| pubmed-article:8662896 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C1337034 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C0205216 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C1150566 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:8662896 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8662896 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:8662896 | pubmed:dateCreated | 1996-8-20 | lld:pubmed |
| pubmed-article:8662896 | pubmed:abstractText | Three proteins known to play a critical role in mammalian DNA double-strand break repair and lymphoid V(D)J recombination are the autoantigens Ku86 and Ku70 and a 465-kDa serine/threonine protein kinase catalytic subunit (DNA-PKcs). These proteins physically associate to form a complex (DNA.PK) with DNA-dependent protein kinase activity. In this study, we demonstrate using electrophoretic mobility shift assays (EMSAs) that the nuclear DNA end-binding activity of Ku is altered in the human promyelocytic leukemic HL-60 cell line. Western blot and EMSA supershift analyses revealed that HL-60 cells expressed both full-length and variant Ku86 proteins. However, a combined EMSA and immunoanalysis revealed that the Ku heterodimers complexed with DNA in HL-60 cells contained only the variant Ku86 proteins. Finally, UV cross-linking experiments and DNA.PK assays demonstrated that the Ku complexes containing variant Ku86 had a greatly reduced ability to interact with DNA-PKcs and that consequently HL-60 cells had severely diminished DNA.K activity. These data provide important insights into the interaction between Ku and DNA-PKcs and into the role of DNA.PK in DNA double-strand break repair. | lld:pubmed |
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| pubmed-article:8662896 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8662896 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8662896 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8662896 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8662896 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8662896 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8662896 | pubmed:author | pubmed-author:CarterTT | lld:pubmed |
| pubmed-article:8662896 | pubmed:author | pubmed-author:JohnstonCC | lld:pubmed |
| pubmed-article:8662896 | pubmed:author | pubmed-author:WycheJ HJH | lld:pubmed |
| pubmed-article:8662896 | pubmed:author | pubmed-author:HaoYY | lld:pubmed |
| pubmed-article:8662896 | pubmed:author | pubmed-author:ReevesW HWH | lld:pubmed |
| pubmed-article:8662896 | pubmed:author | pubmed-author:HendricksonE... | lld:pubmed |
| pubmed-article:8662896 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8662896 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:8662896 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8662896 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8662896 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8662896 | pubmed:pagination | 14098-104 | lld:pubmed |
| pubmed-article:8662896 | pubmed:dateRevised | 2011-4-12 | lld:pubmed |
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| pubmed-article:8662896 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8662896 | pubmed:articleTitle | Characterization of a Ku86 variant protein that results in altered DNA binding and diminished DNA-dependent protein kinase activity. | lld:pubmed |
| pubmed-article:8662896 | pubmed:affiliation | Department of Molecular Biology, Brown University, Providence, Rhode Island 02912, USA. | lld:pubmed |
| pubmed-article:8662896 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8662896 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8662896 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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