Uveitogenic epitopes of a retinal autoantigen are processed via an alternative pathway which does not involve processing by cathepsin B in acidic MIIC

1997 ◽  
Vol 56 (1-3) ◽  
pp. 310
Author(s):  
J Liversidge
2002 ◽  
Vol 38 ◽  
pp. 37-49 ◽  
Author(s):  
Janelle Nunan ◽  
David H Small

The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.


2007 ◽  
Vol 45 (08) ◽  
Author(s):  
F Weiss ◽  
CO Behn ◽  
P Simon ◽  
W Halangk ◽  
MM Lerch
Keyword(s):  

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