Fibroblasts from FAD-linked presenilin 1 mutations display a normal unfolded protein response but overproduce Aβ42 in response to tunicamycin

Neurobiology of Disease

Volumn 15, Issue 2, 2004, Pages 380-386

  Piccini, Alessandra ^a   Fassio, Anna ^a,b   Pasqualetto, Elena ^b   Vitali, Antonella ^a   Borghi, Roberta ^a   Palmieri, Daniela ^a   Nacmias, Benedetta ^c   Sorbi, Sandro ^c   Sitia, Roberto ^b   Tabaton, Massimo ^a  

^a UNIVERSITY OF GENOA   (Italy)

^b VITA SALUTE SAN RAFFAELE UNIVERSITY   (Italy)

^c UNIVERSITY OF FLORENCE   (Italy)

Author keywords

A ; AD; Alzheimer's disease; Amyloid; Amyloid protein; APP; Endoplasmic reticulum; ER; Presenilin; Primary fibroblasts; PS; Unfolded protein response; Unfolding protein response; UPR

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; DITHIOTHREITOL; MESSENGER RNA; PRESENILIN 1; TUNICAMYCIN;

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; FAMILIAL DISEASE; FIBROBLAST; GENE MUTATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN TRANSPORT;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; CARRIER PROTEINS; CELLS, CULTURED; ENDOPLASMIC RETICULUM; FIBROBLASTS; GLYCOPROTEINS; GLYCOSYLATION; HEAT-SHOCK PROTEINS; HUMANS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; PEPTIDE FRAGMENTS; PRESENILIN-1; PROTEIN FOLDING; RNA, MESSENGER; STRESS; TUNICAMYCIN;

EID: 10744222838     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2003.11.013     Document Type: Article

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