Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum

Philosophical Transactions of the Royal Society B: Biological Sciences

Volumn 368, Issue 1617, 2013, Pages 1-9

  Benham, Adam M ^a   van Lith, Marcel ^a,b   Sitia, Roberto ^c,d   Braakman, Ineke ^e  

^a DURHAM UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

^c VITA SALUTE SAN RAFFAELE UNIVERSITY   (Italy)

^d SAN RAFFAELE HOSPITAL   (Italy)

^e UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Chaperone; Disulfide bond; Endoplasmic reticulum; Protein folding; Redox

Indexed keywords

CATALYST; CELL ORGANELLE; ELECTRON; ENZYME ACTIVITY; EUKARYOTE; MOLECULAR ANALYSIS; OXYGEN; PROTEIN; REDOX POTENTIAL;

EUKARYOTA; MAMMALIA;

CHAPERONE; COMPLEMENTARY DNA; DISULFIDE; ERO1L PROTEIN, HUMAN; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE;

ANIMAL; ARTICLE; CELL LINE; CHEMISTRY; ENDOPLASMIC RETICULUM; GENE EXPRESSION REGULATION; GENETICS; HUMAN; MAMMAL; METABOLISM; OXIDATION REDUCTION REACTION; PHYSIOLOGY;

ANIMALS; CELL LINE; DISULFIDES; DNA, COMPLEMENTARY; ENDOPLASMIC RETICULUM; GENE EXPRESSION REGULATION; HUMANS; MAMMALS; MEMBRANE GLYCOPROTEINS; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASES;

EID: 84875470472     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2011.0403     Document Type: Article

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