| pubmed-article:10090724 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10090724 | lifeskim:mentions | umls-concept:C0012860 | lld:lifeskim |
| pubmed-article:10090724 | lifeskim:mentions | umls-concept:C0090388 | lld:lifeskim |
| pubmed-article:10090724 | lifeskim:mentions | umls-concept:C1332753 | lld:lifeskim |
| pubmed-article:10090724 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:10090724 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:10090724 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:10090724 | pubmed:dateCreated | 1999-4-15 | lld:pubmed |
| pubmed-article:10090724 | pubmed:abstractText | The protein kinase Chk1 is required for cell cycle arrest in response to DNA damage. We have found that the 14-3-3 proteins Rad24 and Rad25 physically interact with Chk1 in fission yeast. Association of Chk1 with 14-3-3 proteins is stimulated in response to DNA damage. DNA damage results in phosphorylation of Chk1 and the 14-3-3 proteins bind preferentially to the phosphorylated form. Genetic analysis has independently implicated both Rad24 and Rad25 in the DNA-damage checkpoint pathway. We suggest that DNA damage-dependent association of phosphorylated Chk1 with 14-3-3 proteins mediates an important step along the DNA-damage checkpoint pathway, perhaps by directing Chk1 to a particular substrate or to a particular location within the cell. An additional role for 14-3-3 proteins in the DNA-damage checkpoint has been suggested based on the observation that human Chk1 can phosphorylate Cdc25C in vitro creating a 14-3-3 binding site. Our results suggest that in fission yeast the interaction between the 14-3-3 proteins and Cdc25 does not require Chk1 function and is unaffected by DNA damage, in sharp contrast to the interaction between the 14-3-3 proteins and Chk1. | lld:pubmed |
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| pubmed-article:10090724 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10090724 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10090724 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10090724 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10090724 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:10090724 | pubmed:author | pubmed-author:ChenLL | lld:pubmed |
| pubmed-article:10090724 | pubmed:author | pubmed-author:RAON VNV | lld:pubmed |
| pubmed-article:10090724 | pubmed:author | pubmed-author:WalworthN CNC | lld:pubmed |
| pubmed-article:10090724 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10090724 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10090724 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:10090724 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10090724 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10090724 | pubmed:pagination | 675-85 | lld:pubmed |
| pubmed-article:10090724 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:10090724 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10090724 | pubmed:articleTitle | Association of Chk1 with 14-3-3 proteins is stimulated by DNA damage. | lld:pubmed |
| pubmed-article:10090724 | pubmed:affiliation | Department of Pharmacology, University of Medicine and Dentistry of New Jersey (UMDNJ)-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA. | lld:pubmed |
| pubmed-article:10090724 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10090724 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10090724 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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