ArticleBiochemistry2015
Impact of Rett Syndrome Mutations on MeCP2 MBD Stability.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 43 citations in OpenAlex.
- Revealing function-altering MECP2 mutations in individuals with autism spectrum disorder using yeast and Drosophila.Genetics · 2025Article
- Identification of mutations in five Pakistani families with Epilepsy.Neurogenetics · 2025Article
- Epigenetics in rare neurological diseases.Frontiers in cell and developmental biology · 2024Review
- Nuclease-free precise genome editing corrects MECP2 mutations associated with Rett syndrome.Frontiers in genome editing · 2024Article
- A Severity Comparison between Italian and Israeli Rett Syndrome Cohorts.Diagnostics (Basel, Switzerland) · 2023Article
- Electrostatics in Computational Biophysics and Its Implications for Disease Effects.International journal of molecular sciences · 2022Review
- Genetics behind Cerebral Disease with Ocular Comorbidity: Finding Parallels between the Brain and Eye Molecular Pathology.International journal of molecular sciences · 2022Review
- Oncogenic Mutations in the DNA-Binding Domain of FOXO1 that Disrupt Folding: Quantitative Insights from Experiments and Molecular Simulations.Biochemistry · 2022Article
- Evolved DNA Duplex Readers for Strand-Asymmetrically Modified 5-Hydroxymethylcytosine/5-Methylcytosine CpG Dyads.Journal of the American Chemical Society · 2022Article
- MeCP2 heterochromatin organization is modulated by arginine methylation and serine phosphorylation.Frontiers in cell and developmental biology · 2022Article
- MeCP2: The Genetic Driver of Rett Syndrome Epigenetics.Frontiers in genetics · 2021Review
- SAAMBE-3D: Predicting Effect of Mutations on Protein-Protein Interactions.International journal of molecular sciences · 2020Article
- Binding Analysis of Methyl-CpG Binding Domain of MeCP2 and Rett Syndrome Mutations.ACS chemical biology · 2016Article
- SAAFEC: Predicting the Effect of Single Point Mutations on Protein Folding Free Energy Using a Knowledge-Modified MM/PBSA Approach.International journal of molecular sciences · 2016Article
- Mutations in the KDM5C ARID Domain and Their Plausible Association with Syndromic Claes-Jensen-Type Disease.International journal of molecular sciences · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Rett syndrome causing missense mutations in the methyl-CpG-binding domain (MBD) of methyl CpG-binding protein 2 (MeCP2) were investigated both in silico and in vitro to reveal their effect on protein stability. It is demonstrated that the vast majority of frequently occurring mutations in the human population indeed alter the MBD folding free energy by a fraction of a kcal/mol up to more than 1 kcal/mol. While the absolute magnitude of the change of the free energy is small, the effect on the MBD functionality may be substantial since the folding free energy of MBD is about 2 kcal/mol only. Thus, it is emphasized that the effect of mutations on protein integrity should be evaluated with respect to the wild-type folding free energy but not with the absolute value of the folding free energy change. Furthermore, it was observed that the magnitude of the effect is correlated neither with the burial of the mutation sites nor with the basic amino acid physicochemical property change. Mutations that strongly perturb the immediate structural features were found to have little effect on folding free energy, while very conservative mutations resulted in large changes of the MBD stability. This observation was attributed to the protein's ability to structurally relax and reorganize to reduce the effect of mutation. Comparison between in silico and in vitro results indicated that some Web servers perform relatively well, while the free energy perturbation approach frequently overpredicts the magnitude of the free energy change especially when a charged amino acid is involved.
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Registered trials
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