Extension of lipid-linked oligosaccharides is a high-priority aspect of the unfolded protein response: Endoplasmic reticulum stress in Type I congenital disorder of glycosylation fibroblasts

Glycobiology

Volumn 12, Issue 5, 2002, Pages 307-317

  Shang, Jie ^a   Körner, Christian ^b   Freeze, Hudson ^c   Lehrman, Mark A ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c BURNHAM INSTITUTE   (United States)

Author keywords

Congenital disorder of glycosylation; Endoplasmic reticulum stress; Glycosylation; Lipid linked oligosaccharide; Unfolded protein response

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; GLYCOPROTEIN; CARRIER PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN; LIPID; MOLECULAR CHAPERONE GRP78; OLIGOSACCHARIDE;

ARTICLE; CELL DEATH; CONGENITAL DISORDER OF GLYCOSYLATION TYPE 1; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENETIC DISORDER; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; QUANTITATIVE ANALYSIS; SKIN FIBROBLAST; STRESS; TRANSACTIVATION; TRANSCRIPTION INITIATION; CARBOHYDRATE METABOLISM; CHEMISTRY; FIBROBLAST; GENETIC TRANSCRIPTION; GENETICS; GLYCOSYLATION; METABOLISM; PROTEIN DENATURATION;

CARBOHYDRATE METABOLISM; CARRIER PROTEINS; ENDOPLASMIC RETICULUM; FIBROBLASTS; GLYCOSYLATION; HEAT-SHOCK PROTEINS; HUMANS; LIPIDS; MOLECULAR CHAPERONES; OLIGOSACCHARIDES; PROTEIN DENATURATION; TRANSCRIPTION, GENETIC;

EID: 0036020877     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/12.5.307     Document Type: Article

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