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The Journal of Biological Chemistry|June 14, 2012
The neural cell adhesion molecules L1 and CHL1 are cleaved by BACE1 protease in vivoLujia Zhou, Soraia Barão, Mathias Laga, et al.
International Journal of Molecular Sciences|May 25, 2024
Presenilin Deficiency Results in Cellular Cholesterol Accumulation by Impairment of Protein Glycosylation and NPC1 FunctionMarietta Fabiano, Naoto Oikawa, Anja Kerksiek, et al.
Cellular and Molecular Life Sciences : CMLS|October 27, 2009
Inactivation of the proximal NPXY motif impairs early steps in LRP1 biosynthesisSara M Reekmans, Thorsten Pflanzner, Philip L S M Gordts, et al.
Human Molecular Genetics|October 2, 2002
The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblastsDieter Hartmann, Bart de Strooper, Lutgarde Serneels, et al.
The Journal of Biological Chemistry|January 12, 2007
TrkA receptor activation by nerve growth factor induces shedding of the p75 neurotrophin receptor followed by endosomal gamma-secretase-mediated release of the p75 intracellular domainSoledad Urra, Claudia A Escudero, Patricio Ramos, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 25, 2005
Differential contribution of the three Aph1 genes to gamma-secretase activity in vivoLutgarde Serneels, Tim Dejaegere, Katleen Craessaerts, et al.
Molecular Biology of the Cell|April 24, 2015
Primary cilium suppression by SREBP1c involves distortion of vesicular trafficking by PLA2G3Hannah Laura Gijs, Nicolas Willemarck, Frank Vanderhoydonc, et al.
The Journal of Biological Chemistry|February 14, 2009
ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretaseThomas Tousseyn, Amantha Thathiah, Ellen Jorissen, et al.
Biological Chemistry|May 16, 2016
Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomainsFrederike Schmidt, Miryam Müller, Johannes Prox, et al.
Biological Chemistry|May 16, 2016
Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomainsFrederike Schmidt, Miryam Müller, Johannes Prox, et al.
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