ArticleInternational journal of molecular sciences2015
Mutations in the KDM5C ARID Domain and Their Plausible Association with Syndromic Claes-Jensen-Type Disease.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- A KDM5 variant outside the catalytic Jumonji C domain disrupts demethylase activity and alters the proximity interactome.G3 (Bethesda, Md.) · 2026Article
- Emerging role ofFrontiers in molecular neuroscience · 2026Article
- Article
- First reported case of de Novo claes-jensen syndrome (CJS) in Palestine: diagnostic challenges and genetic insights.BMC pediatrics · 2025Article
- Decoding the effects of mutation on protein interactions using machine learning.Biophysics reviews · 2025Review
- Chromatin modifiers in neurodevelopment.Frontiers in molecular neuroscience · 2025Review
- Domain architecture and protein-protein interactions regulate KDM5A recruitment to the chromatin.Epigenetics · 2023Review
- Molecular and cellular events linking variants in the histone demethylase KDM5C to the intellectual disability disorder Claes-Jensen syndrome.The FEBS journal · 2022Review
- Reprogramming of the epigenome in neurodevelopmental disorders.Critical reviews in biochemistry and molecular biology · 2022Review
- Structural Perspective on Revealing and Altering Molecular Functions of Genetic Variants Linked with Diseases.International journal of molecular sciences · 2019Review
- CoevDB: a database of intramolecular coevolution among protein-coding genes of the bony vertebrates.Nucleic acids research · 2019Article
- Sex Chromosome Effects on Male-Female Differences in Mammals.Current biology : CB · 2018Review
- Article
- Predicting protein-DNA binding free energy change upon missense mutations using modified MM/PBSA approach: SAMPDI webserver.Bioinformatics (Oxford, England) · 2018Article
- Computational Investigation of the Missense Mutations in DHCR7 Gene Associated with Smith-Lemli-Opitz Syndrome.International journal of molecular sciences · 2018Article
- Cofactors-loaded quaternary structure of lysine-specific demethylase 5C (KDM5C) protein: Computational model.Proteins · 2016Article
- SAAMBE: Webserver to Predict the Charge of Binding Free Energy Caused by Amino Acids Mutations.International journal of molecular sciences · 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
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in KDM5C gene are linked to X-linked mental retardation, the syndromic Claes-Jensen-type disease. This study focuses on non-synonymous mutations in the KDM5C ARID domain and evaluates the effects of two disease-associated missense mutations (A77T and D87G) and three not-yet-classified missense mutations (R108W, N142S, and R179H). We predict the ARID domain's folding and binding free energy changes due to mutations, and also study the effects of mutations on protein dynamics. Our computational results indicate that A77T and D87G mutants have minimal effect on the KDM5C ARID domain stability and DNA binding. In parallel, the change in the free energy unfolding caused by the mutants A77T and D87G were experimentally measured by urea-induced unfolding experiments and were shown to be similar to the in silico predictions. The evolutionary conservation analysis shows that the disease-associated mutations are located in a highly-conserved part of the ARID structure (N-terminal domain), indicating their importance for the KDM5C function. N-terminal residues' high conservation suggests that either the ARID domain utilizes the N-terminal to interact with other KDM5C domains or the N-terminal is involved in some yet unknown function. The analysis indicates that, among the non-classified mutations, R108W is possibly a disease-associated mutation, while N142S and R179H are probably harmless.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.