Structures of the Wild-Type and S59L Mutant CHCHD10 ProteinsImportant in Amyotrophic Lateral Sclerosis-FrontotemporalDementia

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dc.authorid0000-0002-0772-9350
dc.contributor.authorAlıcı, Hakan
dc.contributor.authorUversky, Vladimir N.
dc.contributor.authorKang, David E.
dc.contributor.authorWoo, Junga Alexa
dc.contributor.authorWeber, Orkide Coşkuner
dc.date.accessioned2022-11-04T08:54:33Z
dc.date.available2022-11-04T08:54:33Z
dc.date.issued2022
dc.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.description.abstractThe S59L genetic mutation of the mitochondrial coiled-coil-helix-coiled-coil-helixdomain-containing protein 10 (CHCHD10) is involved in the pathogenesis of amyotrophic lateralsclerosis (ALS) and frontotemporal dementia (FTD). The wild-type and mutant forms of this proteincontain intrinsically disordered regions, and their structural characterization has been facing challenges.Here, for thefirst time in the literature, we present the structural ensemble properties of the wild-type andS59L mutant form of CHCHD10 in an aqueous solution environment at the atomic level with dynamics.Even though available experiments suggested that the S59L mutation may not change the structure of theCHCHD10 protein, our structural analysis clearly shows that the structure of this protein is significantlyaffected by the S59L mutation. We present here the secondary structure components with theirabundances per residue, the tertiary structure properties, the free energy surfaces based on the radius ofgyration and end-to-end distance values, the Ramachandran plots, the quantity of intramolecularhydrogen bonds, and the principal component analysis results. These results may be crucial in designingmore efficient treatment for ALS and FTD diseases.
dc.identifier.citationAlici, H., Uversky, V. N., Kang, D. E., Woo, J. A., & Coskuner-Weber, O. (2022). Structures of the Wild-Type and S59L Mutant CHCHD10 Proteins Important in Amyotrophic Lateral Sclerosis–Frontotemporal Dementia. ACS Chemical Neuroscience, 13(8), 1273-1280.
dc.identifier.doi10.1021/acschemneuro.2c00011
dc.identifier.endpage1280en_US
dc.identifier.issue8en_US
dc.identifier.scopus2-s2.0-85127872284
dc.identifier.scopusqualityN/A
dc.identifier.startpage1273en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12846/669
dc.identifier.volume13en_US
dc.identifier.wosWOS:000794206200015
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorWeber, Orkide Coşkuner
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.relation.ispartofACS Chemical Neuroscience
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectGenetic Mutationen_US
dc.subjectGenetik Mutasyonen_US
dc.subjectGenetische Mutationen_US
dc.titleStructures of the Wild-Type and S59L Mutant CHCHD10 ProteinsImportant in Amyotrophic Lateral Sclerosis-FrontotemporalDementia
dc.typeArticle

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