Endoplasmic Reticulum (ER)-Targeted, Galectin-Mediated Retrograde Transport by Using a HaloTag Carrier Protein
DC Field | Value | Language |
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dc.contributor.author | Son, Sang-Hyun | - |
dc.contributor.author | Seko, Akira | - |
dc.contributor.author | Daikoku, Shusaku | - |
dc.contributor.author | Fujikawa, Kohki | - |
dc.contributor.author | Suzuki, Katsuhiko | - |
dc.contributor.author | Ito, Yukishige | - |
dc.contributor.author | Kanie, Osamu | - |
dc.date.accessioned | 2021-09-04T00:50:00Z | - |
dc.date.available | 2021-09-04T00:50:00Z | - |
dc.date.created | 2021-06-17 | - |
dc.date.issued | 2016-04-01 | - |
dc.identifier.issn | 1439-4227 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/88958 | - |
dc.description.abstract | Investigations into metabolic processes within the cell have often relied on genetic methods such as forced expression and knockout or knockdown techniques. An alternative approach would be introducing a molecule into the desired location inside the cell. To translocate compounds from outside cells into the endoplasmic reticulum (ER), we constructed a delivery carrier protein. This comprised N-terminal galectin-1 for cell-surface binding (G1), a protease cleavable sequence (ps), a HaloTag domain for attaching exogenous compounds (Halo), and a C-terminal KDEL sequence for ER retention. Fluorescently labeled G1-ps-Halo-KDEL passed through the Golgi apparatus and reached the ER. By using Man(9)GlcNAc(2)-BODIPY as a cargo compound, the carrier protein was also delivered into the ER with concomitant processing of mannose to Man(5,6), by the ER-resident 1,2-mannosidase. G1-ps-Halo-KDEL might serve as a new type of delivery carrier protein to direct compounds into the ER. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.subject | SITE-DIRECTED MUTAGENESIS | - |
dc.subject | HEPATITIS-C VIRUS | - |
dc.subject | N-BUTYLDEOXYNOJIRIMYCIN | - |
dc.subject | QUALITY-CONTROL | - |
dc.subject | SHIGA TOXIN | - |
dc.subject | ER PROTEINS | - |
dc.subject | GLYCOPROTEIN | - |
dc.subject | DEGRADATION | - |
dc.subject | ENDOCYTOSIS | - |
dc.subject | CHAPERONES | - |
dc.title | Endoplasmic Reticulum (ER)-Targeted, Galectin-Mediated Retrograde Transport by Using a HaloTag Carrier Protein | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Son, Sang-Hyun | - |
dc.identifier.doi | 10.1002/cbic.201500489 | - |
dc.identifier.scopusid | 2-s2.0-84960146404 | - |
dc.identifier.wosid | 000373713000012 | - |
dc.identifier.bibliographicCitation | CHEMBIOCHEM, v.17, no.7, pp.630 - 639 | - |
dc.relation.isPartOf | CHEMBIOCHEM | - |
dc.citation.title | CHEMBIOCHEM | - |
dc.citation.volume | 17 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 630 | - |
dc.citation.endPage | 639 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Pharmacology & Pharmacy | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Medicinal | - |
dc.subject.keywordPlus | SITE-DIRECTED MUTAGENESIS | - |
dc.subject.keywordPlus | HEPATITIS-C VIRUS | - |
dc.subject.keywordPlus | N-BUTYLDEOXYNOJIRIMYCIN | - |
dc.subject.keywordPlus | QUALITY-CONTROL | - |
dc.subject.keywordPlus | SHIGA TOXIN | - |
dc.subject.keywordPlus | ER PROTEINS | - |
dc.subject.keywordPlus | GLYCOPROTEIN | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | ENDOCYTOSIS | - |
dc.subject.keywordPlus | CHAPERONES | - |
dc.subject.keywordAuthor | drug delivery | - |
dc.subject.keywordAuthor | endoplasmic reticulum | - |
dc.subject.keywordAuthor | galectin | - |
dc.subject.keywordAuthor | glycoproteins | - |
dc.subject.keywordAuthor | HaloTag | - |
dc.subject.keywordAuthor | retrograde delivery | - |
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