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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1992-12-15
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pubmed:abstractText |
Interferon is a key substance of the cytokine network, and is functioning not only as the virus inhibitory factor, but also as the factor for differentiation, development, and homeostasis of animals, including man. The molecular structure, induction mechanisms, interaction with receptor, and antiviral action mechanisms of IFN were reviewed. 1. Molecular structure of IFN IFNs are now divided into 4 types--alpha, beta, gamma, omega--according to antigenicities of IFN proteins, and to base sequence of their genes. The omega type was established officially on 1990 by the Nomenclature Committee of International Society for Interferon Research (ISIR). Also, the genes for HuIFNs were named as follows; HuIFN-A for HuIFN-alpha, HuIFN-B for HuIFN-beta, HuIFN-G for HuIFN-gamma, and HuIFN-W for HuIFN-omega. Nevertheless, the names of Type I IFN and Type II IFN are still valuable, since members of Type I IFN, alpha, beta, and omega, are similar in their molecular structures, and they share the common receptor (Type I IFN receptor), on the other hand, HuIFN-gamma (the only one member of Type II IFN) has different characteristics from the other IFNs, and binds to its specific receptor (Type II IFN receptor). However, it has been reported that both N-terminal and C-terminal of IFN protein of all types, participate in the binding of IFN to its receptor. 2. Induction mechanism of IFN. The factors, IRF-1 and IRF-2, were found to play an important role in IFN induction.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
jpn
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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/IRF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/IRF2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Regulatory Factor-1,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Regulatory Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interferon,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0047-1852
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1845-53
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pubmed:dateRevised |
2011-7-27
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pubmed:meshHeading |
pubmed-meshheading:1279237-Amino Acid Sequence,
pubmed-meshheading:1279237-Base Sequence,
pubmed-meshheading:1279237-DNA-Binding Proteins,
pubmed-meshheading:1279237-Gene Expression Regulation,
pubmed-meshheading:1279237-Humans,
pubmed-meshheading:1279237-Interferon Regulatory Factor-1,
pubmed-meshheading:1279237-Interferon Regulatory Factor-2,
pubmed-meshheading:1279237-Interferons,
pubmed-meshheading:1279237-Molecular Sequence Data,
pubmed-meshheading:1279237-Phosphoproteins,
pubmed-meshheading:1279237-Receptors, Interferon,
pubmed-meshheading:1279237-Repressor Proteins,
pubmed-meshheading:1279237-Signal Transduction,
pubmed-meshheading:1279237-Transcription Factors
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pubmed:year |
1992
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pubmed:articleTitle |
[Function, molecular structure and gene expression of interferons].
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pubmed:affiliation |
Department of Microbiology, Asahikawa Medical College.
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pubmed:publicationType |
Journal Article,
English Abstract,
Review
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