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유전체항상성연구단
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Simple Method to Characterize the Ciliary Proteome of Multiciliated Cells

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dc.contributor.authorSim H.J.-
dc.contributor.authorYun S.-
dc.contributor.authorKim H.E.-
dc.contributor.authorKwon K.Y.-
dc.contributor.authorKim G.-H.-
dc.contributor.authorYun S.-
dc.contributor.authorByung Gyu, Kim-
dc.contributor.authorKyungjae Myung-
dc.contributor.authorTae Joo Park-
dc.contributor.authorTaejoon Kwon-
dc.date.available2020-03-18T08:18:21Z-
dc.date.created2019-12-16-
dc.date.issued2020-01-
dc.identifier.issn1535-3893-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/7043-
dc.description.abstractCopyright © 2019 American Chemical Society.Motile cilia of multiciliated epithelial cells have important roles in animal development and cell homeostasis. Although several studies have identified and reported proteins localized in this complex organelle and the related immotile primary cilia from various cell types, it is still challenging to isolate high quantities of ciliary proteins for proteomic analysis. In this study, African clawed frog (Xenopus laevis) embryos, which have many multiciliated cells in the epidermis, were treated with a simple ionic buffer to identify 1009 proteins conserved across vertebrates; these proteins were putatively localized in motile cilia. Using two ciliary proteome databases, we confirmed that previously validated cilia-associated proteins are highly enriched in our ciliary proteome. Proteins localized at the transition zone and Ellis-van Creveld zone, which are distinct regions at the base of cilia, near the junction with the apical cell surface, were isolated using our method. Among the newly identified ciliary proteins, we report that KRT17 may have an unrecognized function in motile cilia. Hence, the method developed in this study would be useful for understanding the ciliary proteome-
dc.description.uri1-
dc.language영어-
dc.publisherAMER CHEMICAL SOC-
dc.titleSimple Method to Characterize the Ciliary Proteome of Multiciliated Cells-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000506722100036-
dc.identifier.scopusid2-s2.0-85075546992-
dc.identifier.rimsid70694-
dc.contributor.affiliatedAuthorByung Gyu, Kim-
dc.contributor.affiliatedAuthorKyungjae Myung-
dc.contributor.affiliatedAuthorTae Joo Park-
dc.contributor.affiliatedAuthorTaejoon Kwon-
dc.identifier.doi10.1021/acs.jproteome.9b00589-
dc.identifier.bibliographicCitationJOURNAL OF PROTEOME RESEARCH, v.19, no.1, pp.391 - 400-
dc.citation.titleJOURNAL OF PROTEOME RESEARCH-
dc.citation.volume19-
dc.citation.number1-
dc.citation.startPage391-
dc.citation.endPage400-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordAuthorcilia-
dc.subject.keywordAuthorDTBP-
dc.subject.keywordAuthormulticiliated cells-
dc.subject.keywordAuthorXenopus laevis-
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > 1. Journal Papers (저널논문)
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