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pubmed-article:18538572pubmed:abstractTextProteins that improperly mature in the endoplasmic reticulum (ER) are dislocated to the cytoplasm for proteasome-mediated destruction. A recent study provides insight into the incompletely understood processes for selection and targeting of aberrant proteins for ER-associated protein degradation. The identification of the ER chaperones GRP94 and BiP as binding partners for the mannose-binding proteins OS-9 and XTP3-B, indicates that these protein complexes bind to aberrant proteins and direct them to the Hrd1 dislocation and ubiquitylation complex in the ER membrane.lld:pubmed
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pubmed-article:18538572pubmed:articleTitleSweet bays of ERAD.lld:pubmed
pubmed-article:18538572pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of Massachusetts, 710N. Pleasant Street, Amherst, MA 01003, USA.lld:pubmed
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