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rdf:type |
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lifeskim:mentions |
umls-concept:C0012854,
umls-concept:C0037791,
umls-concept:C0205095,
umls-concept:C0678594,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1334043,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2349209,
umls-concept:C2825311
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pubmed:issue |
7
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pubmed:dateCreated |
1999-10-19
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pubmed:databankReference |
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pubmed:abstractText |
NF-kappa B/Rel transcription factors play important roles in immunity and development in mammals and insects. Their activity is regulated by their cellular localization, homo- and heterodimerization and association with other factors on their target gene promoters. Gambif1 from Anopheles gambiae is a member of the Rel family and a close homologue of the morphogen Dorsal, which establishes dorsoventral polarity in the Drosophila embryo.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Gambif1 protein, Anopheles gambiae,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/dl (dorsal) protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
841-52
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pubmed:dateRevised |
2008-10-15
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pubmed:meshHeading |
pubmed-meshheading:10425685-Amino Acid Sequence,
pubmed-meshheading:10425685-Animals,
pubmed-meshheading:10425685-Base Sequence,
pubmed-meshheading:10425685-Binding Sites,
pubmed-meshheading:10425685-Crystallography, X-Ray,
pubmed-meshheading:10425685-DNA-Binding Proteins,
pubmed-meshheading:10425685-Dimerization,
pubmed-meshheading:10425685-Drosophila Proteins,
pubmed-meshheading:10425685-Humans,
pubmed-meshheading:10425685-Insect Proteins,
pubmed-meshheading:10425685-Models, Molecular,
pubmed-meshheading:10425685-Molecular Sequence Data,
pubmed-meshheading:10425685-Nuclear Proteins,
pubmed-meshheading:10425685-Phosphoproteins,
pubmed-meshheading:10425685-Protein Conformation,
pubmed-meshheading:10425685-Sequence Homology, Amino Acid,
pubmed-meshheading:10425685-Solutions,
pubmed-meshheading:10425685-Trans-Activators,
pubmed-meshheading:10425685-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Structure of the specificity domain of the Dorsal homologue Gambif1 bound to DNA.
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pubmed:affiliation |
European Molecular Biology Laboratory, Grenoble Outstation, France.
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pubmed:publicationType |
Journal Article
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