| pubmed-article:3037011 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C0017161 | lld:lifeskim |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C0206419 | lld:lifeskim |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C0681842 | lld:lifeskim |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3037011 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:3037011 | pubmed:dateCreated | 1987-8-25 | lld:pubmed |
| pubmed-article:3037011 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3037011 | pubmed:abstractText | The complete nucleotide sequence of cloned cDNAs containing the E2 glycoprotein-encoding region of the genome of transmissible gastroenteritis virus (TGEV) has been determined. A single large translatable frame of 4.3 kb starting at 8.2 kb from the 3' end of the genome was identified. Its deduced amino acid sequence contains the characteristic features of a coronavirus peplomer protein: the precursor polypeptide of TGEV E2 is 1447 residues long (i.e. 285 longer than the avian infectious bronchitis coronavirus spike protein); partial N-terminal sequencing demonstrated that a putative secretory signal sequence of 16 amino acids is absent in the virion-associated protein; the predicted mol. wt. of the apoprotein is 158K; most of the 32 potential N-glycosylation sites available in the sequence are presumed to be functional to account for the difference between this and the experimentally determined value (200K to 220K); a typical hydrophobic sequence near the C terminus is likely to be responsible for anchoring the peplomer to the virion envelope. | lld:pubmed |
| pubmed-article:3037011 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3037011 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3037011 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3037011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3037011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3037011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3037011 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3037011 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:3037011 | pubmed:issn | 0022-1317 | lld:pubmed |
| pubmed-article:3037011 | pubmed:author | pubmed-author:LaudeHH | lld:pubmed |
| pubmed-article:3037011 | pubmed:author | pubmed-author:RasschaertDD | lld:pubmed |
| pubmed-article:3037011 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3037011 | pubmed:volume | 68 ( Pt 7) | lld:pubmed |
| pubmed-article:3037011 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3037011 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3037011 | pubmed:pagination | 1883-90 | lld:pubmed |
| pubmed-article:3037011 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
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| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:meshHeading | pubmed-meshheading:3037011-... | lld:pubmed |
| pubmed-article:3037011 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3037011 | pubmed:articleTitle | The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus. | lld:pubmed |
| pubmed-article:3037011 | pubmed:publicationType | Journal Article | lld:pubmed |
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