ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity

Journal of Biological Chemistry

Volumn 284, Issue 15, 2009, Pages 10160-10173

  Zhang, Yinan ^a   Kozlov, Guennadi ^b   Pocanschi, Cosmin L ^a   Brockmeier, Ulf ^a   Ireland, Breanna S ^a   Maattanen, Pekka ^b   Howe, Chris ^c   Elliott, Tim ^c   Gehring, Kalle ^b   Williams, David B ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CALRETICULIN; CATALYTIC ROLE; CLASS I; ENZYMATIC ACTIVITIES; HEAVY CHAIN; IN-CELL; LECTIN CHAPERONES; OXIDOREDUCTASE; PEPTIDE LOADING; PEPTIDE-LOADING COMPLEX; POLYPEPTIDE BINDING SITES; REDOX ACTIVITY; REDOX-ACTIVE SITES; SUBSTRATE RECOGNITION; TAPASIN; WILD-TYPE CELLS;

AMINES; BINDING ENERGY; BINDING SITES; LOADING; MOLECULES; REDOX REACTIONS;

SUBSTRATES;

CALNEXIN; CALRETICULIN; CHAPERONE; COMPLEMENTARY DNA; DISULFIDE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; OLIGOSACCHARIDE; OXIDOREDUCTASE; PEPTIDE; POLYPEPTIDE; PROTEIN ERP57; TAPASIN; UNCLASSIFIED DRUG; HLA ANTIGEN CLASS 1; PDIA3 PROTEIN, MOUSE; PROTEIN DISULFIDE ISOMERASE;

ANIMAL CELL; ARTICLE; BIOGENESIS; CELL LINE; CIRCULAR DICHROISM; CONTROLLED STUDY; DNA ISOLATION; ENZYME ACTIVITY; FIBROBLAST; FLOW CYTOMETRY; GENETIC TRANSFECTION; MOUSE; MUTAGENESIS; MUTANT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN INTERACTION; RNA INTERFERENCE; WESTERN BLOTTING; WILD TYPE; ANIMAL; CATALYSIS; CHEMISTRY; CONFORMATION; METABOLISM; OXIDATION REDUCTION REACTION;

ANIMALS; CALNEXIN; CALRETICULIN; CATALYSIS; CELL LINE; FIBROBLASTS; HISTOCOMPATIBILITY ANTIGENS CLASS I; MAGNETIC RESONANCE SPECTROSCOPY; MICE; MOLECULAR CHAPERONES; MOLECULAR CONFORMATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PEPTIDES; PROTEIN DISULFIDE-ISOMERASES;

EID: 65649095933     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M808356200     Document Type: Article

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