ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons
By Peer-Hendrik Kuhn, Huanhuan Wang, B. Dislich, A. Colombo, U. Zeitschel, J. Ellwart, E. Kremmer, S. Roßner, S. Lichtenthaler. EMBO Journal, 2010
640 citations recorded by the source corpus.
Subfields: Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/dffd3996f14fbf65316cf86b6f725026d299c98e
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Citations in the corpus
- APP processing in Alzheimer's disease (2011, background): “tion [49], implying that ADAM9 is involved only in regulated a-cleavage.”
- Trafficking and proteolytic processing of APP. (2012, background): “Lowering cholesterol levels in cultured cells stimulates a-secretase cleavage of APP through mechanisms involving impaired APP endocytosis and increased steadystate levels of ADAM10 (Kojro et al. 2001).”
- Alzheimer's disease risk genes and mechanisms of disease pathogenesis (2014, positive): “org/journ in ADAM10, the major α-secretase involved in shedding of the APP ectodomain (30), cosegregate in seven LOAD families (8,31).”
- Alzheimer's disease. (2011, background): “…(12 residues amino-terminal to the transmembrane domain) and is affected by one of the a-secretases, which are members of the ADAM family of membrane-anchored metalloproteases (Sisodia Cite this article as Cold Spring Harb Perspect Biol 2011;3:a004457 3 1992; Buxbaum et al. 1998; Kuhn et al. 2010).”