CNS amyloid-ß, soluble APP-α and -ß kinetics during BACE inhibition.
Dobrowolska, Justyna A; Michener, Maria S; Wu, Guoxin; Patterson, Bruce W; Chott, Robert; Ovod, Vitaliy; Pyatkivskyy, Yuriy; Wildsmith, Kristin R; Kasten, Tom; Mathers, Parker; Dancho, Mandy; Lennox, Christina; Smith, Brad E; Gilberto, David; McLoughlin, Debra; Holder, Daniel J; Stamford, Andrew W; Yarasheski, Kevin E; Kennedy, Matthew E; Savage, Mary J; Bateman, Randall J.
; 34(24): 8336-46, 2014 Jun 11.
Artigo em Inglês | MEDLINE | ID: mdl-24920637
Nicastrin functions to sterically hinder Î³-secretase-substrate interactions driven by substrate transmembrane domain.
An atomic structure of human Î³-secretase.
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Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.
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Î·-Secretase processing of APP inhibits neuronal activity in the hippocampus.
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Influence of membrane lipid composition on the structure and activity of Î³-secretase.
Label-free Quantitative Proteomics of Mouse Cerebrospinal Fluid Detects ß-Site APP Cleaving Enzyme (BACE1) Protease Substrates In Vivo.