Glycoprotein folding in the endoplasmic reticulum

Critical Reviews in Biochemistry and Molecular Biology

Volumn 35, Issue 6, 2000, Pages 433-473

  Benham, A M ^a,b   Braakman, I ^a,b  

^a UTRECHT UNIVERSITY   (Netherlands)

^b ACADEMIC MEDICAL CENTER   (Netherlands)

Author keywords

Chaperones; ER; ERAD; Glycosylation; Protein folding

Indexed keywords

ALPHA MANNOSIDASE; CALCIUM; CALNEXIN; CALRETICULIN; CHAPERONE; COLLAGEN; CYCLOPHILIN; GLUCOSE REGULATED PROTEIN; GLYCOPROTEIN; GLYCOPROTEIN GP 96; HEAT SHOCK PROTEIN 47; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NUCLEAR PROTEIN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE; TAPASIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN;

ARTICLE; CELL TYPE; ENDOPLASMIC RETICULUM; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; PROTEIN TARGETING; RNA TRANSLATION;

EUKARYOTA;

EID: 0034486544     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409230091169258     Document Type: Article

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262. Kinetic analysis of the mechanism and specificity of protein-disulfide isomerase using fluorescence-quenched peptides
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264. Functional expression of low density lipoprotein receptor-related protein is controlled by receptor-associated protein in vivo
265. RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors
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275. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
276. Flavin-containing monooxygenases: Enzymes adapted for multisubstrate specificity
277. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum