pubmed-article:17316564 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:17316564 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
pubmed-article:17316564 | lifeskim:mentions | umls-concept:C1414351 | lld:lifeskim |
pubmed-article:17316564 | lifeskim:mentions | umls-concept:C1420371 | lld:lifeskim |
pubmed-article:17316564 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:17316564 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:17316564 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:17316564 | lifeskim:mentions | umls-concept:C0443220 | lld:lifeskim |
pubmed-article:17316564 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:17316564 | pubmed:dateCreated | 2007-3-6 | lld:pubmed |
pubmed-article:17316564 | pubmed:abstractText | To investigate the binding preference of eIF4E for the three eIF4E-binding isoforms (4E-BP1-3) and the function of N-terminal flexible region of eIF4E for their interactions, the binding parameters of recombinant full-length and N-terminal residues-deleted eIF4Es with 4E-BP1-3 were investigated by the surface plasmon resonance (SPR) analysis. Consequently, it was clarified that 4E-BP2 exhibits the highest binding affinity for both m7GTP-bound and -unbound full-length eIF4Es when compared with 4E-BP1 and 4E-BP3. This is primarily due to the difference among their dissociation rates, because their association rates are almost the same. Interestingly, the deletion of the 33 N-terminal residues of eIF4E increased its binding affinities for 4E-BP1 and 4E-BP2 markedly, whereas such a change was not observed by at least the N-terminal deletion up to 26 residues. In contrast, the binding parameters of 4E-BP3 were hardly influenced by N-terminal deletion up to 33 residues. From the comparison of the amino acid sequences of 4E-BP1-3, the present result indicates the importance of N-terminal flexible region of eIF4E for the suppressive binding with 4E-BP1 and 2, together with the possible contribution of N-terminal sequence of 4E-BP isoform to the regulative binding to eIF4E. | lld:pubmed |
pubmed-article:17316564 | pubmed:language | eng | lld:pubmed |
pubmed-article:17316564 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17316564 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17316564 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17316564 | pubmed:month | Apr | lld:pubmed |
pubmed-article:17316564 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:17316564 | pubmed:author | pubmed-author:MizunoAtsuoA | lld:pubmed |
pubmed-article:17316564 | pubmed:author | pubmed-author:TomooKojiK | lld:pubmed |
pubmed-article:17316564 | pubmed:author | pubmed-author:MorinoShigeno... | lld:pubmed |
pubmed-article:17316564 | pubmed:author | pubmed-author:IshidaToshima... | lld:pubmed |
pubmed-article:17316564 | pubmed:author | pubmed-author:ImatakaHiroak... | lld:pubmed |
pubmed-article:17316564 | pubmed:author | pubmed-author:AbikoFumiF | lld:pubmed |
pubmed-article:17316564 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17316564 | pubmed:day | 13 | lld:pubmed |
pubmed-article:17316564 | pubmed:volume | 355 | lld:pubmed |
pubmed-article:17316564 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17316564 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17316564 | pubmed:pagination | 667-72 | lld:pubmed |
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pubmed-article:17316564 | pubmed:meshHeading | pubmed-meshheading:17316564... | lld:pubmed |
pubmed-article:17316564 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17316564 | pubmed:articleTitle | Binding preference of eIF4E for 4E-binding protein isoform and function of eIF4E N-terminal flexible region for interaction, studied by SPR analysis. | lld:pubmed |
pubmed-article:17316564 | pubmed:affiliation | Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan. | lld:pubmed |
pubmed-article:17316564 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17316564 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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