Volume and energy folding landscape of prion protein revealed by pressure

Detalhes bibliográficos
Autor(a) principal: Cordeiro,Y.
Data de Publicação: 2005
Outros Autores: Kraineva,J., Winter,R., Silva,J.L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Medical and Biological Research
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006
Resumo: The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion.
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spelling Volume and energy folding landscape of prion protein revealed by pressurePrionHigh pressureStructural conversionAggregationThe main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion.Associação Brasileira de Divulgação Científica2005-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006Brazilian Journal of Medical and Biological Research v.38 n.8 2005reponame:Brazilian Journal of Medical and Biological Researchinstname:Associação Brasileira de Divulgação Científica (ABDC)instacron:ABDC10.1590/S0100-879X2005000800006info:eu-repo/semantics/openAccessCordeiro,Y.Kraineva,J.Winter,R.Silva,J.L.eng2005-07-30T00:00:00Zoai:scielo:S0100-879X2005000800006Revistahttps://www.bjournal.org/https://old.scielo.br/oai/scielo-oai.phpbjournal@terra.com.br||bjournal@terra.com.br1414-431X0100-879Xopendoar:2005-07-30T00:00Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)false
dc.title.none.fl_str_mv Volume and energy folding landscape of prion protein revealed by pressure
title Volume and energy folding landscape of prion protein revealed by pressure
spellingShingle Volume and energy folding landscape of prion protein revealed by pressure
Cordeiro,Y.
Prion
High pressure
Structural conversion
Aggregation
title_short Volume and energy folding landscape of prion protein revealed by pressure
title_full Volume and energy folding landscape of prion protein revealed by pressure
title_fullStr Volume and energy folding landscape of prion protein revealed by pressure
title_full_unstemmed Volume and energy folding landscape of prion protein revealed by pressure
title_sort Volume and energy folding landscape of prion protein revealed by pressure
author Cordeiro,Y.
author_facet Cordeiro,Y.
Kraineva,J.
Winter,R.
Silva,J.L.
author_role author
author2 Kraineva,J.
Winter,R.
Silva,J.L.
author2_role author
author
author
dc.contributor.author.fl_str_mv Cordeiro,Y.
Kraineva,J.
Winter,R.
Silva,J.L.
dc.subject.por.fl_str_mv Prion
High pressure
Structural conversion
Aggregation
topic Prion
High pressure
Structural conversion
Aggregation
description The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion.
publishDate 2005
dc.date.none.fl_str_mv 2005-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0100-879X2005000800006
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Associação Brasileira de Divulgação Científica
publisher.none.fl_str_mv Associação Brasileira de Divulgação Científica
dc.source.none.fl_str_mv Brazilian Journal of Medical and Biological Research v.38 n.8 2005
reponame:Brazilian Journal of Medical and Biological Research
instname:Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
instname_str Associação Brasileira de Divulgação Científica (ABDC)
instacron_str ABDC
institution ABDC
reponame_str Brazilian Journal of Medical and Biological Research
collection Brazilian Journal of Medical and Biological Research
repository.name.fl_str_mv Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)
repository.mail.fl_str_mv bjournal@terra.com.br||bjournal@terra.com.br
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