| pubmed-article:7958847 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7958847 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:7958847 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7958847 | lifeskim:mentions | umls-concept:C1511029 | lld:lifeskim |
| pubmed-article:7958847 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:7958847 | pubmed:dateCreated | 1994-12-1 | lld:pubmed |
| pubmed-article:7958847 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7958847 | pubmed:abstractText | We describe a novel zinc finger protein, ZID (zinc finger protein with interaction domain). At its amino terminus ZID contains a 120-amino-acid conserved motif present in a large family of proteins that includes both the otherwise unrelated zinc finger proteins, such as Ttk, GAGA, and ZF5, and a group of poxvirus proteins: We therefore refer to this domain as the POZ (poxvirus and zinc finger) domain. The POZ domains of ZID, Ttk, and GAGA act to inhibit the interaction of their associated finger regions with DNA. This inhibitory effect is not dependent on interactions with other proteins and does not appear dependent on specific interactions between the POZ domain and the finger region. The POZ domain acts as a specific protein-protein interaction domain: The POZ domains of ZID and Ttk can interact with themselves but not with each other, POZ domains from ZF5, or the viral protein SalF17R. However, the POZ domain of GAGA can interact efficiently with the POZ domain of Ttk. In transfection experiments, the ZID POZ domain inhibits DNA binding in NIH-3T3 cells and appears to localize the protein to discrete regions of the nucleus. We discuss the implications of multimerization for the function of POZ domain proteins. | lld:pubmed |
| pubmed-article:7958847 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7958847 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7958847 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7958847 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7958847 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:7958847 | pubmed:author | pubmed-author:TreismanRR | lld:pubmed |
| pubmed-article:7958847 | pubmed:author | pubmed-author:BardwellV JVJ | lld:pubmed |
| pubmed-article:7958847 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7958847 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7958847 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:7958847 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7958847 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7958847 | pubmed:pagination | 1664-77 | lld:pubmed |
| pubmed-article:7958847 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:7958847 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7958847 | pubmed:articleTitle | The POZ domain: a conserved protein-protein interaction motif. | lld:pubmed |
| pubmed-article:7958847 | pubmed:affiliation | Imperial Cancer Research Fund Laboratories, London, UK. | lld:pubmed |
| pubmed-article:7958847 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7958847 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7958847 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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