rdf:type |
|
lifeskim:mentions |
umls-concept:C0021311,
umls-concept:C0021469,
umls-concept:C0021747,
umls-concept:C0031715,
umls-concept:C0086982,
umls-concept:C0205548,
umls-concept:C0206679,
umls-concept:C0597721,
umls-concept:C0805732,
umls-concept:C1306673,
umls-concept:C1335960,
umls-concept:C1366753,
umls-concept:C1548425
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pubmed:issue |
1
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pubmed:dateCreated |
2001-7-12
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pubmed:abstractText |
We examined the influence on the interferon (IFN) signaling pathway of infection with herpes simplex virus type 1 (HSV-1) strain VR3. Data from reporter gene assays showed that expression of both type I and type II IFN-inducible genes was dramatically suppressed during the early stage of HSV-1 infection (2 to 3 h postinfection). During these periods, phosphorylation levels of janus kinases (JAKs) and STATs did not increase after treatment of HSV-1-infected FL cells with IFN-alpha or IFN-gamma, although cellular protein levels of the JAKs and the STATs were not significantly changed. In contrast, the inhibitory effect of HSV-1 on phosphorylation of STAT1 was not observed in U937 cells, which show resistance to steady-state accumulation of RNA for HSV-1 immediate-early genes. The phosphorylation of STAT1 in FL cells was not inhibited by infection with a UV-inactivated virus. These results indicate that viral gene expression or viral protein production is necessary for the inhibition of phosphorylation by HSV-1.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/JAK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/JAK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0042-6822
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
119-24
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11448165-DNA-Binding Proteins,
pubmed-meshheading:11448165-Herpes Simplex,
pubmed-meshheading:11448165-Herpesvirus 1, Human,
pubmed-meshheading:11448165-Humans,
pubmed-meshheading:11448165-Interferons,
pubmed-meshheading:11448165-Janus Kinase 1,
pubmed-meshheading:11448165-Janus Kinase 2,
pubmed-meshheading:11448165-Phosphorylation,
pubmed-meshheading:11448165-Protein-Tyrosine Kinases,
pubmed-meshheading:11448165-Proto-Oncogene Proteins,
pubmed-meshheading:11448165-STAT1 Transcription Factor,
pubmed-meshheading:11448165-Signal Transduction,
pubmed-meshheading:11448165-Trans-Activators,
pubmed-meshheading:11448165-U937 Cells,
pubmed-meshheading:11448165-Virus Replication
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pubmed:year |
2001
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pubmed:articleTitle |
Herpes simplex virus type 1 suppresses the interferon signaling pathway by inhibiting phosphorylation of STATs and janus kinases during an early infection stage.
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pubmed:affiliation |
Department of Microbiology, Sapporo Medical University School of Medicine, Chuo-ku, Sapporo, 060-8556, Japan. syokota@sapmed.ac.jp
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pubmed:publicationType |
Journal Article
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