| pubmed-article:11014197 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11014197 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:11014197 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:11014197 | lifeskim:mentions | umls-concept:C0002085 | lld:lifeskim |
| pubmed-article:11014197 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
| pubmed-article:11014197 | pubmed:issue | 6802 | lld:pubmed |
| pubmed-article:11014197 | pubmed:dateCreated | 2000-10-19 | lld:pubmed |
| pubmed-article:11014197 | pubmed:abstractText | Protein kinases have proved to be largely resistant to the design of highly specific inhibitors, even with the aid of combinatorial chemistry. The lack of these reagents has complicated efforts to assign specific signalling roles to individual kinases. Here we describe a chemical genetic strategy for sensitizing protein kinases to cell-permeable molecules that do not inhibit wild-type kinases. From two inhibitor scaffolds, we have identified potent and selective inhibitors for sensitized kinases from five distinct subfamilies. Tyrosine and serine/threonine kinases are equally amenable to this approach. We have analysed a budding yeast strain carrying an inhibitor-sensitive form of the cyclin-dependent kinase Cdc28 (CDK1) in place of the wild-type protein. Specific inhibition of Cdc28 in vivo caused a pre-mitotic cell-cycle arrest that is distinct from the G1 arrest typically observed in temperature-sensitive cdc28 mutants. The mutation that confers inhibitor-sensitivity is easily identifiable from primary sequence alignments. Thus, this approach can be used to systematically generate conditional alleles of protein kinases, allowing for rapid functional characterization of members of this important gene family. | lld:pubmed |
| pubmed-article:11014197 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11014197 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11014197 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11014197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11014197 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11014197 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11014197 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:MorganD ODO | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:WoodJ LJL | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:RoseM DMD | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:ShimizuEE | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:BishopA CAC | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:SchultzP GPG | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:GrayN SNS | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:ShokatK MKM | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:TsienJ ZJZ | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:MatheosD PDP | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:BlethrowJJ | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:UbersaxJ AJA | lld:pubmed |
| pubmed-article:11014197 | pubmed:author | pubmed-author:PetschD TDT | lld:pubmed |
| pubmed-article:11014197 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11014197 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:11014197 | pubmed:volume | 407 | lld:pubmed |
| pubmed-article:11014197 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11014197 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11014197 | pubmed:pagination | 395-401 | lld:pubmed |
| pubmed-article:11014197 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:11014197 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11014197 | pubmed:articleTitle | A chemical switch for inhibitor-sensitive alleles of any protein kinase. | lld:pubmed |
| pubmed-article:11014197 | pubmed:affiliation | Department of Chemistry, Princeton University, New Jersey 08544, USA. | lld:pubmed |
| pubmed-article:11014197 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11014197 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11014197 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11014197 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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