pubmed-article:18603589 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18603589 | lifeskim:mentions | umls-concept:C1512977 | lld:lifeskim |
pubmed-article:18603589 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:18603589 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
pubmed-article:18603589 | lifeskim:mentions | umls-concept:C0017817 | lld:lifeskim |
pubmed-article:18603589 | lifeskim:mentions | umls-concept:C0011209 | lld:lifeskim |
pubmed-article:18603589 | lifeskim:mentions | umls-concept:C0301869 | lld:lifeskim |
pubmed-article:18603589 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:18603589 | pubmed:dateCreated | 2008-10-6 | lld:pubmed |
pubmed-article:18603589 | pubmed:abstractText | The glutathione S-transferase (GST)-fused protein expression system has been extensively used to generate a large quantity of proteins and has served for functional analysis in vitro. In this study, we developed a novel approach for the efficient intracellular delivery of GST-fused proteins into living cells to expand their usefulness up to in vivo use. Since protein cationization techniques are powerful strategies for efficient intracellular uptake by adsorptive-mediated endocytosis, GST-fused proteins were cationized by forming a complex with a polycationic polyethylenimine (PEI)-glutathione conjugate. On screening of protein transduction, optimized PEI-glutathione conjugate for protein transduction was characterized by a partly oligomerized mixture of PEI with average molecular masses of 600 (PEI600) modified with multiple glutathiones, which could have sufficient avidity for GST. Furthermore, enhanced endosomal escape of transduced GST-fused proteins was observed when they were delivered with a glutathione-conjugated PEI600 derivative possessing a hydroxybutenyl moiety. These results were confirmed by both intracellular confocal imaging of GST-fused green fluorescent protein and activation of an endogenous growth signal transduction pathway by a GST-fused constitutively active mutant of a kinase protein. These PEI-glutathione conjugates seem to be convenient molecular tools for protein transduction of widely used GST-fused proteins. | lld:pubmed |
pubmed-article:18603589 | pubmed:language | eng | lld:pubmed |
pubmed-article:18603589 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18603589 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18603589 | pubmed:month | Oct | lld:pubmed |
pubmed-article:18603589 | pubmed:issn | 0021-924X | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:KitazoeMidori... | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:TadaHirokoH | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:YamadaHidenor... | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:SenoMasaharuM | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:SakaguchiMasa... | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:HuhNam-hoNH | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:FutamiJunichi... | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:KosakaMegumiM | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:MurataHitoshi... | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:YagiYasuyukiY | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:YoneharaTakay... | lld:pubmed |
pubmed-article:18603589 | pubmed:author | pubmed-author:NakanishiHide... | lld:pubmed |
pubmed-article:18603589 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18603589 | pubmed:volume | 144 | lld:pubmed |
pubmed-article:18603589 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18603589 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18603589 | pubmed:pagination | 447-55 | lld:pubmed |
pubmed-article:18603589 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:18603589 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18603589 | pubmed:articleTitle | Intracellular delivery of glutathione S-transferase-fused proteins into mammalian cells by polyethylenimine-glutathione conjugates. | lld:pubmed |
pubmed-article:18603589 | pubmed:affiliation | Department of Bioscience and Biotechnology, Faculty of Engineering, Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan. | lld:pubmed |
pubmed-article:18603589 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18603589 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18603589 | lld:pubmed |