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NMR-based structural characterization of transthyretin in its aggregation-prone state

Title
NMR-based structural characterization of transthyretin in its aggregation-prone state
Authors
Kim, BokyungKim, Jin Hae
DGIST Authors
Kim, Bokyung; Kim, Jin Hae
Issue Date
2020-09
Citation
Journal of the Korean Magnetic Resonance Society, 24(3), 91-95
Type
Article
Article Type
Article
Author Keywords
transthyretintransthyretin amyloidosisamyloidprotein aggregationNMR spectroscopy
ISSN
1226-6531
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.
URI
http://hdl.handle.net/20.500.11750/12714
DOI
10.6564/JKMRS.2020.24.3.091
Publisher
한국자기공명학회
Related Researcher
Files:
There are no files associated with this item.
Collection:
Department of New BiologyProtein Structure Aging Laboratory1. Journal Articles


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