| pubmed-article:3686832 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C0027984 | lld:lifeskim |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C0010654 | lld:lifeskim |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C0019822 | lld:lifeskim |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:3686832 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:3686832 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3686832 | pubmed:dateCreated | 1988-1-21 | lld:pubmed |
| pubmed-article:3686832 | pubmed:abstractText | Viruses within the Newcastle disease virus (NDV) serotype induce a wide array of disease manifestations ranging from an almost apathogenic pattern to the high mortality caused by avirulent or virulent isolates, respectively. A disulfide-linked dimer form of the NDV hemagglutinin-neuraminidase (HN) glycoprotein can be demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions for only some of these isolates. For others, indeed the majority of those we have studied, no such reducing agent-sensitive dimeric form of HN is demonstrable. Apparently, there is no causal relationship between disulfide-linked dimeric HN and virulence. Using the deduced amino acid sequence of the dimeric HN of isolate AV as a basis for selection of oligonucleotide primers, we sequenced three additional reducing agent-sensitive dimeric HN glycoproteins and eight for which a disulfide-linked dimer has not been identified, using primer extension and dideoxy sequencing. The deduced amino acid sequences reveal a strict correlation between the presence of cysteine at residue 123 and reducing agent-sensitive dimerization of HN. | lld:pubmed |
| pubmed-article:3686832 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3686832 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3686832 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3686832 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3686832 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3686832 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3686832 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3686832 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3686832 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3686832 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:3686832 | pubmed:author | pubmed-author:SheehanJ PJP | lld:pubmed |
| pubmed-article:3686832 | pubmed:author | pubmed-author:BrattM AMA | lld:pubmed |
| pubmed-article:3686832 | pubmed:author | pubmed-author:GlickmanR LRL | lld:pubmed |
| pubmed-article:3686832 | pubmed:author | pubmed-author:IorioR MRM | lld:pubmed |
| pubmed-article:3686832 | pubmed:author | pubmed-author:SyddallR JRJ | lld:pubmed |
| pubmed-article:3686832 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3686832 | pubmed:volume | 161 | lld:pubmed |
| pubmed-article:3686832 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3686832 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3686832 | pubmed:pagination | 603-6 | lld:pubmed |
| pubmed-article:3686832 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:meshHeading | pubmed-meshheading:3686832-... | lld:pubmed |
| pubmed-article:3686832 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3686832 | pubmed:articleTitle | Reducing agent-sensitive dimerization of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus correlates with the presence of cysteine at residue 123. | lld:pubmed |
| pubmed-article:3686832 | pubmed:affiliation | Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655. | lld:pubmed |
| pubmed-article:3686832 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3686832 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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