Effects of the Amyotrophic Lateral Sclerosis-related Q108P Mutation on the Structural Ensemble Characteristics of CHCHD10.

Hakan Alici, Vladimir N Uversky, David E Kang, Junga Alexa Woo, Orkid Coskuner-Weber

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Article in Current protein & peptide science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

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5 authors.

Hakan AliciDepartment of Physics, Faculty of Science, Zonguldak Bulent Ecevit University, Zonguldak, 67100, Turkey.

Vladimir N UverskyDepartment of Molecular Medicine and USF Health Byrd Alzheimer`s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, 33612, USA.

David E KangDepartment of Pathology, School of Medicine, Case Western Reserve University, 2103 Cornell Road, 5129 WRB, Cleveland, OH, 44106, USA.

Junga Alexa WooDepartment of Pathology, School of Medicine, Case Western Reserve University, 2103 Cornell Road, 5129 WRB, Cleveland, OH, 44106, USA.

Orkid Coskuner-WeberDepartment of Molecular Biotechnology, Turkish-German University, Sahinkaya Caddesi, No. 106, Beykoz, Istanbul, 34820, Turkey.ORCID 0000-0002-0772-9350

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionThe Q108P pathological variant of the mitochondrial Coiled-Coil-Helix-- Coiled-Coil-Helix Domain-Containing Protein 10 (CHCHD10) has been implicated in amyotrophic lateral sclerosis (ALS). Both the wild-type and CHCHD10

methodsThis study presents the foundational characterization of the structural features of CHCHD10

resultsOur findings reveal distinct differences in structural properties, free energy surfaces, and the outputs of principal component analysis between these two proteins. These results contribute significantly to the comprehension of CHCHD10 and its Q108P variant in terms of pathology, biochemistry, and structural biology.

conclusionThe reported structural properties hold promise for informing the development of more effective treatments for ALS.

Indexed as

Amyotrophic Lateral SclerosisMitochondrial ProteinsMutationHumansMolecular Dynamics SimulationPrincipal Component AnalysisProtein ConformationThermodynamicsCHCHD10 protein, humanMitochondrial Proteinsamyotrophic lateral sclerosisbioinformatics.CHCHD10geneticsmultiple run molecular dynamics simulationsQ108Pstructural properties

Identifiers

PMID39444183

DOI10.1016/j.bbapap.2010.01.011

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