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citation_title: Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90
WT.cg_s: Article
access: Yes
keywords: Solution-state NMR, Chaperones
emanating: 134X76X223X157
citation_publisher: Nature Research
citation_journal_title: Nature Structural & Molecular Biology
description: The interaction of Hsp90 with misfolded monomeric transthyretin is characterized via biophysical approaches, and the data indicate that Hsp90 may have a distinct recognition mode for aggregation-prone proteins.
WT.site_id: 18696
citation_date: 
title: Hsp90 uses several binding interfaces to bind M-TTR. : Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90 : Nature Structural & Molecular Biology : Nature Research
DC.title: Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90
DC.date: 2017-02-20
prism.issn: 1545-9993
DC.publisher: Nature Research
citation_online_date: 2017-02-20
WT.cg_n: Nature Structural & Molecular Biology
DC.creator: Javier Oroz
prism.issue: 
DC.identifier: doi:10.1038/nsmb.3380
dc:title: Hsp90 uses several binding interfaces to bind M-TTR. : Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90 : Nature Structural & Molecular Biology : Nature Research
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prism.publicationDate: 2017-02-20
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DC.rights: © 2017 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
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citation_author: Javier Oroz
citation_issue: 
prism.eIssn: 1545-9985
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DC.language: en
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prism.publicationName: Nature Structural & Molecular Biology
citation_doi: doi:10.1038/nsmb.3380
prism.section: Article
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WT.site_id_name: Max Planck Inst for Biophysical Chemistry (Karl Friedrich Bonhoeffer Inst)
Content-Language: en
prism.copyright: © 2017 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.