The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules

EMBO Journal

Volumn 21, Issue 11, 2002, Pages 2655-2663

  Antoniou, Antony N ^a   Ford, Stuart ^a   Alphey, Magnus ^a   Osborne, Andrew ^a   Elliott, Tim ^a   Powis, Simon J ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

Chaperone; Endoplasmic reticulum; MHC class I; Oxidoreductase ERp57; Protein folding

Indexed keywords

HLA B27 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; OXIDOREDUCTASE; PROTEIN ERP57; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CELL FRACTIONATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME METABOLISM; GENE TRANSLOCATION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING;

AMINO ACID MOTIFS; ANIMALS; CELL LINE; CYSTEINE; DISULFIDES; DNA, COMPLEMENTARY; HEAT-SHOCK PROTEINS; HUMANS; INSULIN; ISOMERASES; MAJOR HISTOCOMPATIBILITY COMPLEX; MUTATION; PEPTIDES; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; RATS; RECOMBINANT PROTEINS; SUBCELLULAR FRACTIONS; TIME FACTORS;

ANIMALIA;

EID: 0037013950     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/21.11.2655     Document Type: Article

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