MersV1, Main, Exploration, bibRecord, 004C18

Multiple and cooperative trans -activation domains of the human glucocorticoid receptor

Identifieur interne : 004C18 ( Main/Exploration ); précédent : 004C17; suivant : 004C19

Multiple and cooperative trans -activation domains of the human glucocorticoid receptor

Auteurs : Stanley M. Hollenberg [États-Unis] ; Ronald M. Evans [États-Unis]

Source :

Cell [ 0092-8674 ] ; 1988.

RBID : ISTEX:FECAD15F94E5DCFCD4923776338D7391998E6864

English descriptors

Teeft :
- Acidic, Activation, Activation domains, Activator, Amino, Amino acid, Amino acids, Amino terminus, Bamhl, Bamhl site, Binding, Binding domain, Binding domains, Carboxyl terminus, Chambon, Common mechanism, Deletion, Derivative, Domain, Eukaryotic, Functional analysis, Gal4, Ggalg, Glucocorticoid, Glucocorticoid receptor, Glycine, Hollenberg, Hormone binding domain, Howard hughes, Human glucocorticoid receptor, Hybrid, Luciferase, Mutagenesis, Mutant, Plasmid, Promoter, Ptashne, Receptor, Specific binding, Steroid, Terminus, Transcription, Transcriptional, Transcriptional activation, Yeast, Yeast gal4.

Abstract

Abstract: A 30 amino acid peptide (referred to as τ2) that functions as an activation domain has been localized in the carboxyl terminus of the human glucocorticoid receptor. This sequence, when fused to yeast GAL4 as part of the ligand binding domain, generates a hormone-inducible activator. τ2 functions in a position-independent fashion and leads to a progressive gain of function when multimerized. A similar and independent activity has also been identified in the amino terminus of the receptor. These two sequences, although structurally unrelated, are both acidic in character and thus may have certain properties in common with yeast activator sequences.

Url:

https://api.istex.fr/ark:/67375/6H6-WXLJX754-H/fulltext.pdf

DOI: 10.1016/0092-8674(88)90145-6

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Istex, to step Corpus: 002017
to stream Istex, to step Curation: 002017
to stream Istex, to step Checkpoint: 002105
to stream Main, to step Merge: 004C98
to stream Main, to step Curation: 004C18

Le document en format XML

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<term>Amino acid</term>
<term>Amino acids</term>
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<term>Bamhl site</term>
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<term>Binding domain</term>
<term>Binding domains</term>
<term>Carboxyl terminus</term>
<term>Chambon</term>
<term>Common mechanism</term>
<term>Deletion</term>
<term>Derivative</term>
<term>Domain</term>
<term>Eukaryotic</term>
<term>Functional analysis</term>
<term>Gal4</term>
<term>Ggalg</term>
<term>Glucocorticoid</term>
<term>Glucocorticoid receptor</term>
<term>Glycine</term>
<term>Hollenberg</term>
<term>Hormone binding domain</term>
<term>Howard hughes</term>
<term>Human glucocorticoid receptor</term>
<term>Hybrid</term>
<term>Luciferase</term>
<term>Mutagenesis</term>
<term>Mutant</term>
<term>Plasmid</term>
<term>Promoter</term>
<term>Ptashne</term>
<term>Receptor</term>
<term>Specific binding</term>
<term>Steroid</term>
<term>Terminus</term>
<term>Transcription</term>
<term>Transcriptional</term>
<term>Transcriptional activation</term>
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<front><div type="abstract" xml:lang="en">Abstract: A 30 amino acid peptide (referred to as τ2) that functions as an activation domain has been localized in the carboxyl terminus of the human glucocorticoid receptor. This sequence, when fused to yeast GAL4 as part of the ligand binding domain, generates a hormone-inducible activator. τ2 functions in a position-independent fashion and leads to a progressive gain of function when multimerized. A similar and independent activity has also been identified in the amino terminus of the receptor. These two sequences, although structurally unrelated, are both acidic in character and thus may have certain properties in common with yeast activator sequences.</div>
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Multiple and cooperative trans -activation domains of the human glucocorticoid receptor

Multiple and cooperative trans -activation domains of the human glucocorticoid receptor

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri