| pubmed-article:1370605 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1370605 | lifeskim:mentions | umls-concept:C0035870 | lld:lifeskim |
| pubmed-article:1370605 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:1370605 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:1370605 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
| pubmed-article:1370605 | pubmed:issue | 3-4 | lld:pubmed |
| pubmed-article:1370605 | pubmed:dateCreated | 1992-2-18 | lld:pubmed |
| pubmed-article:1370605 | pubmed:abstractText | To study morphogenetic events of rotavirus SA11-infected MA104 cells with strictly defined reagents we produced monoclonal antibodies against synthetic peptides from both outer capsid proteins VP4 (aa residues 228-241: QNTRNIVPVSIVSR) and VP7 (aa residues 319-326: SAAFYYRV) of simian rotavirus SA11. Two of the selected monoclonal antibodies proved to be reactive with determinants of SA11-infected MA104 rhesus monkey kidney cells, with purified SA11 as well as with the particular peptides used for immunization. The anti-VP4 antibody had a demonstrable neutralizing titer of 200 (50% focus reduction) whereas the anti-VP7 MuMAb revealed no detectable neutralizing activity. In peptide-inhibition experiments, the corresponding peptide inhibited its MuMAb whereas the noncorresponding peptide had no effect on antibody binding to intracellular viral antigen. Localization of VP7 was preceded by VP4 as shown by immunofluorescence microscopy. | lld:pubmed |
| pubmed-article:1370605 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1370605 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1370605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370605 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1370605 | pubmed:issn | 0304-8608 | lld:pubmed |
| pubmed-article:1370605 | pubmed:author | pubmed-author:HansenGG | lld:pubmed |
| pubmed-article:1370605 | pubmed:author | pubmed-author:WerchauHH | lld:pubmed |
| pubmed-article:1370605 | pubmed:author | pubmed-author:MehnertFF | lld:pubmed |
| pubmed-article:1370605 | pubmed:author | pubmed-author:StreckertH... | lld:pubmed |
| pubmed-article:1370605 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1370605 | pubmed:volume | 122 | lld:pubmed |
| pubmed-article:1370605 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1370605 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1370605 | pubmed:pagination | 281-91 | lld:pubmed |
| pubmed-article:1370605 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:meshHeading | pubmed-meshheading:1370605-... | lld:pubmed |
| pubmed-article:1370605 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1370605 | pubmed:articleTitle | Monoclonal antipeptide antibodies recognize epitopes upon VP4 and VP7 of simian rotavirus SA11 in infected MA104 cells. | lld:pubmed |
| pubmed-article:1370605 | pubmed:affiliation | Institut für Hygiene und Mikrobiologie, Ruhr-Universität Bochum, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:1370605 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1370605 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
