pubmed-article:3277595 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3277595 | lifeskim:mentions | umls-concept:C0025011 | lld:lifeskim |
pubmed-article:3277595 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
pubmed-article:3277595 | lifeskim:mentions | umls-concept:C0042717 | lld:lifeskim |
pubmed-article:3277595 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
pubmed-article:3277595 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:3277595 | pubmed:dateCreated | 1988-3-2 | lld:pubmed |
pubmed-article:3277595 | pubmed:abstractText | Intracellular processing of measles virus fusion (F) protein was studied by radiolabeling and immunoprecipitation with a monoclonal antibody against F protein. The cleavage of F protein into F1 and F2 subunits was complete after 5 hours of chase during which the growth of oligosaccharide chains on the F2 domain of F protein continued. The addition of terminal sialic acid conferred a strong negative charge on the F2 subunit. F protein expressed on the cell surface was removed by a fungal semi-alkaline protease, providing a method to follow the kinetics of its transport to the cell surface. The transport of the F protein was faster than that of the hemagglutinin (HA) protein. Uncleaved F protein, as well as cleaved subunits became digestible by the protease, indicating that a portion of the F protein reaches the cell surface uncleaved. The treatment of measles virus-infected cells with tunicamycin resulted in the synthesis of unglycosylated HA (65 kilodaltons, Kd) and F (48 Kd) proteins. Unglycosylated F protein was not cleaved into smaller subunits, nor was it transported to the cell surface. Unglycosylated HA protein likewise failed to reach the cell surface. | lld:pubmed |
pubmed-article:3277595 | pubmed:language | eng | lld:pubmed |
pubmed-article:3277595 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3277595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3277595 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3277595 | pubmed:issn | 0304-8608 | lld:pubmed |
pubmed-article:3277595 | pubmed:author | pubmed-author:SatoT ATA | lld:pubmed |
pubmed-article:3277595 | pubmed:author | pubmed-author:SugiuraAA | lld:pubmed |
pubmed-article:3277595 | pubmed:author | pubmed-author:KohamaTT | lld:pubmed |
pubmed-article:3277595 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3277595 | pubmed:volume | 98 | lld:pubmed |
pubmed-article:3277595 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3277595 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3277595 | pubmed:pagination | 39-50 | lld:pubmed |
pubmed-article:3277595 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:3277595 | pubmed:meshHeading | pubmed-meshheading:3277595-... | lld:pubmed |
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pubmed-article:3277595 | pubmed:meshHeading | pubmed-meshheading:3277595-... | lld:pubmed |
pubmed-article:3277595 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3277595 | pubmed:articleTitle | Intracellular processing of measles virus fusion protein. | lld:pubmed |
pubmed-article:3277595 | pubmed:affiliation | Department of Measles Virus, National Institute of Health, Tokyo, Japan. | lld:pubmed |
pubmed-article:3277595 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3277595 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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