The oxidoreductase behavior of protein disulfide isomerase impedes fold maturation of endoplasmic reticulum-processed proteins in the pivotal structure-coupled step of oxidative folding: Implications for subcellular protein trafficking

Biochemistry

Volumn 49, Issue 29, 2010, Pages 6282-6289

  Gonzalez, Veronica ^a   Pal, Rituraj ^a   Narayan, Mahesh ^a  

^a UNIVERSITY OF TEXAS AT EL PASO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE-LIKE ACTIVITY; CHEMICAL TOOLS; CONFORMATIONAL FOLDING; DISULFIDE BONDS; ENDOPLASMIC RETICULUM; EXCHANGE REACTION; FOLDING KINETICS; IN-VIVO; LIMITING BEHAVIOR; MISFOLDING; OXIDATIVE FOLDING; OXIDOREDUCTASES; PHYSICAL STRUCTURES; PROTEIN DISULFIDE ISOMERASES; PROTEIN TRAFFICKING; RATE DETERMINING STEP; RIBONUCLEASE A; RNASE A; SUB-CELLULAR; SUB-DOMAINS; THIOL-DISULFIDE;

CONFORMATIONS; ISOMERIZATION;

PROTEINS;

CHAPERONE; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; RIBONUCLEASE A;

ARTICLE; CATALYST; CELL MIGRATION; CHEMICAL REACTION; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ISOMERIZATION; OXIDATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STRUCTURE;

ENDOPLASMIC RETICULUM; MOLECULAR CHAPERONES; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RIBONUCLEASE, PANCREATIC;

EID: 77954825807     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100753s     Document Type: Article

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