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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-6-21
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pubmed:abstractText |
In transient co-transfection assays, there is extensive cross-interaction between glucocorticoid receptor (GR) domains. For example, mutation of the conserved Ile residue at position 484 (rat GR map) to cysteine allows a net separation of transactivation and DNA binding. We also observed that the ligand binding domain plays a key role in cooperative transactivation. Furthermore, some carboxy-located mutations markedly alter the response of GR to agonists and antagonists. Finally, different reading frames of the CAG repeat that normally produces an amino-located poly-Gln repeat profoundly affect GR transactivation without altering DNA or ligand binding. This trans-dominant negative phenotype, seen when the CAG repeat yields a poly-Ala stretch, may turn out to be an excellent tool for functional analysis of GR in transgenic organisms.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0039-128X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
148-52
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8191545-Amino Acid Sequence,
pubmed-meshheading:8191545-Base Sequence,
pubmed-meshheading:8191545-Binding Sites,
pubmed-meshheading:8191545-DNA,
pubmed-meshheading:8191545-Enhancer Elements, Genetic,
pubmed-meshheading:8191545-Molecular Sequence Data,
pubmed-meshheading:8191545-Mutation,
pubmed-meshheading:8191545-Promoter Regions, Genetic,
pubmed-meshheading:8191545-Receptors, Glucocorticoid,
pubmed-meshheading:8191545-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8191545-Transcriptional Activation,
pubmed-meshheading:8191545-Transfection,
pubmed-meshheading:8191545-Zinc Fingers
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pubmed:year |
1994
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pubmed:articleTitle |
Active, interactive, and inactive steroid receptor mutants.
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pubmed:affiliation |
Institüt für Molekularbiologie II der Universität Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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