Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.21 (thymidine kinase)
 7,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The secretion of thymidine by mononuclear phagocytes was correlated with the activity of the enzyme thymidine kinase (TK). Macrophages cultured in regular tissue culture medium released thymidine and did not express TK. However, when macrophages were incubated with medium conditioned by L cells, they expressed TK, incorporated 3H thymidine into trichloroacetic acid precipitable material, and ceased to secrete the nucleotide. Furthermore, replicating P388/D1 cells were induced to secrete thymidine by inhibiting TK with d-glucosamine. These results have demonstrated an inverse relationship between thymidine secretion and the expression of TK. They suggest that thymidine secretion by macrophages may be attributed to their lack of TK activity.
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PMID:The regulation of thymidine secretion by macrophages. 45 47

The major glycoprotein, G, of human respiratory syncytial (RS) virus is a Mr 84,000-90,000 species that has about 60% of its mass contributed by carbohydrate, most of which is in the form of O-linked oligosaccharides. The G protein contains neither a hydrophobic N-terminal signal sequence nor a hydrophobic C-terminal anchor region. Instead, its amino acid sequence reveals only one region with significant hydrophobic character, which is between residues 38 and 66. In order to study the synthesis, processing, and functions of this unusual viral glycoprotein, full-length cDNA copies of the G protein mRNA were inserted into the DNA genome of vaccinia virus (VV) in a position that was adjacent to a strong VV promoter and within the VV gene for thymidine kinase (TK). The resulting TK- recombinant viruses were selected, plaque-purified, and characterized by Southern blot analysis of restriction enzyme digests of the viral DNA. Recombinant RNA transcripts that contained both G-specific and VV-specific sequences accumulated in cells infected with recombinant viruses having the G protein gene in the positive orientation. The translation product of these transcripts in infected cells was a Mr 84,000-90,000 glycoprotein that was indistinguishable from authentic RS virus G protein. It could be detected in cell lysates after metabolic labeling with [3H]glucosamine and was immunoprecipitated by anti-RS-virus antiserum. Immunofluorescence studies showed that the G protein accumulated intracellularly with the perinuclear distribution that is characteristic of newly synthesized glycoproteins. Furthermore, the protein was also clearly detectable on the surface of recombinant-infected cells, showing that it was transported to and inserted into the plasma membrane.
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PMID:Expression of the major glycoprotein G of human respiratory syncytial virus from recombinant vaccinia virus vectors. 345 62

(E)-5-(2-Bromovinyl)-2'-deoxyuridine (BVdU) was phosphorylated by the bovine herpesvirus 1 (BHV-1)-induced thymidine kinase and subsequently incorporated into viral DNA, resulting in DNA that was more dense than DNA from untreated cells. Incorporation of the drug did not result in the termination of replicating BHV-1 DNA molecules since radioactively labeled DNA synthesized in drug-treated and untreated cells sedimented at similar rates in alkaline sucrose gradients. No differences were observed in the electrophoretic mobility of [35S]methionine-labeled viral polypeptides synthesized in treated and untreated cells, although [3H]glucosamine-labeled viral glycoproteins synthesized in treated cells were of a lower molecular weight than those in untreated cells. In BVdU-treated cells, unlike untreated cells, immature neutral and basic precursors of the mature viral glycoproteins accumulated. Although BVdU-treated and untreated cells contained similar amounts of virus, very little virus was released into the culture supernatant from BVdU-treated cells. Our results suggest that BVdU partially inhibits the glycosylation of BHV-1 glycoproteins. BVdU-sensitive glycosylation, however, is not necessary for expression of these glycoproteins on the surface of infected cells since the glycoproteins could be labeled on intact cells with 125I and because BVdU-treated cells remained sensitive to antibody-dependent, cell-mediated cytotoxity mediated by anti-BHV-1 serum. The phosphorylation of BVdU was a prerequisite for its effect on glycosylation since the glycoproteins of a thymidine kinase-deficient mutant of BHV-1 were not affected.
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PMID:Inhibition of glycosylation of bovine herpesvirus 1 glycoproteins by the thymidine analog (E)-5-(2 Bromovinyl)-2'-deoxyuridine. 661 91