000023150 001__ 23150
000023150 005__ 20200402210322.0
000023150 0247_ $$2pmid$$apmid:23001756
000023150 0247_ $$2DOI$$a10.1002/psc.2456
000023150 0247_ $$2WOS$$aWOS:000310029900006
000023150 037__ $$aPreJuSER-23150
000023150 041__ $$aeng
000023150 082__ $$a570
000023150 1001_ $$0P:(DE-Juel1)VDB106075$$aSun, N.$$b0$$uFZJ
000023150 245__ $$aStructural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy
000023150 260__ $$aNew York, NY [u.a.]$$bWiley$$c2012
000023150 300__ $$a691 - 695
000023150 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000023150 3367_ $$2DataCite$$aOutput Types/Journal article
000023150 3367_ $$00$$2EndNote$$aJournal Article
000023150 3367_ $$2BibTeX$$aARTICLE
000023150 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000023150 3367_ $$2DRIVER$$aarticle
000023150 440_0 $$018981$$aJournal of Peptide Science$$v18$$x1075-2617$$y11
000023150 500__ $$aRecord converted from VDB: 12.11.2012
000023150 520__ $$aThe aggregation of the Aβ plays a fundamental role in the pathology of AD. Recently, N-terminally modified Aβ species, pE-Aβ, have been described as major constituents of Aβ deposits in the brains of AD patients. pE-Aβ has an increased aggregation propensity and shows increased toxicity compared with Aβ1-40 and Aβ1-42. In the present work, high-resolution NMR spectroscopy was performed to study pE-Aβ3-40 in aqueous TFE-containing solution. Two-dimensional TOCSY and NOESY experiments were performed. On the basis of NOE and chemical shift data, pE-Aβ3-40 was shown to contain two helical regions formed by residues 14-22 and 30-36. This is similar as previously described for Aβ1-40. However, the secondary chemical shift data indicate decreased helical propensity in pE-Aβ3-40 when compared with Aβ1-40 under exactly the same conditions. This is in agreement with the observation that pE-Aβ3-40 shows a drastically increased tendency to form β-sheet-rich structures under more physiologic conditions. Structural studies of pE-Aβ are crucial for better understanding the structural basis of amyloid fibril formation in the brain during development of AD, especially because an increasing number of reports indicate a decisive role of pE-Aβ for the pathogenesis of AD. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.
000023150 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000023150 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000023150 588__ $$aDataset connected to Pubmed
000023150 7001_ $$0P:(DE-Juel1)VDB57647$$aHartmann, R.$$b1$$uFZJ
000023150 7001_ $$0P:(DE-Juel1)VDB94799$$aLecher, J.$$b2$$uFZJ
000023150 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b3$$uFZJ
000023150 7001_ $$0P:(DE-Juel1)VDB101069$$aFunke, S.A.$$b4$$uFZJ
000023150 7001_ $$0P:(DE-Juel1)VDB109415$$aGremer, L.$$b5$$uFZJ
000023150 7001_ $$0P:(DE-HGF)0$$aLudwig, H.-H.$$b6
000023150 7001_ $$0P:(DE-HGF)0$$aDemuth, H.U.$$b7
000023150 7001_ $$0P:(DE-HGF)0$$aKleinschmidt, H.$$b8
000023150 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b9$$uFZJ
000023150 773__ $$0PERI:(DE-600)1491819-5$$a10.1002/psc.2456$$gVol. 18, p. 691 - 695$$p691 - 695$$q18<691 - 695$$tJournal of peptide science$$v18$$x1075-2617$$y2012
000023150 8567_ $$uhttp://dx.doi.org/10.1002/psc.2456
000023150 909CO $$ooai:juser.fz-juelich.de:23150$$pVDB
000023150 9141_ $$y2012
000023150 915__ $$0StatID:(DE-HGF)0010$$2StatID$$aJCR/ISI refereed
000023150 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000023150 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000023150 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000023150 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000023150 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000023150 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000023150 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000023150 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000023150 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000023150 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000023150 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000023150 9131_ $$0G:(DE-Juel1)FUEK409$$1G:(DE-HGF)POF2-330$$2G:(DE-HGF)POF2-300$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000023150 9131_ $$0G:(DE-Juel1)FUEK505$$1G:(DE-HGF)POF2-450$$2G:(DE-HGF)POF2-400$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000023150 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
000023150 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$gICS$$kICS-6$$lStrukturbiochemie$$x0
000023150 970__ $$aVDB:(DE-Juel1)140115
000023150 980__ $$aVDB
000023150 980__ $$aConvertedRecord
000023150 980__ $$ajournal
000023150 980__ $$aI:(DE-Juel1)ICS-6-20110106
000023150 980__ $$aUNRESTRICTED
000023150 981__ $$aI:(DE-Juel1)IBI-7-20200312