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dc.contributor.author Saponaro, Federica -
dc.contributor.author Kim, Jin Hae -
dc.contributor.author Chiellini, Grazia -
dc.date.accessioned 2021-01-22T07:16:22Z -
dc.date.available 2021-01-22T07:16:22Z -
dc.date.created 2020-11-26 -
dc.date.issued 2020-11 -
dc.identifier.issn 1661-6596 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/12709 -
dc.description.abstract Transthyretin (TTR), previously named prealbumin is a plasma protein secreted mainly by the liver and choroid plexus (CP) that is a carrier for thyroid hormones (THs) and retinol (vitamin A). The structure of TTR, with four monomers rich in β-chains in a globular tetrameric protein, accounts for the predisposition of the protein to aggregate in fibrils, leading to a rare and severe disease, namely transthyretin amyloidosis (ATTR). Much effort has been made and still is required to find new therapeutic compounds that can stabilize TTR (“kinetic stabilization”) and prevent the amyloid genetic process. Moreover, TTR is an interesting therapeutic target for neurodegenerative diseases due to its recognized neuroprotective properties in the cognitive impairment context and interestingly in Alzheimer’s disease (AD). Much evidence has been collected regarding the neuroprotective effects in AD, including through in vitro and in vivo studies as well as a wide range of clinical series. Despite this supported hypothesis of neuroprotection for TTR, the mechanisms are still not completely clear. The aim of this review is to highlight the most relevant findings on the neuroprotective role of TTR, and to summarize the recent progress on the development of TTR tetramer stabilizers. © 2020 by the authors. Licensee MDPI, Basel, Switzerland. -
dc.language English -
dc.publisher MDPI AG -
dc.title Transthyretin Stabilization: An Emerging Strategy for the Treatment of Alzheimer’s Disease? -
dc.type Article -
dc.identifier.doi 10.3390/ijms21228672 -
dc.identifier.scopusid 2-s2.0-85096213900 -
dc.identifier.bibliographicCitation International Journal of Molecular Sciences, v.21, no.22, pp.8672 - 13 -
dc.description.isOpenAccess TRUE -
dc.subject.keywordAuthor transthyretin -
dc.subject.keywordAuthor protein misfolding -
dc.subject.keywordAuthor protein aggregation -
dc.subject.keywordAuthor amyloidosis -
dc.subject.keywordAuthor Alzheimer’ -
dc.subject.keywordAuthor s disease -
dc.subject.keywordAuthor TTR stabilizers -
dc.subject.keywordPlus RETINOL-BINDING-PROTEIN -
dc.subject.keywordPlus FAMILIAL AMYLOID POLYNEUROPATHY -
dc.subject.keywordPlus CEREBROSPINAL-FLUID -
dc.subject.keywordPlus BETA PEPTIDE -
dc.subject.keywordPlus THYROXINE-BINDING -
dc.subject.keywordPlus CHOROID-PLEXUS -
dc.subject.keywordPlus NATIVE-STATE -
dc.subject.keywordPlus MOUSE MODEL -
dc.subject.keywordPlus VITAMIN-A -
dc.subject.keywordPlus PREALBUMIN -
dc.citation.endPage 13 -
dc.citation.number 22 -
dc.citation.startPage 8672 -
dc.citation.title International Journal of Molecular Sciences -
dc.citation.volume 21 -
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Department of New Biology Protein Structure Aging Laboratory 1. Journal Articles

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