The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide

EMBO Journal

Volumn 18, Issue 1, 1999, Pages 65-74

  Koivunen, Peppi ^a   Pirneskoski, Annamari ^a   Karvonen, Päivi ^a   Ljung, Johanna ^b   Helaakoski, Tarja ^a   Notbohm, Holger ^c   Kivirikko, Kari I ^a  

^a UNIVERSITY OF OULU   (Finland)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF LÜBECK   (Germany)

Author keywords

Chaperone; Collagen; Microsomal triglyceride transfer protein; Prolyl 4 hydroxylase; Protein disulfide isomerase

Indexed keywords

CHAPERONE; MUTANT PROTEIN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME SUBUNIT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; CAENORHABDITIS ELEGANS; CATALYTIC DOMAIN; CIRCULAR DICHROISM; DIMERIZATION; ESCHERICHIA COLI; HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEOPOLYHEDROVIRUS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE DELETION; SPODOPTERA;

ANIMALIA; INSECTA;

EID: 0033521682     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.1.65     Document Type: Article

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