Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2008-8-27
pubmed:abstractText
Membrane and secretory proteins that fail to pass quality control in the endoplasmic reticulum are discharged into the cytosol and degraded by the proteasome. Many of the mammalian components involved in this process remain to be identified. We performed a biochemical search for proteins that interact with SEL1L, a protein that is part of the mammalian HRD1 ligase complex and involved in substrate recognition. SEL1L is crucial for dislocation of Class I major histocompatibility complex heavy chains by the human cytomegalovirus US11 protein. We identified AUP1, UBXD8, UBC6e, and OS9 as functionally important components of this degradation complex in mammalian cells, as confirmed by mutagenesis and dominant negative versions of these proteins.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-10854174, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-11285222, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-11641273, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-11717308, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-11790769, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12042322, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12062168, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12082160, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12372427, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12606569, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12612637, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12952521, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-12972557, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-14593114, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-15215855, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-15215856, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-15721254, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16168370, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16179953, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16186509, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16449189, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16720581, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16738546, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16845381, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16868077, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16873065, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16873066, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16901789, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16912321, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-16968747, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-17034365, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-17043138, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-17653186, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-18264092, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-667938, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-8393731, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-8625414, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-8855296, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-8945469, http://linkedlifedata.com/resource/pubmed/commentcorrection/18711132-9562620
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1091-6490
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
105
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12325-30
pubmed:dateRevised
2010-8-31
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins.
pubmed:affiliation
Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural