Calnexin phosphorylation attenuates the release of partially misfolded α1-antitrypsin to the secretory pathway

Journal of Biological Chemistry

Volumn 284, Issue 50, 2009, Pages 34570-34579

  Cameron, Pamela H ^a   Chevet, Eric ^b   Pluquet, Olivier ^b   Thomas, David Y ^a   Bergeron, John J M ^a  

^a MCGILL UNIVERSITY   (Canada)

^b INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANTITRYPSIN; AZETIDINES; CYTOSOLIC; ENDOPLASMIC RETICULUM; INTEGRAL MEMBRANE; INTRALUMINAL; KIFUNENSINE; LECTIN CHAPERONES; LOW DOSE; MANNOSIDASE; MISFOLDING; N-LINKED; PHOSPHORYLATION SITES; SECRETORY PATHWAYS; TRANSLOCON;

CARBOXYLIC ACIDS; GLYCOPROTEINS; ORGANIC ACIDS; QUALITY FUNCTION DEPLOYMENT; TOTAL QUALITY MANAGEMENT;

PHOSPHORYLATION;

ALPHA 1 ANTITRYPSIN; ALPHA MANNOSIDASE; CALNEXIN; GLYCOPROTEIN; KIFUNENSINE;

ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN SYNTHESIS; QUALITY CONTROL; WILD TYPE;

ALKALOIDS; ALPHA 1-ANTITRYPSIN; ANIMALS; CALNEXIN; CELL LINE, TUMOR; ENZYME INHIBITORS; FLAVONOIDS; HUMANS; MITOGEN-ACTIVATED PROTEIN KINASE 3; PHOSPHORYLATION; PROTEIN FOLDING; SECRETORY PATHWAY; SERINE;

EID: 71749088618     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.053165     Document Type: Article

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