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Development of Multiplexed Immuno-N-Terminomics to Reveal the Landscape of Proteolytic Processing in Early Embryogenesis of Drosophila melanogaster

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dc.contributor.authorSanghee Shin-
dc.contributor.authorJi Hye Hong-
dc.contributor.authorYongwoo Na-
dc.contributor.authorLee, Mihye-
dc.contributor.authorQian, Wei-Jun-
dc.contributor.authorV. Narry Kim-
dc.contributor.authorJong-Seo Kim-
dc.date.accessioned2021-01-08T08:30:03Z-
dc.date.accessioned2021-01-08T08:30:03Z-
dc.date.available2021-01-08T08:30:03Z-
dc.date.available2021-01-08T08:30:03Z-
dc.date.created2020-04-28-
dc.date.issued2020-04-
dc.identifier.issn0003-2700-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/9019-
dc.description.abstractProtein expression levels are regulated through both translation and degradation mechanisms. Levels of degradation intermediates, that is, partially degraded proteins, cannot be distinguished from those of intact proteins by global proteomics analysis, which quantify total protein abundance levels. This study aimed to develop a tool for assessing the aspects of degradation regulation via proteolytic processing through a new multiplexed Nterminomics method involving selective isobaric labeling of protein N-termini and immunoaffinity capture of the labeled N-terminal peptides. Our method allows for not only identification of proteolytic cleavage sites, but also highly multiplexed quantification of proteolytic processing. We profiled a number of potential cleavage sites by signal peptidase and provided experimental confirmation of predicted cleavage sites of signal peptide. Furthermore, the present method uniquely represents the landscape of proteomic proteolytic processing rate during early embryogenesis in Drosophila melanogaster, revealing the underlying mechanism of stringent decay regulation of zygotically expressed proteins during early stages of embryogenesis.-
dc.language영어-
dc.publisherAMER CHEMICAL SOC-
dc.titleDevelopment of Multiplexed Immuno-N-Terminomics to Reveal the Landscape of Proteolytic Processing in Early Embryogenesis of Drosophila melanogaster-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000526569200033-
dc.identifier.scopusid2-s2.0-85088924722-
dc.identifier.rimsid71995-
dc.contributor.affiliatedAuthorSanghee Shin-
dc.contributor.affiliatedAuthorJi Hye Hong-
dc.contributor.affiliatedAuthorYongwoo Na-
dc.contributor.affiliatedAuthorV. Narry Kim-
dc.contributor.affiliatedAuthorJong-Seo Kim-
dc.identifier.doi10.1021/acs.analchem.9b05035-
dc.identifier.bibliographicCitationANALYTICAL CHEMISTRY, v.92, no.7, pp.4926 - 4934-
dc.relation.isPartOfANALYTICAL CHEMISTRY-
dc.citation.titleANALYTICAL CHEMISTRY-
dc.citation.volume92-
dc.citation.number7-
dc.citation.startPage4926-
dc.citation.endPage4934-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalWebOfScienceCategoryChemistry, Analytical-
dc.subject.keywordPlusRNA-BINDING PROTEIN-
dc.subject.keywordPlusCLEAVAGE SITES-
dc.subject.keywordPlusALPHA-LACTALBUMIN-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusDENATURATION-
dc.subject.keywordPlusDEGRADOMICS-
dc.subject.keywordPlusTRANSITION-
dc.subject.keywordPlusPEPTIDASE-
dc.subject.keywordPlusSELECTION-
dc.subject.keywordPlusMOUSE-
dc.subject.keywordAuthorRNA-BINDING PROTEIN-
dc.subject.keywordAuthorCLEAVAGE SITES-
dc.subject.keywordAuthorALPHA-LACTALBUMIN-
dc.subject.keywordAuthorIDENTIFICATION-
dc.subject.keywordAuthorDENATURATION-
dc.subject.keywordAuthorDEGRADOMICS-
dc.subject.keywordAuthorTRANSITION-
dc.subject.keywordAuthorPEPTIDASE-
dc.subject.keywordAuthorSELECTION-
dc.subject.keywordAuthorMOUSE-
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Center for RNA Research(RNA 연구단) > 1. Journal Papers (저널논문)
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