Nanolithography of Amyloid Precursor Protein Cleavage with β-Secretase by Atomic Force Microscopy

2016 ◽  
Vol 12 (3) ◽  
pp. 546-553 ◽  
Author(s):  
Sung-Woong Han ◽  
Hoon-Kyu Shin ◽  
Taiji Adachi
Keyword(s):  
Atomic Force Microscopy ◽  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Protein Cleavage ◽  
Force Microscopy ◽  
Atomic Force ◽  
Amyloid Precursor Protein Cleavage

scholarly journals Modulation of Amyloid Precursor Protein Cleavage by Cellular Sphingolipids

2004 ◽  
Vol 279 (12) ◽  
pp. 11984-11991 ◽  
Author(s):  
Naoya Sawamura ◽  
Mihee Ko ◽  
Wenxin Yu ◽  
Kun Zou ◽  
Kentaro Hanada ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Protein Cleavage ◽  
Amyloid Precursor Protein Cleavage

BACE1 Overexpression Regulates Amyloid Precursor Protein Cleavage and Interaction with the ShcA Adapter

2004 ◽  
Vol 1030 (1) ◽  
pp. 330-338 ◽  
Author(s):  
EMANUELA REPETTO ◽  
CLAUDIO RUSSO ◽  
VALENTINA VENEZIA ◽  
MARIO NIZZARI ◽  
ROGER M. NITSCH ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Protein Cleavage ◽  
Amyloid Precursor Protein Cleavage

Astroglial mGlu3 receptors promote alpha-secretase-mediated amyloid precursor protein cleavage

2014 ◽  
Vol 79 ◽  
pp. 180-189 ◽  
Author(s):  
Daniela Durand ◽  
Lila Carniglia ◽  
Juan Beauquis ◽  
Carla Caruso ◽  
Flavia Saravia ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Protein Cleavage ◽  
Amyloid Precursor Protein Cleavage

scholarly journals Manipulations of amyloid precursor protein cleavage disrupt the circadian clock in aging Drosophila

2015 ◽  
Vol 77 ◽  
pp. 117-126 ◽  
Author(s):  
Matthew R. Blake ◽  
Scott D. Holbrook ◽  
Joanna Kotwica-Rolinska ◽  
Eileen S. Chow ◽  
Doris Kretzschmar ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Circadian Clock ◽  
Precursor Protein ◽  
Protein Cleavage ◽  
Amyloid Precursor Protein Cleavage

scholarly journals Amino Acid Sequence and Structural Comparison of BACE1 and BACE2 Using Evolutionary Trace Method

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Hoda Mirsafian ◽  
Adiratna Mat Ripen ◽  
Amir Feisal Merican ◽  
Saharuddin Bin Mohamad
Keyword(s):  
Amino Acid ◽  
Ligand Binding ◽  
Amyloid Precursor Protein ◽  
Beta Amyloid ◽  
Precursor Protein ◽  
Aspartyl Protease ◽  
Protein Cleavage ◽  
Evolutionary Trace ◽  
Cleavage Enzyme ◽  
Amyloid Precursor Protein Cleavage

Beta-amyloid precursor protein cleavage enzyme 1 (BACE1) and beta-amyloid precursor protein cleavage enzyme 2 (BACE2), members of aspartyl protease family, are close homologues and have high similarity in their protein crystal structures. However, their enzymatic properties differ leading to disparate clinical consequences. In order to identify the residues that are responsible for such differences, we used evolutionary trace (ET) method to compare the amino acid conservation patterns of BACE1 and BACE2 in several mammalian species. We found that, in BACE1 and BACE2 structures, most of the ligand binding sites are conserved which indicate their enzymatic property of aspartyl protease family members. The other conserved residues are more or less randomly localized in other parts of the structures. Four group-specific residues were identified at the ligand binding site of BACE1 and BACE2. We postulated that these residues would be essential for selectivity of BACE1 and BACE2 biological functions and could be sites of interest for the design of selective inhibitors targeting either BACE1 or BACE2.

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