@article{3f88b53cb37d4f6995a5e12926bacc4e,
title = "Presenilin 1 is actively degraded by the 26S proteasome",
abstract = "The metabolic pathways governing the turnover of presenilin 1 (PS1) have been incompletely worked out. The PS1 holoprotein has low abundance in many cells and appears to undergo endoproteolytic cleavage near residue 298. We provide evidence that one mechanism by which the PS1 holoprotein is degraded is through the action of the 26S proteasome. We also show that the proteasome does not participate in the endoproteolytic cleavage.",
keywords = "Alzheimer Disease, Degradation, Endoplasmic reticulum, PS1, PS2, Presenilin, Proteasome, Proteolysis, Transmembrane protein",
author = "Fraser, {P. E.} and G. Levesque and G. Yu and Mills, {L. R.} and J. Thirlwell and M. Frantseva and Gandy, {S. E.} and M. Seeger and Carlen, {P. L.} and {St George-Hyslop}, P.",
note = "Funding Information: Supported by grants from the Medical Research Council of Canada, Canadian Genetic Diseases Network, Alzheimer Association of Ontario, American Health Assistance Foundation, EJLB Foundation, Scottish Rite Charitable Foundation, Ontario Mental Health Foundation, NSERC, Heart and Stroke Foundation, Howard Hughes Medical Research Foundation, Peterborough-Burgess Fellowship (E.A.R.), Helen B. Hunter Fellowship (G.L., G.Y.), the US National Institutes of Health, and New York State Office of Mental Health. P.H.St.G.-H. is an MRC Scientist.",
year = "1998",
month = jan,
doi = "10.1016/S0197-4580(98)00029-3",
language = "English",
volume = "19",
pages = "S19--S21",
journal = "Neurobiology of Aging",
issn = "0197-4580",
publisher = "Elsevier Inc.",
number = "SUPPL. 1",
}