| pubmed-article:12482753 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12482753 | lifeskim:mentions | umls-concept:C0012691 | lld:lifeskim |
| pubmed-article:12482753 | lifeskim:mentions | umls-concept:C1655065 | lld:lifeskim |
| pubmed-article:12482753 | lifeskim:mentions | umls-concept:C0679209 | lld:lifeskim |
| pubmed-article:12482753 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:12482753 | pubmed:dateCreated | 2003-2-24 | lld:pubmed |
| pubmed-article:12482753 | pubmed:abstractText | We examined the effects of protein folding on endoplasmic reticulum (ER)-to-cytosol transport (dislocation) by exploiting the well-characterized dihydrofolate reductase (DHFR) domain. DHFR retains the capacity to bind folate analogues in the lumen of microsomes and in the ER of intact cells, upon which it acquires a conformation resistant to proteinase K digestion. Here we show that a Class I major histocompatibility complex heavy chain fused to DHFR is still recognized by the human cytomegalovirus-encoded glycoproteins US2 and US11, resulting in dislocation of the fusion protein from the ER in vitro and in vivo. A folded state of the DHFR domain does not impair dislocation of Class I MHC heavy chains in vitro or in living cells. In fact, a slight acceleration of the dislocation of DHFR heavy chain fusion was observed in vitro in the presence of a folate analogue. These results suggest that one or more of the channels used for dislocation can accommodate polypeptides that contain a tightly folded domain of considerable size. Our data raise the possibility that the Sec61 channel can be modified to accommodate a folded DHFR domain for dislocation, but not for translocation into the ER, or that a channel altogether distinct from Sec61 is used for dislocation. | lld:pubmed |
| pubmed-article:12482753 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482753 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12482753 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482753 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12482753 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482753 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12482753 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482753 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12482753 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12482753 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12482753 | pubmed:author | pubmed-author:PloeghHidde... | lld:pubmed |
| pubmed-article:12482753 | pubmed:author | pubmed-author:FurmanMargo... | lld:pubmed |
| pubmed-article:12482753 | pubmed:author | pubmed-author:TortorellaDom... | lld:pubmed |
| pubmed-article:12482753 | pubmed:author | pubmed-author:TiroshBoazB | lld:pubmed |
| pubmed-article:12482753 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12482753 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:12482753 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12482753 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12482753 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12482753 | pubmed:pagination | 6664-72 | lld:pubmed |
| pubmed-article:12482753 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12482753 | pubmed:meshHeading | pubmed-meshheading:12482753... | lld:pubmed |
| pubmed-article:12482753 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12482753 | pubmed:articleTitle | Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation. | lld:pubmed |
| pubmed-article:12482753 | pubmed:affiliation | Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:12482753 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12482753 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12482753 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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