X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid .beta.-protein precursor

Biochemistry ◽  
1990 ◽  
Vol 29 (43) ◽  
pp. 10018-10022 ◽  
Author(s):  
Thomas R. Hynes ◽  
Michael Randal ◽  
Laura A. Kennedy ◽  
Charles Eigenbrot ◽  
Anthony A. Kossiakoff
2015 ◽  
Vol 44 (5) ◽  
pp. 2359-2369 ◽  
Author(s):  
Tushar S. Basu Baul ◽  
Sajal Kundu ◽  
Palwinder Singh ◽  
Shaveta Shaveta ◽  
M. Fátima C. Guedes da Silva

LRshows interactions with the human amyloid beta protein precursor (APP)viazinc atoms. Such interactions were confirmed from the X-ray diffraction studies.


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.


1994 ◽  
Vol 269 (36) ◽  
pp. 22623-22627 ◽  
Author(s):  
J. Davis-Salinas ◽  
S.M. Saporito-Irwin ◽  
F.M. Donovan ◽  
D.D. Cunningham ◽  
W.E. Van Nostrand

Science ◽  
1990 ◽  
Vol 248 (4959) ◽  
pp. 1120-1122 ◽  
Author(s):  
C Van Broeckhoven ◽  
J Haan ◽  
E Bakker ◽  
J. Hardy ◽  
W Van Hul ◽  
...  

Science ◽  
1990 ◽  
Vol 248 (4956) ◽  
pp. 745-748 ◽  
Author(s):  
W. Van Nostrand ◽  
A. Schmaier ◽  
J. Farrow ◽  
D. Cunningham

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