Ontology highlight
ABSTRACT:
SUBMITTER: Anelli T
PROVIDER: S-EPMC125352 | biostudies-literature | 2002 Feb
REPOSITORIES: biostudies-literature
Anelli Tiziana T Alessio Massimo M Mezghrani Alexandre A Simmen Thomas T Talamo Fabio F Bachi Angela A Sitia Roberto R
The EMBO journal 20020201 4
In human cells, Ero1-Lalpha and -Lbeta (hEROs) regulate oxidative protein folding by selectively oxidizing protein disulfide isomerase. Specific protein--protein interactions are probably crucial for regulating the formation, isomerization and reduction of disulfide bonds in the endoplasmic reticulum (ER). To identify molecules involved in ER redox control, we searched for proteins interacting with Ero1-Lalpha. Here, we characterize a novel ER resident protein (ERp44), which contains a thioredox ...[more]