Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/5234
DC FieldValueLanguage
dc.contributor.authorShnyrov, Valery L.-
dc.contributor.authorVillar, Enrique-
dc.contributor.authorZhadan, Galina G.-
dc.contributor.authorSanchez-Ruiz, Jose M.-
dc.contributor.authorQuintas, Alexandre-
dc.contributor.authorSaraiva, Maria João M.-
dc.contributor.authorBrito, Rui M. M.-
dc.date.accessioned2008-09-01T15:06:15Z-
dc.date.available2008-09-01T15:06:15Z-
dc.date.issued2000en_US
dc.identifier.citationBiophysical Chemistry. 88:1-3 (2000) 61-67en_US
dc.identifier.urihttps://hdl.handle.net/10316/5234-
dc.description.abstractFamilial amyloidotic polyneuropathy (FAP) is an autosomal dominant hereditary type of amyloidosis involving amino acid substitutions in transthyretin (TTR). V30M-TTR is the most frequent variant, and L55P-TTR is the variant associated with the most aggressive form of FAP. The thermal stability of the wild-type, V30M-TTR, L55P-TTR and a non-amyloidogenic variant, T119M-TTR, was studied by high-sensitivity differential scanning calorimetry (DSC). The thermal unfolding of TTR is a spontaneous reversible process involving a highly co-operative transition between folded tetramers and unfolded monomers. All variants of transthyretin are very stable to the thermal unfolding that occurs at very high temperatures, most probably because of their oligomeric structure. The data presented in this work indicated that for the homotetrameric form of the wild-type TTR and its variants, the order of stability is as follows: wild-type TTRT119M-TTR>L55P-TTR>V30M-TTR, which does not correlate with their known amyloidogenic potential.en_US
dc.description.urihttp://www.sciencedirect.com/science/article/B6TFB-41NK91T-5/1/472cf0fa1a8c059202a368bff3786720en_US
dc.format.mimetypeaplication/PDFen
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectTransthyretinen_US
dc.subjectFamilial amyloidotic polyneuropathyen_US
dc.subjectDifferential scanning calorimetryen_US
dc.subjectThermal stabilityen_US
dc.titleComparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretinen_US
dc.typearticleen_US
dc.identifier.doi10.1016/S0301-4622(00)00199-X-
uc.controloAutoridadeSim-
item.languageiso639-1en-
item.openairetypearticle-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextCom Texto completo-
item.cerifentitytypePublications-
crisitem.author.researchunitCQC - Coimbra Chemistry Centre-
crisitem.author.parentresearchunitFaculty of Sciences and Technology-
crisitem.author.orcid0000-0001-9128-2557-
Appears in Collections:FCTUC Química - Artigos em Revistas Internacionais
Files in This Item:
File Description SizeFormat
file4b15859df382481ca650920faecb7d28.pdf175.9 kBAdobe PDFView/Open
Show simple item record

SCOPUSTM   
Citations

54
checked on May 27, 2024

WEB OF SCIENCETM
Citations

47
checked on May 2, 2024

Page view(s) 50

411
checked on May 28, 2024

Download(s)

361
checked on May 28, 2024

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.