Cytoplasmic presenilin aggregates in proteasome inhibitor-treated cells.
Ingano
L A
LA
Genetics and Aging Unit and Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, USA.
Lentini
K M
KM
Kovacs
I
I
Tanzi
R E
RE
Kovacs
D M
DM
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000544:Alzheimer Disease / Q000473:pathology; D000818:Animals; D001921:Brain / Q000473:pathology; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D009097:Multienzyme Complexes / Q000378:metabolism*; D016874:Neurofibrillary Tangles / Q000473:pathology; D053764:Presenilin-1; D011480:Protease Inhibitors / Q000494:pharmacology*; D046988:Proteasome Endopeptidase Complex; D011994:Recombinant Proteins / Q000378:metabolism / Q000648:ultrastructure; D014162:Transfection
D008565:Membrane Proteins; D009097:Multienzyme Complexes; C508853:PSEN1 protein, human; D053764:Presenilin-1; D011480:Protease Inhibitors; D011994:Recombinant Proteins; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases