pubmed-article:8391184 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8391184 | lifeskim:mentions | umls-concept:C0019351 | lld:lifeskim |
pubmed-article:8391184 | lifeskim:mentions | umls-concept:C0033840 | lld:lifeskim |
pubmed-article:8391184 | lifeskim:mentions | umls-concept:C0682451 | lld:lifeskim |
pubmed-article:8391184 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:8391184 | lifeskim:mentions | umls-concept:C1422036 | lld:lifeskim |
pubmed-article:8391184 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8391184 | pubmed:dateCreated | 1993-7-23 | lld:pubmed |
pubmed-article:8391184 | pubmed:abstractText | I have examined the state of phosphorylation of the envelope glycoproteins of two neurotropic herpesviruses, HSV-2 and PRV. HSV-2 gE2 and PRV gI, which are the homologues to HSV-1 gE, were found to be phosphorylated and phosphoaminoacid analysis revealed that both contained phosphoserine. These findings are consistent with a conserved phosphorylation of the glycoprotein homologues to HSV gE among the neurotropic alphaherpesviruses. | lld:pubmed |
pubmed-article:8391184 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391184 | pubmed:language | eng | lld:pubmed |
pubmed-article:8391184 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391184 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8391184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391184 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8391184 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8391184 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:8391184 | pubmed:author | pubmed-author:EdsonC MCM | lld:pubmed |
pubmed-article:8391184 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8391184 | pubmed:volume | 195 | lld:pubmed |
pubmed-article:8391184 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8391184 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8391184 | pubmed:pagination | 268-70 | lld:pubmed |
pubmed-article:8391184 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:8391184 | pubmed:meshHeading | pubmed-meshheading:8391184-... | lld:pubmed |
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pubmed-article:8391184 | pubmed:meshHeading | pubmed-meshheading:8391184-... | lld:pubmed |
pubmed-article:8391184 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8391184 | pubmed:articleTitle | Phosphorylation of neurotropic alphaherpesvirus envelope glycoproteins: herpes simplex virus type 2 gE2 and pseudorabies virus gI. | lld:pubmed |
pubmed-article:8391184 | pubmed:affiliation | Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111. | lld:pubmed |
pubmed-article:8391184 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8391184 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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