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dc.contributor.author Kim, Bokyung -
dc.contributor.author Kim, Jin Hae -
dc.date.accessioned 2021-01-22T07:16:35Z -
dc.date.available 2021-01-22T07:16:35Z -
dc.date.created 2020-09-24 -
dc.date.created 2020-09-24 -
dc.date.created 2020-09-24 -
dc.date.issued 2020-09 -
dc.identifier.citation Journal of the Korean Magnetic Resonance Society, v.24, no.3, pp.91 - 95 -
dc.identifier.issn 1226-6531 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/12714 -
dc.description.abstract Transthyretin (TTR) is an abundant protein in blood plasma and cerebrospinal fluid (CSF), working as a homo-tetrameric complex to transport thyroxine (T4) and a holo-retinol binding protein. TTR is well-known for its amyloidogenic property; several types of systemic amyloidosis diseases are caused by aggregation of either wild-type TTR or its variants, for which more than 100 mutations were reported to increase the amyloidogenicity of TTR. The rate-limiting step of TTR aggregation is the dissociation of a monomeric subunit from a tetrameric complex. A wide range of biochemical and biophysical techniques have been employed to elucidate the TTR aggregation processes, among which nuclear magnetic resonance (NMR) spectroscopy contributed much to characterize the structural and functional features of TTR during its aggregation processes. The present review focuses on discussing the recent advances of our understanding to the amyloidosis mechanism of TTR and to the structural features of its monomeric aggregation-prone state in solution. We expect that the present review provides novel insights to appreciate the molecular basis of TTR amyloidosis and to develop novel therapeutic strategies to treat diverse TTR-related diseases. -
dc.language English -
dc.publisher 한국자기공명학회 -
dc.title NMR-based structural characterization of transthyretin in its aggregation-prone state -
dc.type Article -
dc.identifier.doi 10.6564/JKMRS.2020.24.3.091 -
dc.identifier.wosid 000588490200005 -
dc.type.local Article(Domestic) -
dc.type.rims ART -
dc.description.journalClass 2 -
dc.citation.publicationname Journal of the Korean Magnetic Resonance Society -
dc.identifier.kciid ART002625794 -
dc.contributor.localauthor Kim, Bokyung -
dc.contributor.localauthor Kim, Jin Hae -
dc.contributor.nonIdAuthor Kim, Bokyung -
dc.identifier.citationVolume 24 -
dc.identifier.citationNumber 3 -
dc.identifier.citationStartPage 91 -
dc.identifier.citationEndPage 95 -
dc.identifier.citationTitle Journal of the Korean Magnetic Resonance Society -
dc.type.journalArticle Article -
dc.description.isOpenAccess N -
dc.subject.keywordAuthor transthyretin -
dc.subject.keywordAuthor transthyretin amyloidosis -
dc.subject.keywordAuthor amyloid -
dc.subject.keywordAuthor protein aggregation -
dc.subject.keywordAuthor NMR spectroscopy -

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