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복잡계자기조립연구단
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A Combination of Bio-Orthogonal Supramolecular Clicking and Proximity Chemical Tagging as a Supramolecular Tool for Discovery of Putative Proteins Associated with Laminopathic Disease

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dc.contributor.authorJaehwan Sim-
dc.contributor.authorAra Lee-
dc.contributor.authorKim, Dasom-
dc.contributor.authorKyung Lock Kim-
dc.contributor.authorPark, Bum-Joon-
dc.contributor.authorPark, Kyeng Min-
dc.contributor.authorKimoon Kim-
dc.date.accessioned2023-06-15T22:00:42Z-
dc.date.available2023-06-15T22:00:42Z-
dc.date.created2023-03-28-
dc.date.issued2023-05-
dc.identifier.issn1613-6810-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/13459-
dc.description.abstractProtein mutations alter protein-protein interactions that can lead to a number of illnesses. Mutations in lamin A (LMNA) have been reported to cause laminopathies. However, the proteins associated with the LMNA mutation have mostly remained unexplored. Herein, a new chemical tool for proximal proteomics is reported, developed by a combination of proximity chemical tagging and a bio-orthogonal supramolecular latching based on cucurbit[7]uril (CB[7])-based host-guest interactions. As this host-guest interaction acts as a noncovalent clickable motif that can be unclicked on-demand, this new chemical tool is exploited for reliable detection of the proximal proteins of LMNA and its mutant that causes laminopathic dilated cardiomyopathy (DCM). Most importantly, a comparison study reveals, for the first time, mutant-dependent alteration in LMNA proteomic environments, which allows to identify putative laminopathic DCM-linked proteins including FOXJ3 and CELF2. This study demonstrates the feasibility of this chemical tool for reliable proximal proteomics, and its immense potential as a new research platform for discovering biomarkers associated with protein mutation-linked diseases.-
dc.language영어-
dc.publisherWILEY-V C H VERLAG GMBH-
dc.titleA Combination of Bio-Orthogonal Supramolecular Clicking and Proximity Chemical Tagging as a Supramolecular Tool for Discovery of Putative Proteins Associated with Laminopathic Disease-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000939674200001-
dc.identifier.scopusid2-s2.0-85148863600-
dc.identifier.rimsid80309-
dc.contributor.affiliatedAuthorJaehwan Sim-
dc.contributor.affiliatedAuthorAra Lee-
dc.contributor.affiliatedAuthorKyung Lock Kim-
dc.contributor.affiliatedAuthorKimoon Kim-
dc.identifier.doi10.1002/smll.202208088-
dc.identifier.bibliographicCitationSMALL, v.19, no.21-
dc.relation.isPartOfSMALL-
dc.citation.titleSMALL-
dc.citation.volume19-
dc.citation.number21-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalResearchAreaScience & Technology - Other Topics-
dc.relation.journalResearchAreaMaterials Science-
dc.relation.journalResearchAreaPhysics-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.relation.journalWebOfScienceCategoryChemistry, Physical-
dc.relation.journalWebOfScienceCategoryNanoscience & Nanotechnology-
dc.relation.journalWebOfScienceCategoryMaterials Science, Multidisciplinary-
dc.relation.journalWebOfScienceCategoryPhysics, Applied-
dc.relation.journalWebOfScienceCategoryPhysics, Condensed Matter-
dc.subject.keywordPlusMASS-SPECTROMETRY-
dc.subject.keywordPlusLATCHING SYSTEM-
dc.subject.keywordPlusBINDING PAIRS-
dc.subject.keywordPlusLIVING CELLS-
dc.subject.keywordPlusLAMIN-C-
dc.subject.keywordPlusMUTATIONS-
dc.subject.keywordPlusCARDIOMYOPATHY-
dc.subject.keywordPlusCOMPLEXES-
dc.subject.keywordPlusNETWORKS-
dc.subject.keywordAuthorcucurbit[7]uril-
dc.subject.keywordAuthordilated cardiomyopathy-
dc.subject.keywordAuthorhost-guest chemistry-
dc.subject.keywordAuthorlamin A-
dc.subject.keywordAuthorlaminopathies-
dc.subject.keywordAuthorproteomics-
Appears in Collections:
Center for Self-assembly and Complexity(복잡계 자기조립 연구단) > 1. Journal Papers (저널논문)
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