| pubmed-article:10353722 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10353722 | lifeskim:mentions | umls-concept:C0007625 | lld:lifeskim |
| pubmed-article:10353722 | lifeskim:mentions | umls-concept:C0162847 | lld:lifeskim |
| pubmed-article:10353722 | lifeskim:mentions | umls-concept:C1254042 | lld:lifeskim |
| pubmed-article:10353722 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10353722 | pubmed:dateCreated | 1999-8-5 | lld:pubmed |
| pubmed-article:10353722 | pubmed:abstractText | Reduced cellular systems have provided important tools to study complex cellular processes. Here we describe the oxidation, oligomerization, and chaperone binding of the viral glycoprotein influenza hemagglutinin in a cell-free system. The cell-free system, comprised of rough endoplasmic reticulum derived microsomes and a reticulocyte lysate, supported the complete maturation of hemagglutinin from the earliest oxidative intermediate to the mature homo-oligomer. Hemagglutinin disulfide bond formation and oligomerization were found to occur in a time- and temperature-dependent manner. Hemagglutinin's temporal association with the molecular chaperones calnexin and calreticulin was similar to that observed for their association with elongating ribosome-attached nascent chains in live cells. Furthermore, a procedure is described that permits the translocation of protein into microsomes that are depleted of lumenal contents. This cell-free system, therefore, provided an effective means to study the biological maturation processes of a protein that traverses the secretory pathway. | lld:pubmed |
| pubmed-article:10353722 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10353722 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10353722 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10353722 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10353722 | pubmed:issn | 0829-8211 | lld:pubmed |
| pubmed-article:10353722 | pubmed:author | pubmed-author:HeleniusAA | lld:pubmed |
| pubmed-article:10353722 | pubmed:author | pubmed-author:ZhangJ XJX | lld:pubmed |
| pubmed-article:10353722 | pubmed:author | pubmed-author:HebertD NDN | lld:pubmed |
| pubmed-article:10353722 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10353722 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:10353722 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10353722 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10353722 | pubmed:pagination | 867-73 | lld:pubmed |
| pubmed-article:10353722 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:meshHeading | pubmed-meshheading:10353722... | lld:pubmed |
| pubmed-article:10353722 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:10353722 | pubmed:articleTitle | Protein folding and maturation in a cell-free system. | lld:pubmed |
| pubmed-article:10353722 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003, USA. dhebert@biochem.umass.edu | lld:pubmed |
| pubmed-article:10353722 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10353722 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10353722 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10353722 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10353722 | lld:pubmed |
