000279306 001__ 279306
000279306 005__ 20210129221032.0
000279306 0247_ $$2doi$$a10.1021/acs.jpcb.5b04822
000279306 0247_ $$2ISSN$$a1089-5647
000279306 0247_ $$2ISSN$$a1520-5207
000279306 0247_ $$2ISSN$$a1520-6106
000279306 0247_ $$2WOS$$aWOS:000359031400022
000279306 0247_ $$2altmetric$$aaltmetric:4240936
000279306 0247_ $$2pmid$$apmid:26130191
000279306 037__ $$aFZJ-2015-07321
000279306 082__ $$a530
000279306 1001_ $$0P:(DE-HGF)0$$aCarballo-Pacheco, Martín$$b0
000279306 245__ $$aOligomer Formation of Toxic and Functional Amyloid Peptides Studied with Atomistic Simulations
000279306 260__ $$aWashington, DC$$bSoc.$$c2015
000279306 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1449731619_5827
000279306 3367_ $$2DataCite$$aOutput Types/Journal article
000279306 3367_ $$00$$2EndNote$$aJournal Article
000279306 3367_ $$2BibTeX$$aARTICLE
000279306 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000279306 3367_ $$2DRIVER$$aarticle
000279306 520__ $$aAmyloids are associated with diseases, including Alzheimer’s, as well as functional roles such as storage of peptide hormones. It is still unclear what differences exist between aberrant and functional amyloids. However, it is known that soluble oligomers formed during amyloid aggregation are more toxic than the final fibrils. Here, we perform molecular dynamics simulations to study the aggregation of the amyloid-β peptide Aβ25–35, associated with Alzheimer’s disease, and two functional amyloid-forming tachykinin peptides: kassinin and neuromedin K. Although the three peptides have similar primary sequences, tachykinin peptides, in contrast to Aβ25–35, form nontoxic amyloids. Our simulations reveal that the charge of the C-terminus is essential to controlling the aggregation process. In particular, when the kassinin C-terminus is not amidated, the aggregation kinetics decreases considerably. In addition, we observe that the monomeric peptides in extended conformations aggregate faster than those in collapsed hairpin-like conformations.
000279306 536__ $$0G:(DE-HGF)POF3-553$$a553 - Physical Basis of Diseases (POF3-553)$$cPOF3-553$$fPOF III$$x0
000279306 588__ $$aDataset connected to CrossRef
000279306 7001_ $$0P:(DE-HGF)0$$aIsmail, Ahmed E.$$b1
000279306 7001_ $$0P:(DE-Juel1)132024$$aStrodel, Birgit$$b2$$eCorresponding author$$ufzj
000279306 773__ $$0PERI:(DE-600)2006039-7$$a10.1021/acs.jpcb.5b04822$$gVol. 119, no. 30, p. 9696 - 9705$$n30$$p9696 - 9705$$tThe @journal of physical chemistry <Washington, DC> / B$$v119$$x1520-5207$$y2015
000279306 8564_ $$uhttp://pubs.acs.org/doi/abs/10.1021/acs.jpcb.5b04822
000279306 8564_ $$uhttps://juser.fz-juelich.de/record/279306/files/Oligomer%20Formation%20of%20Toxic%20and%20Functional%20Amyloid%20Peptides%20Studied%20with%20Atomistic%20Simulations.pdf$$yRestricted
000279306 8564_ $$uhttps://juser.fz-juelich.de/record/279306/files/Oligomer%20Formation%20of%20Toxic%20and%20Functional%20Amyloid%20Peptides%20Studied%20with%20Atomistic%20Simulations.gif?subformat=icon$$xicon$$yRestricted
000279306 8564_ $$uhttps://juser.fz-juelich.de/record/279306/files/Oligomer%20Formation%20of%20Toxic%20and%20Functional%20Amyloid%20Peptides%20Studied%20with%20Atomistic%20Simulations.jpg?subformat=icon-1440$$xicon-1440$$yRestricted
000279306 8564_ $$uhttps://juser.fz-juelich.de/record/279306/files/Oligomer%20Formation%20of%20Toxic%20and%20Functional%20Amyloid%20Peptides%20Studied%20with%20Atomistic%20Simulations.jpg?subformat=icon-180$$xicon-180$$yRestricted
000279306 8564_ $$uhttps://juser.fz-juelich.de/record/279306/files/Oligomer%20Formation%20of%20Toxic%20and%20Functional%20Amyloid%20Peptides%20Studied%20with%20Atomistic%20Simulations.jpg?subformat=icon-640$$xicon-640$$yRestricted
000279306 8564_ $$uhttps://juser.fz-juelich.de/record/279306/files/Oligomer%20Formation%20of%20Toxic%20and%20Functional%20Amyloid%20Peptides%20Studied%20with%20Atomistic%20Simulations.pdf?subformat=pdfa$$xpdfa$$yRestricted
000279306 909CO $$ooai:juser.fz-juelich.de:279306$$pVDB
000279306 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132024$$aForschungszentrum Jülich GmbH$$b2$$kFZJ
000279306 9131_ $$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$$x0
000279306 9141_ $$y2015
000279306 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000279306 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000279306 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000279306 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000279306 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000279306 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000279306 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000279306 915__ $$0StatID:(DE-HGF)1150$$2StatID$$aDBCoverage$$bCurrent Contents - Physical, Chemical and Earth Sciences
000279306 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ PHYS CHEM B : 2014
000279306 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000279306 920__ $$lyes
000279306 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000279306 980__ $$ajournal
000279306 980__ $$aVDB
000279306 980__ $$aI:(DE-Juel1)ICS-6-20110106
000279306 980__ $$aUNRESTRICTED
000279306 981__ $$aI:(DE-Juel1)IBI-7-20200312