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| Hauptseite > Publikationsdatenbank > A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins > print |
| Hauptseite > Publikationsdatenbank > A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins > print |
| 001 | 203089 | ||
| 005 | 20210129220301.0 | ||
| 024 | 7 | _ | |a 10.1002/cbic.201402552 |2 doi |
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| 100 | 1 | _ | |a Shaykhalishahi, Hamed |0 P:(DE-Juel1)167315 |b 0 |u fzj |
| 245 | _ | _ | |a A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins |
| 260 | _ | _ | |a Weinheim |c 2015 |b Wiley-VCH |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1438761839_16994 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a Amyloidogenic proteins share a propensity to convert to the b-structure-rich amyloid state that is associated with the progression of several protein-misfolding disorders. Here we show that a single engineered b-hairpin-binding protein, the bwrapin AS10, binds monomers of three different amyloidogenic proteins, that is, amyloid-b peptide, a-synuclein, and islet amyloid polypeptide, with sub-micromolar affinity. AS10 binding inhibits the aggregation and toxicity of all three proteins. The results demonstrate common conformational preferences and related binding sites in a subset of the amyloidogenic proteins. These commonalities enable the generation of multispecific monomer-binding agents. |
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| 700 | 1 | _ | |a Gauhar, Aziz |0 P:(DE-HGF)0 |b 2 |
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| 700 | 1 | _ | |a Hoyer, Wolfgang |0 P:(DE-Juel1)166306 |b 7 |e Corresponding author |u fzj |
| 773 | _ | _ | |a 10.1002/cbic.201402552 |g Vol. 16, no. 3, p. 411 - 414 |0 PERI:(DE-600)2020469-3 |n 3 |p 411 - 414 |t ChemBioChem |v 16 |y 2015 |x 1439-4227 |
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