000841860 001__ 841860
000841860 005__ 20220930130138.0
000841860 0247_ $$2doi$$a10.1038/s41598-017-18313-x
000841860 0247_ $$2Handle$$a2128/17205
000841860 0247_ $$2pmid$$apmid:29269939
000841860 0247_ $$2WOS$$aWOS:000418562100010
000841860 037__ $$aFZJ-2018-00157
000841860 041__ $$aEnglish
000841860 082__ $$a000
000841860 1001_ $$0P:(DE-Juel1)131989$$aYang, Ge$$b0
000841860 245__ $$aInfluence of solubilization and AD-mutations on stability and structure of human presenilins
000841860 260__ $$aLondon$$bNature Publishing Group$$c2017
000841860 3367_ $$2DRIVER$$aarticle
000841860 3367_ $$2DataCite$$aOutput Types/Journal article
000841860 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1517993383_8813
000841860 3367_ $$2BibTeX$$aARTICLE
000841860 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000841860 3367_ $$00$$2EndNote$$aJournal Article
000841860 520__ $$aPresenilin (PS1 or PS2) functions as the catalytic subunit of γ-secretase, which produces the toxic amyloid beta peptides in Alzheimer’s disease (AD). The dependence of folding and structural stability of PSs on the lipophilic environment and mutation were investigated by far UV CD spectroscopy. The secondary structure content and stability of PS2 depended on the lipophilic environment. PS2 undergoes a temperature-dependent structural transition from α-helical to β-structure at 331 K. The restructured protein formed structures which tested positive in spectroscopic amyloid fibrils assays. The AD mutant PS1L266F, PS1L424V and PS1ΔE9 displayed reduced stability which supports a proposed ‘loss of function’ mechanism of AD based on protein instability. The exon 9 coded sequence in the inhibitory loop of the zymogen was found to be required for the modulation of the thermal stability of PS1 by the lipophilic environment.
000841860 536__ $$0G:(DE-HGF)POF3-553$$a553 - Physical Basis of Diseases (POF3-553)$$cPOF3-553$$fPOF III$$x0
000841860 588__ $$aDataset connected to CrossRef
000841860 7001_ $$00000-0002-9973-3321$$aYu, Kun$$b1
000841860 7001_ $$0P:(DE-HGF)0$$aKaitatzi, Christina-Symina$$b2
000841860 7001_ $$0P:(DE-Juel1)171201$$aSingh, Abhilasha$$b3$$ufzj
000841860 7001_ $$0P:(DE-Juel1)131973$$aLabahn, Jörg$$b4$$eCorresponding author$$ufzj
000841860 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/s41598-017-18313-x$$gVol. 7, no. 1, p. 17970$$n1$$p17970$$tScientific reports$$v7$$x2045-2322$$y2017
000841860 8564_ $$uhttps://juser.fz-juelich.de/record/841860/files/s41598-017-18313-x.pdf$$yOpenAccess
000841860 8564_ $$uhttps://juser.fz-juelich.de/record/841860/files/s41598-017-18313-x.gif?subformat=icon$$xicon$$yOpenAccess
000841860 8564_ $$uhttps://juser.fz-juelich.de/record/841860/files/s41598-017-18313-x.jpg?subformat=icon-1440$$xicon-1440$$yOpenAccess
000841860 8564_ $$uhttps://juser.fz-juelich.de/record/841860/files/s41598-017-18313-x.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000841860 8564_ $$uhttps://juser.fz-juelich.de/record/841860/files/s41598-017-18313-x.jpg?subformat=icon-640$$xicon-640$$yOpenAccess
000841860 8564_ $$uhttps://juser.fz-juelich.de/record/841860/files/s41598-017-18313-x.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000841860 8767_ $$82676089124$$92017-12-12$$d2017-12-15$$eAPC$$jZahlung erfolgt$$pSREP-17-31433B
000841860 909CO $$ooai:juser.fz-juelich.de:841860$$popenCost$$pVDB$$pdriver$$pOpenAPC$$popen_access$$popenaire$$pdnbdelivery
000841860 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131989$$aForschungszentrum Jülich$$b0$$kFZJ
000841860 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)171201$$aForschungszentrum Jülich$$b3$$kFZJ
000841860 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131973$$aForschungszentrum Jülich$$b4$$kFZJ
000841860 9131_ $$0G:(DE-HGF)POF3-553$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vPhysical Basis of Diseases$$x0
000841860 9141_ $$y2017
000841860 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000841860 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000841860 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000841860 915__ $$0StatID:(DE-HGF)1040$$2StatID$$aDBCoverage$$bZoological Record
000841860 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bSCI REP-UK : 2015
000841860 915__ $$0StatID:(DE-HGF)9905$$2StatID$$aIF >= 5$$bSCI REP-UK : 2015
000841860 915__ $$0StatID:(DE-HGF)0501$$2StatID$$aDBCoverage$$bDOAJ Seal
000841860 915__ $$0StatID:(DE-HGF)0500$$2StatID$$aDBCoverage$$bDOAJ
000841860 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000841860 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000841860 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000841860 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000841860 915__ $$0StatID:(DE-HGF)1150$$2StatID$$aDBCoverage$$bCurrent Contents - Physical, Chemical and Earth Sciences
000841860 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000841860 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000841860 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000841860 920__ $$lyes
000841860 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000841860 9801_ $$aAPC
000841860 9801_ $$aFullTexts
000841860 980__ $$ajournal
000841860 980__ $$aVDB
000841860 980__ $$aUNRESTRICTED
000841860 980__ $$aI:(DE-Juel1)ICS-6-20110106
000841860 980__ $$aAPC
000841860 981__ $$aI:(DE-Juel1)IBI-7-20200312