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| 001 | 139178 | ||
| 005 | 20240321220553.0 | ||
| 024 | 7 | _ | |a 10.1038/nsmb.3380 |2 doi |
| 024 | 7 | _ | |a pmid:28218749 |2 pmid |
| 024 | 7 | _ | |a 1072-8368 |2 ISSN |
| 024 | 7 | _ | |a 1545-9985 |2 ISSN |
| 024 | 7 | _ | |a 1545-9993 |2 ISSN |
| 024 | 7 | _ | |a 2331-365X |2 ISSN |
| 024 | 7 | _ | |a altmetric:16561063 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-05500 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Oroz, Javier |0 P:(DE-2719)2810826 |b 0 |e First author |u dzne |
| 245 | _ | _ | |a Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90. |
| 260 | _ | _ | |a London [u.a.] |c 2017 |b Nature Publishing Group |
| 264 | _ | 1 | |3 online |2 Crossref |b Springer Science and Business Media LLC |c 2017-02-20 |
| 264 | _ | 1 | |3 print |2 Crossref |b Springer Science and Business Media LLC |c 2017-04-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1685113171_10310 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The critical toxic species in over 40 human diseases are misfolded proteins. Their interaction with molecular chaperones such as Hsp90, which preferentially interacts with metastable proteins, is essential for the blocking of disease progression. Here we used nuclear magnetic resonance (NMR) spectroscopy to determine the three-dimensional structure of the misfolded cytotoxic monomer of the amyloidogenic human protein transthyretin, which is characterized by the release of the C-terminal β-strand and perturbations of the A-B loop. The misfolded transthyretin monomer, but not the wild-type protein, binds to human Hsp90. In the bound state, the Hsp90 dimer predominantly populates an open conformation, and transthyretin retains its globular structure. The interaction surface for the transthyretin monomer comprises the N-terminal and middle domains of Hsp90 and overlaps with that of the Alzheimer's-disease-related protein tau. Taken together, the data suggest that Hsp90 uses a mechanism for the recognition of aggregation-prone proteins that is largely distinct from those of other Hsp90 clients. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 542 | _ | _ | |i 2017-02-20 |2 Crossref |u http://www.springer.com/tdm |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a HSP90 Heat-Shock Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Intrinsically Disordered Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Molecular Chaperones |2 NLM Chemicals |
| 650 | _ | 7 | |a Prealbumin |2 NLM Chemicals |
| 650 | _ | 7 | |a tau Proteins |2 NLM Chemicals |
| 650 | _ | 2 | |a HSP90 Heat-Shock Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a HSP90 Heat-Shock Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Imaging, Three-Dimensional |2 MeSH |
| 650 | _ | 2 | |a Intrinsically Disordered Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a Intrinsically Disordered Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Magnetic Resonance Spectroscopy |2 MeSH |
| 650 | _ | 2 | |a Models, Biological |2 MeSH |
| 650 | _ | 2 | |a Models, Molecular |2 MeSH |
| 650 | _ | 2 | |a Molecular Chaperones: chemistry |2 MeSH |
| 650 | _ | 2 | |a Molecular Chaperones: metabolism |2 MeSH |
| 650 | _ | 2 | |a Prealbumin: chemistry |2 MeSH |
| 650 | _ | 2 | |a Prealbumin: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Binding |2 MeSH |
| 650 | _ | 2 | |a Protein Conformation |2 MeSH |
| 650 | _ | 2 | |a Protein Folding |2 MeSH |
| 650 | _ | 2 | |a Protein Multimerization |2 MeSH |
| 650 | _ | 2 | |a tau Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a tau Proteins: metabolism |2 MeSH |
| 700 | 1 | _ | |a Kim, Jin Hae |0 P:(DE-2719)9000457 |b 1 |u dzne |
| 700 | 1 | _ | |a Chang, Bliss J |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Zweckstetter, Markus |0 P:(DE-2719)2810591 |b 3 |e Last author |u dzne |
| 773 | 1 | 8 | |a 10.1038/nsmb.3380 |b : Springer Science and Business Media LLC, 2017-02-20 |n 4 |p 407-413 |3 journal-article |2 Crossref |t Nature Structural & Molecular Biology |v 24 |y 2017 |x 1545-9993 |
| 773 | _ | _ | |a 10.1038/nsmb.3380 |g Vol. 24, no. 4, p. 407 - 413 |0 PERI:(DE-600)2131437-8 |n 4 |q 24:4<407 - 413 |p 407-413 |t Nature structural & molecular biology |v 24 |y 2017 |x 1545-9993 |
| 856 | 4 | _ | |u https://www.nature.com/articles/nsmb.3380 |
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| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 0 |6 P:(DE-2719)2810826 |
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| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 3 |6 P:(DE-2719)2810591 |
| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-342 |3 G:(DE-HGF)POF3 |2 G:(DE-HGF)POF3-300 |4 G:(DE-HGF)POF |v Disease Mechanisms and Model Systems |x 0 |
| 914 | 1 | _ | |y 2017 |
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