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| http://purl.uniprot.org/citations/23485826 | http://www.w3.org/2000/01/rdf-schema#comment | "The CIDE domain is a well known protein-protein interaction module that is initially detected at the apoptotic DNA fragmentation factor (DFF40/45). The interaction mechanism via the CIDE domain is not well understood. To elucidate CIDE domain mediated interactions in the apoptotic DNA fragmentation system, we conducted biochemical and mutational studies and found that the surface of CIDE domains can be divided into an acidic side and a basic side. In addition, a mutagenesis study revealed that the basic surface side of Drep2 CIDE is involved in the interaction with the acidic surface side of Drep1 CIDE and Drep3 CIDE. Our research supports the idea that a charge-charge interaction might be the general interaction mode of the CIDE:CIDE interaction."xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2013.02.031"xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/author | "Lee S.M."xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/author | "Park H.H."xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/name | "FEBS Lett"xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/pages | "854-859"xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/title | "General interaction mode of CIDE:CIDE complex revealed by a mutation study of the Drep2 CIDE domain."xsd:string |
| http://purl.uniprot.org/citations/23485826 | http://purl.uniprot.org/core/volume | "587"xsd:string |
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