| pubmed-article:15134464 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15134464 | lifeskim:mentions | umls-concept:C0030390 | lld:lifeskim |
| pubmed-article:15134464 | lifeskim:mentions | umls-concept:C1166730 | lld:lifeskim |
| pubmed-article:15134464 | lifeskim:mentions | umls-concept:C1416749 | lld:lifeskim |
| pubmed-article:15134464 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:15134464 | lifeskim:mentions | umls-concept:C0217704 | lld:lifeskim |
| pubmed-article:15134464 | lifeskim:mentions | umls-concept:C1721219 | lld:lifeskim |
| pubmed-article:15134464 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:15134464 | pubmed:dateCreated | 2004-5-11 | lld:pubmed |
| pubmed-article:15134464 | pubmed:abstractText | The influenza virus uses hemagglutinin (HA) to fuse the viral and cellular membranes. As part of an effort to study the membrane-interacting elements of HA, the fusion peptide, and the C-terminal transmembrane anchor, we have expressed in Escherichia coli the full-length HA(2) chain with maltose-binding protein fused at its N-terminus. The chimeric protein can be refolded in vitro in the presence of specific detergents to yield stable, homogeneous trimers, as determined by analytical ultracentrifugation. The trimers have the so-called "low pH" conformation-the rearranged HA(2) conformation obtained when intact HA(1)/HA(2) is induced to refold by exposure to low pH-as detected by electron microscopy and monoclonalantibody reactivity. These results provide further evidence for the notion that the neutral-pH structure of intact HA is metastable and that binding of protons lowers the kinetic barriers that prevent rearrangement to the minimum-free-energy conformation. The refolded chimeric protein described here is a suitable species for undertaking studies of how the fusion peptide inserts into membranes and assessing the nature of possible intermediates in the fusion process. | lld:pubmed |
| pubmed-article:15134464 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15134464 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15134464 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15134464 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15134464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15134464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15134464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15134464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15134464 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15134464 | pubmed:month | May | lld:pubmed |
| pubmed-article:15134464 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15134464 | pubmed:author | pubmed-author:HarrisonSteph... | lld:pubmed |
| pubmed-article:15134464 | pubmed:author | pubmed-author:SkehelJohn... | lld:pubmed |
| pubmed-article:15134464 | pubmed:author | pubmed-author:WileyDon CDC | lld:pubmed |
| pubmed-article:15134464 | pubmed:author | pubmed-author:BakerBrian... | lld:pubmed |
| pubmed-article:15134464 | pubmed:author | pubmed-author:SwalleySusann... | lld:pubmed |
| pubmed-article:15134464 | pubmed:author | pubmed-author:CalderLesley... | lld:pubmed |
| pubmed-article:15134464 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15134464 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:15134464 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:15134464 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15134464 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15134464 | pubmed:pagination | 5902-11 | lld:pubmed |
| pubmed-article:15134464 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:15134464 | pubmed:meshHeading | pubmed-meshheading:15134464... | lld:pubmed |
| pubmed-article:15134464 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15134464 | pubmed:articleTitle | Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation. | lld:pubmed |
| pubmed-article:15134464 | pubmed:affiliation | Department of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, 250 Longwood Avenue, Boston, Massachusetts 02115, USA. swalley@crystal.harvard.edu | lld:pubmed |
| pubmed-article:15134464 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15134464 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15134464 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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