Different interaction modes for Protein-disulfide Isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α)

Journal of Biological Chemistry

Volumn 289, Issue 45, 2014, Pages 31188-31199

  Zhang, Lihui ^a,b   Niu, Yingbo ^a,b   Zhu, Li ^a,b   Fang, Jingqi ^a,b   Wang, Xi'e ^a   Wang, Lei ^a   Wang, Chih Chen ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; HYDROPHOBICITY; MAMMALS; PROTEIN FOLDING; PROTEINS; SULFUR COMPOUNDS;

ENDOPLASMIC RETICULUM; HYDROPHOBIC INTERACTIONS; INTERACTION MODES; MAMMALIAN ENDOPLASMIC RETICULUM; PROTEIN DISULFIDE ISOMERASES; SPECIFIC SUBSTRATES; SUBSTRATE BINDING DOMAIN; SULFHYDRYL OXIDASE;

SUBSTRATES;

ENDOPLASMIC RETICULUM OXIDOREDUCTIN 1ALPHA; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; UNCLASSIFIED DRUG; CYSTEINE; DISULFIDE; ERO1L PROTEIN, HUMAN; MEMBRANE PROTEIN; OXYGEN; PROTEIN BINDING;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME BINDING; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HELA CELL LINE; HYDROPHOBICITY; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; CHEMISTRY; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYMOLOGY; HOMEOSTASIS; HUMAN; METABOLISM; RNA INTERFERENCE;

CATALYTIC DOMAIN; CYSTEINE; DISULFIDES; ENDOPLASMIC RETICULUM; HELA CELLS; HOMEOSTASIS; HUMANS; MEMBRANE GLYCOPROTEINS; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN; PROTEIN BINDING; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; RNA INTERFERENCE; SUBSTRATE SPECIFICITY;

EID: 84909952630     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.602961     Document Type: Article

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