Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin

Journal of Biological Chemistry

Volumn 284, Issue 4, 2009, Pages 2194-2202

  Jessop, Catherine E ^a   Tavender, Timothy J ^a   Watkins, Rachel H ^a   Chambers, Joseph E ^a   Bulleid, Neil J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON TRANSITIONS; ENZYMES; GLYCOPROTEINS; ISOMERIZATION; ISOMERS; PROTEINS;

CALNEXIN CYCLES; CALRETICULIN; DISULFIDE BONDS; ENDOPLASMIC RETICULUMS; ISOMERIZATION REACTIONS; NON NATIVES; OXIDOREDUCTASE; OXIDOREDUCTASES; PROTEIN DISULFIDE ISOMERASE; SECRETORY PATHWAYS; SUBSTRATE SPECIFICITIES;

SUBSTRATES;

BETA1 INTEGRIN; CALNEXIN; CALRETICULIN; DISULFIDE; ERP57 ENZYME; GLYCOPROTEIN; HEMAGGLUTININ; OXIDOREDUCTASE; TAPASIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GLYCOSYLATION; HUMAN; HUMAN CELL; ISOMERIZATION; MOUSE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION;

ANIMALS; ANTIGENS, CD29; CALNEXIN; CALRETICULIN; CELL LINE; DISULFIDES; HUMANS; MICE; MICE, KNOCKOUT; MUTATION; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; SUBSTRATE SPECIFICITY;

EID: 59049105293     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M808054200     Document Type: Article

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