pubmed-article:8383250 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0206679 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C1261468 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:8383250 | lifeskim:mentions | umls-concept:C0205231 | lld:lifeskim |
pubmed-article:8383250 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:8383250 | pubmed:dateCreated | 1993-4-8 | lld:pubmed |
pubmed-article:8383250 | pubmed:abstractText | Three amber mutations were introduced proximal to the syn3 locus of the herpes simplex virus type 1 glycoprotein B (gB) gene specifying gB derivatives lacking the carboxy-terminal 28, 49, or 64 amino acids. A complementation system that utilized gBs expressed in COS cells to complement gB-null virus K delta T was established. The 49- or 64-amino-acid-truncated gBs failed to complement gB-null virus K delta T, while the 28-amino-acid-truncated gB complemented K delta T efficiently. Mutant herpes simplex virus type 1 KOS (amb1511-7) specifying the 28-amino-acid-truncated gB fused Vero cells extensively. | lld:pubmed |
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pubmed-article:8383250 | pubmed:language | eng | lld:pubmed |
pubmed-article:8383250 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8383250 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8383250 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8383250 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8383250 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:8383250 | pubmed:author | pubmed-author:HuangLL | lld:pubmed |
pubmed-article:8383250 | pubmed:author | pubmed-author:KousoulasK... | lld:pubmed |
pubmed-article:8383250 | pubmed:author | pubmed-author:NewmanSS | lld:pubmed |
pubmed-article:8383250 | pubmed:author | pubmed-author:BaghianAA | lld:pubmed |
pubmed-article:8383250 | pubmed:author | pubmed-author:JayachandraSS | lld:pubmed |
pubmed-article:8383250 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8383250 | pubmed:volume | 67 | lld:pubmed |
pubmed-article:8383250 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8383250 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8383250 | pubmed:pagination | 2396-401 | lld:pubmed |
pubmed-article:8383250 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8383250 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8383250 | pubmed:articleTitle | Truncation of the carboxy-terminal 28 amino acids of glycoprotein B specified by herpes simplex virus type 1 mutant amb1511-7 causes extensive cell fusion. | lld:pubmed |
pubmed-article:8383250 | pubmed:affiliation | Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge 70803-8416. | lld:pubmed |
pubmed-article:8383250 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8383250 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:8383250 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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