Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond

Archives of Biochemistry and Biophysics

Volumn 485, Issue 1, 2009, Pages 1-9

  Fu, Xinmiao ^a   Zhu, Bao Ting ^a  

^a Shimane University School of Medicine   (United States)

Author keywords

Chaperone; Dimer; Disulfide bond; Isomerase activity; Monomer; Oligomeric structure; PDI; PDIp; Redox regulation

Indexed keywords

CELL PROTEIN; CHAPERONE; CYSTEINE; GLUTARALDEHYDE; MONOMER; PROTEIN DISULFIDE ISOMERASE;

ARTICLE; CROSS LINKING; DISULFIDE BOND; GENETIC TRANSFECTION; HUMAN; HUMAN TISSUE; MAMMAL CELL; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CERCOPITHECUS AETHIOPS; COS CELLS; CYSTEINE; DISULFIDES; HUMANS; HYDROPHOBICITY; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; ORGAN SPECIFICITY; OXIDATION-REDUCTION; PANCREAS; PEPTIDE HYDROLASES; PROTEIN DISULFIDE-ISOMERASES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY;

PRIMATES; RODENTIA;

EID: 64549112593     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.12.021     Document Type: Article

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