Modeling of intracellular processes occurring during the development of Alzheimer's disease (AD) can be instrumental in understanding the disease and can potentially contribute to finding treatments for the disease. The model of intracellular processes in AD, which we previously developed, contains a large number of parameters. To distinguish between more important and less important parameters, we performed a local sensitivity analysis of this model around the values of parameters that give the best fit with published experimental results. We show that the influence of model parameters on the total concentrations of amyloid precursor protein (APP) and tubulin-associated unit (tau) protein in the axon is reciprocal to the influence of the same parameters on the average velocities of the same proteins during their transport in the axon. The results of our analysis also suggest that in the beginning of AD the aggregation of amyloid-β and misfolded tau protein have little effect on transport of APP and tau in the axon, which suggests that early damage in AD may be reversible.


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