Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57

Journal of Biological Chemistry

Volumn 277, Issue 48, 2002, Pages 46415-46423

  Radcliffe, Catherine M ^a   Diedrich, Gundo ^b   Harvey, David J ^a   Dwek, Raymond A ^a   Cresswell, Peter ^b   Rudd, Pauline M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; CELLS; GLUCOSE; PROTEINS;

GLYCOSYLATION;

BIOCHEMISTRY;

CALRETICULIN; CHAPERONE; GLUCOSE; GLYCAN DERIVATIVE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE DERIVATIVE; PROTEIN P57; TAPASIN;

ANTIGEN PRESENTATION; ARTICLE; DISSOCIATION; ENDOPLASMIC RETICULUM; GLYCOSYLATION; HUMAN; HUMAN CELL; MAJOR HISTOCOMPATIBILITY COMPLEX; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; QUALITY CONTROL; REGULATORY MECHANISM;

CALRETICULIN; CELL LINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; ISOMERASES; PROTEIN DISULFIDE-ISOMERASE; PROTEIN ISOFORMS; QUALITY CONTROL;

EID: 2242469355     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M202466200     Document Type: Article

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