| pubmed-article:6876179 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6876179 | lifeskim:mentions | umls-concept:C0037170 | lld:lifeskim |
| pubmed-article:6876179 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:6876179 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:6876179 | lifeskim:mentions | umls-concept:C0599814 | lld:lifeskim |
| pubmed-article:6876179 | lifeskim:mentions | umls-concept:C0162801 | lld:lifeskim |
| pubmed-article:6876179 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6876179 | pubmed:dateCreated | 1983-9-9 | lld:pubmed |
| pubmed-article:6876179 | pubmed:abstractText | We have sequenced the complementary DNA corresponding to the genes encoding the viral glycoproteins of ts10 and ts23, mutants of Sindbis virus defective in the intracellular transport of their glycoproteins, and of revertants of these mutants. These studies have been augmented by direct amino acid sequencing of the amino-terminal regions of the glycoproteins of several virus strains. By comparing the deduced amino acid sequence with that of Sindbis HR virus, the parental strain of these mutants, and with the sequence of the revertants, we found ts23 to have a double mutation in glycoprotein E1, while ts10 was a single mutant in the same glycoprotein. In each case reversion to temperature insensitivity occurred by changes at the same site as the mutation, in two cases restoring the original amino acid and in the third case substituting an homologous amino acid (arginine in place of lysine). The three mutations were far apart from each other in the protein, suggesting that the three-dimensional conformation is very important for the correct migration of the glycoproteins from the rough endoplasmic reticulum to the plasma membrane. The sequence data also reveal that a number of other changes have occurred in the various virus strains during mutagenesis or passage. | lld:pubmed |
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| pubmed-article:6876179 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6876179 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6876179 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6876179 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6876179 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:6876179 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:6876179 | pubmed:author | pubmed-author:StraussJ HJH | lld:pubmed |
| pubmed-article:6876179 | pubmed:author | pubmed-author:StraussE GEG | lld:pubmed |
| pubmed-article:6876179 | pubmed:author | pubmed-author:LenchesE MEM | lld:pubmed |
| pubmed-article:6876179 | pubmed:author | pubmed-author:AriasCC | lld:pubmed |
| pubmed-article:6876179 | pubmed:author | pubmed-author:BellJ RJR | lld:pubmed |
| pubmed-article:6876179 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6876179 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6876179 | pubmed:volume | 168 | lld:pubmed |
| pubmed-article:6876179 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6876179 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6876179 | pubmed:pagination | 87-102 | lld:pubmed |
| pubmed-article:6876179 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:6876179 | pubmed:meshHeading | pubmed-meshheading:6876179-... | lld:pubmed |
| pubmed-article:6876179 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6876179 | pubmed:articleTitle | Sequence analysis of two mutants of Sindbis virus defective in the intracellular transport of their glycoproteins. | lld:pubmed |
| pubmed-article:6876179 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6876179 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6876179 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:6876179 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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