Human thyroperoxidase is largely retained and rapidly degraded in the endoplasmic reticulum. Its N-glycans are required for folding and intracellular trafficking

Endocrinology

Volumn 139, Issue 10, 1998, Pages 4277-4285

  Fayadat, Laurence ^a   Niccoli Sire, Patricia ^a   Lanet, Jeanne ^a   Franc, Jean Louis ^a  

^a INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; GLYCAN DERIVATIVE; THYROID PEROXIDASE; TUNICAMYCIN;

ANIMAL CELL; APICAL MEMBRANE; ARTICLE; CELL MEMBRANE; CELL SURFACE; CHO CELL; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; GLYCOSYLATION; HORMONE SYNTHESIS; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; THYROID CELL;

EID: 0031764940     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.139.10.6265     Document Type: Article

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