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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6508
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pubmed:dateCreated |
1995-1-17
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pubmed:databankReference |
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pubmed:abstractText |
Production of interleukin-1 and tumour necrosis factor from stimulated human monocytes is inhibited by a new series of pyridinyl-imidazole compounds. Using radiolabelled and radio-photoaffinity-labelled chemical probes, the target of these compounds was identified as a pair of closely related mitogen-activated protein kinase homologues, termed CSBPs. Binding of the pyridinyl-imidazole compounds inhibited CSBP kinase activity and could be directly correlated with their ability to inhibit cytokine production, suggesting that the CSBPs are critical for cytokine production.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Imidazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Inflammation Mediators,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...
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pubmed:status |
MEDLINE
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
372
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
739-46
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7997261-Amino Acid Sequence,
pubmed-meshheading:7997261-Base Sequence,
pubmed-meshheading:7997261-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:7997261-Cell Line,
pubmed-meshheading:7997261-Chromosomes, Human, Pair 6,
pubmed-meshheading:7997261-Cloning, Molecular,
pubmed-meshheading:7997261-Cytokines,
pubmed-meshheading:7997261-DNA, Complementary,
pubmed-meshheading:7997261-Humans,
pubmed-meshheading:7997261-Imidazoles,
pubmed-meshheading:7997261-Inflammation Mediators,
pubmed-meshheading:7997261-Interleukin-1,
pubmed-meshheading:7997261-Mitogen-Activated Protein Kinases,
pubmed-meshheading:7997261-Molecular Sequence Data,
pubmed-meshheading:7997261-Monocytes,
pubmed-meshheading:7997261-Peptide Fragments,
pubmed-meshheading:7997261-Pyridines,
pubmed-meshheading:7997261-Radioligand Assay,
pubmed-meshheading:7997261-Recombinant Proteins,
pubmed-meshheading:7997261-Tumor Necrosis Factor-alpha,
pubmed-meshheading:7997261-p38 Mitogen-Activated Protein Kinases
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pubmed:articleTitle |
A protein kinase involved in the regulation of inflammatory cytokine biosynthesis.
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pubmed:affiliation |
Department of Cellular Biochemistry, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406.
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pubmed:publicationType |
Journal Article
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