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dc.contributor.authorWeber, Orkide Coşkuner
dc.contributor.authorUversky, Vladimir N.
dc.date.accessioned2021-01-08T21:51:24Z
dc.date.available2021-01-08T21:51:24Z
dc.date.issued2018
dc.identifier.issn1422-0067
dc.identifier.urihttp://doi.org/10.3390/ijms19020336
dc.identifier.urihttps://hdl.handle.net/20.500.12846/228
dc.descriptionUversky, Vladimir N./0000-0002-4037-5857; Coskuner, Orkid/0000-0002-0772-9350en_US
dc.descriptionWOS:000427527400020en_US
dc.descriptionPubMed: 29364151en_US
dc.description.abstractAmyloid-beta and alpha-synuclein are intrinsically disordered proteins (IDPs), which are at the center of Alzheimer's and Parkinson's disease pathologies, respectively. These IDPs are extremely flexible and do not adopt stable structures. Furthermore, both amyloid- and -synuclein can form toxic oligomers, amyloid fibrils and other type of aggregates in Alzheimer's and Parkinson's diseases. Experimentalists face challenges in investigating the structures and thermodynamic properties of these IDPs in their monomeric and oligomeric forms due to the rapid conformational changes, fast aggregation processes and strong solvent effects. Classical molecular dynamics simulations complement experiments and provide structural information at the atomic level with dynamics without facing the same experimental limitations. Artificial missense mutations are employed experimentally and computationally for providing insights into the structure-function relationships of amyloid- and -synuclein in relation to the pathologies of Alzheimer's and Parkinson's diseases. Furthermore, there are several natural genetic variations that play a role in the pathogenesis of familial cases of Alzheimer's and Parkinson's diseases, which are related to specific genetic defects inherited in dominant or recessive patterns. The present review summarizes the current understanding of monomeric and oligomeric forms of amyloid- and -synuclein, as well as the impacts of artificial and pathological missense mutations on the structural ensembles of these IDPs using molecular dynamics simulations. We also emphasize the recent investigations on residual secondary structure formation in dynamic conformational ensembles of amyloid- and -synuclein, such as -structure linked to the oligomerization and fibrillation mechanisms related to the pathologies of Alzheimer's and Parkinson's diseases. This information represents an important foundation for the successful and efficient drug design studies.en_US
dc.language.isoengen_US
dc.publisherMdpien_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectGeneticsen_US
dc.subjectArtificial Mutationen_US
dc.subjectIntrinsically Disordered Proteinen_US
dc.subjectAlzheimer's Diseaseen_US
dc.subjectParkinson's Diseaseen_US
dc.subjectMolecular Dynamics Simulationsen_US
dc.titleInsights into the molecular mechanisms of Alzheimer's and Parkinson's diseases with molecular simulations: understanding the roles of artificial and pathological missense mutations in intrinsically disordered proteins related to pathologyen_US
dc.typeReviewen_US
dc.relation.journalInternational Journal Of Molecular Sciencesen_US
dc.identifier.volume19en_US
dc.identifier.issue2en_US
dc.relation.publicationcategoryotheren_US
dc.contributor.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.contributor.institutionauthorWeber, Orkide Coşkuner
dc.identifier.doi10.3390/ijms19020336
dc.identifier.wosqualityQ2en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.wosWOS:000427527400020en_US


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