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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
7
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|
pubmed:dateCreated |
2008-7-8
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|
pubmed:abstractText |
Proteins 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.
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pubmed:grant |
|
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pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0968-0004
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
33
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
298-300
|
|
pubmed:dateRevised |
2010-9-16
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|
pubmed:meshHeading |
|
|
pubmed:year |
2008
|
|
pubmed:articleTitle |
Sweet bays of ERAD.
|
|
pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Massachusetts, 710N. Pleasant Street, Amherst, MA 01003, USA.
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|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|
