Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
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...
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| Veröffentlicht in: | Cell 1988-12, Vol.55 (5), p.899-906 |
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| container_title | Cell |
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| creator | Hollenberg, Stanley M. Evans, Ronald M. |
| description | 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. |
| doi_str_mv | 10.1016/0092-8674(88)90145-6 |
| format | Article |
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Psychology</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Promoter Regions, Genetic</subject><subject>Receptors, Glucocorticoid - physiology</subject><subject>Transcription Factors - physiology</subject><subject>Transcription, Genetic</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1r3DAQhkVJ2WzS_oMGdAghObiVLMmSL4Gw5KOQ0kvbq5ClcaNgW44kB_rvo-0ue8xpmHmfGYYHoS-UfKWENt8IaetKNZJfKnXVEspF1XxAa0paWXEq6yO0PiDH6CSlZ0KIEkKs0IrRlgpG1-jPj2XIfh4Am8lhG8IM0WT_CjhHM6XK2NKUQZiwC6PxU8Khx_kJ8NMymgn_HRYbbIjZ2-AdjmBhziF-Qh97MyT4vK-n6Pfd7a_NQ_X48_775uaxslzUuWoFN0w52jau63pgdd84WdedFdAR2RpwPSiumOycITXvWSNaIgUxHTdCOMtO0cXu7hzDywIp69EnC8NgJghL0lIJVhPOCsh3oI0hpQi9nqMfTfynKdFbnXrrSm9daaX0f526KWtn-_tLN4I7LO39lfx8n5tkzdAXZ9anA9ZIKQQlBbveYVBcvHqIOlkPkwXni7GsXfDv__EGJ6GSbA</recordid><startdate>19881202</startdate><enddate>19881202</enddate><creator>Hollenberg, Stanley M.</creator><creator>Evans, Ronald M.</creator><general>Elsevier Inc</general><general>Cell Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19881202</creationdate><title>Multiple and cooperative trans-activation domains of the human glucocorticoid receptor</title><author>Hollenberg, Stanley M. ; Evans, Ronald M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-954a38d196dbbfe32f6d722bc5eb079aedfe84837bda024f36590750ab4a55dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cloning, Molecular</topic><topic>DNA - metabolism</topic><topic>DNA Mutational Analysis</topic><topic>DNA-Binding Proteins - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Promoter Regions, Genetic</topic><topic>Receptors, Glucocorticoid - physiology</topic><topic>Transcription Factors - physiology</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hollenberg, Stanley M.</creatorcontrib><creatorcontrib>Evans, Ronald M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hollenberg, Stanley M.</au><au>Evans, Ronald M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple and cooperative trans-activation domains of the human glucocorticoid receptor</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1988-12-02</date><risdate>1988</risdate><volume>55</volume><issue>5</issue><spage>899</spage><epage>906</epage><pages>899-906</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><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. 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| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 1988-12, Vol.55 (5), p.899-906 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Binding Sites Biological and medical sciences Cell receptors Cell structures and functions Cloning, Molecular DNA - metabolism DNA Mutational Analysis DNA-Binding Proteins - physiology Fundamental and applied biological sciences. Psychology Humans In Vitro Techniques Molecular and cellular biology Molecular Sequence Data Promoter Regions, Genetic Receptors, Glucocorticoid - physiology Transcription Factors - physiology Transcription, Genetic |
| title | Multiple and cooperative trans-activation domains of the human glucocorticoid receptor |
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