Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein

Journal of Biological Chemistry

Volumn 281, Issue 41, 2006, Pages 30431-30438

  Orsi, Andrea ^a   Fioriti, Luana ^b   Chiesa, Roberto ^b,c   Sitia, Roberto ^a  

^a VITA SALUTE SAN RAFFAELE UNIVERSITY   (Italy)

^b MARIO NEGRI INSTITUTE FOR PHARMACOLOGICAL RESEARCH   (Italy)

^c DULBECCO TELETHON INSTITUTE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOL; CYTOTOXIC; GLYCOSYLATION; GLYCOSYLPHOSPHATIDYLINOSITOL; TRANSLOCATION;

BIOCOMMUNICATIONS; CELL CULTURE; CELLS; CHEMICAL BONDS; PHOSPHOLIPIDS; TOXICITY;

ENZYMES;

GLYCAN DERIVATIVE; GLYCOSYLPHOSPHATIDYLINOSITOL; PRION PROTEIN; PROTEASOME; THAPSIGARGIN;

ARTICLE; CELL LINE; CONTROLLED STUDY; CYTOSOL; DISULFIDE BOND; ENDOPLASMIC RETICULUM; GLYCOSYLATION; HELA CELL; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; NERVE CELL; NEUROBLASTOMA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; STRESS;

ANIMALS; CYTOSOL; DISULFIDES; ENDOPLASMIC RETICULUM; GLYCOSYLPHOSPHATIDYLINOSITOLS; HELA CELLS; HUMANS; MICE; NEURONS; PRIONS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; XERODERMA PIGMENTOSUM GROUP A PROTEIN;

EID: 33750087269     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M605320200     Document Type: Article

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