000153349 001__ 153349
000153349 005__ 20210129213727.0
000153349 0247_ $$2doi$$a10.1002/anie.201309001
000153349 0247_ $$2pmid$$apmid:24623599
000153349 0247_ $$2WOS$$aWOS:000338968700022
000153349 0247_ $$2altmetric$$aaltmetric:2179133
000153349 037__ $$aFZJ-2014-02981
000153349 041__ $$aeng
000153349 082__ $$a540
000153349 1001_ $$0P:(DE-HGF)0$$aMirecka, E. A$$b0
000153349 245__ $$aSequestration of a β-Hairpin for Control of α-Synuclein Aggregation
000153349 260__ $$aWeinheim$$bWiley-VCH$$c2014
000153349 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1398856744_20156
000153349 3367_ $$2DataCite$$aOutput Types/Journal article
000153349 3367_ $$00$$2EndNote$$aJournal Article
000153349 3367_ $$2BibTeX$$aARTICLE
000153349 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000153349 3367_ $$2DRIVER$$aarticle
000153349 520__ $$aThe misfolding and aggregation of the protein α-synuclein (α-syn), which results in the formation of amyloid fibrils, is involved in the pathogenesis of Parkinson's disease and other synucleinopathies. The emergence of amyloid toxicity is associated with the formation of partially folded aggregation intermediates. Here, we engineered a class of binding proteins termed β-wrapins (β-wrap proteins) with affinity for α-synuclein (α-syn). The NMR structure of an α-syn:β-wrapin complex reveals a β-hairpin of α-syn comprising the sequence region α-syn(37-54). The β-wrapin inhibits α-syn aggregation and toxicity at substoichiometric concentrations, demonstrating that it interferes with the nucleation of aggregation.© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
000153349 536__ $$0G:(DE-HGF)POF2-452$$a452 - Structural Biology (POF2-452)$$cPOF2-452$$fPOF II$$x0
000153349 588__ $$aDataset connected to CrossRef, juser.fz-juelich.de, PubMed,
000153349 7001_ $$0P:(DE-HGF)0$$aShaykhalishahi, H.$$b1
000153349 7001_ $$0P:(DE-HGF)0$$aGauhar, A.$$b2
000153349 7001_ $$0P:(DE-HGF)0$$aAkgül, S.$$b3
000153349 7001_ $$0P:(DE-Juel1)132010$$aLecher, Justin$$b4$$ufzj
000153349 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b5$$ufzj
000153349 7001_ $$0P:(DE-Juel1)132023$$aStoldt, Matthias$$b6$$ufzj
000153349 7001_ $$0P:(DE-HGF)0$$aHoyer, W.$$b7$$eCorresponding Author
000153349 773__ $$0PERI:(DE-600)2011836-3$$a10.1002/anie.201309001$$gVol. 53, no. 16, p. 4227 - 4230$$n16$$p4227-4230$$tAngewandte Chemie / International edition$$v53$$x0570-0833$$y2014
000153349 8564_ $$uhttps://juser.fz-juelich.de/record/153349/files/FZJ-2014-02981.pdf$$yRestricted
000153349 909CO $$ooai:juser.fz-juelich.de:153349$$pVDB
000153349 9141_ $$y2014
000153349 915__ $$0StatID:(DE-HGF)0010$$2StatID$$aJCR/ISI refereed
000153349 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer review
000153349 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000153349 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000153349 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000153349 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000153349 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000153349 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000153349 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000153349 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000153349 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000153349 915__ $$0StatID:(DE-HGF)1020$$2StatID$$aDBCoverage$$bCurrent Contents - Social and Behavioral Sciences
000153349 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000153349 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132010$$aForschungszentrum Jülich GmbH$$b4$$kFZJ
000153349 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132029$$aForschungszentrum Jülich GmbH$$b5$$kFZJ
000153349 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132023$$aForschungszentrum Jülich GmbH$$b6$$kFZJ
000153349 9132_ $$0G:(DE-HGF)POF3-553$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vPhysical Basis of Diseases$$x0
000153349 9131_ $$0G:(DE-HGF)POF2-452$$1G:(DE-HGF)POF2-450$$2G:(DE-HGF)POF2-400$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$aDE-HGF$$bSchlüsseltechnologien$$lBioSoft$$vStructural Biology$$x0
000153349 920__ $$lyes
000153349 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000153349 980__ $$ajournal
000153349 980__ $$aVDB
000153349 980__ $$aI:(DE-Juel1)ICS-6-20110106
000153349 980__ $$aUNRESTRICTED
000153349 981__ $$aI:(DE-Juel1)IBI-7-20200312