Ontology highlight
ABSTRACT:
SUBMITTER: Horna-Terron E
PROVIDER: S-EPMC4284777 | biostudies-literature | 2014 Dec
REPOSITORIES: biostudies-literature
Horna-Terrón Elena E Pradilla-Dieste Alberto A Sánchez-de-Diego Cristina C Osada Jesús J
International journal of molecular sciences 20141217 12
Thioredoxin domain-containing 5 (TXNDC5) is a member of the protein disulfide isomerase family, acting as a chaperone of endoplasmic reticulum under not fully characterized conditions As a result, TXNDC5 interacts with many cell proteins, contributing to their proper folding and correct formation of disulfide bonds through its thioredoxin domains. Moreover, it can also work as an electron transfer reaction, recovering the functional isoform of other protein disulfide isomerases, replacing reduce ...[more]