ArticleInternational journal of molecular sciences2016
Revealing the Effects of Missense Mutations Causing Snyder-Robinson Syndrome on the Stability and Dimerization of Spermine Synthase.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- Metabolic alterations in Snyder-Robinson syndrome lymphoblasts are ameliorated by phenylbutyrate treatment.Molecular genetics and metabolism · 2026Article
- Genetic and Phenotypic Features of the Five Known Polyaminopathies: A Critical Narrative Review.American journal of medical genetics. Part A · 2026Review
- Decoding the effects of mutation on protein interactions using machine learning.Biophysics reviews · 2025Review
- Identification of a Rare Branch Point Variant in the SMS Gene in a Large Family With a Severe Form of Snyder-Robinson Syndrome.Clinical genetics · 2025Article
- Development and characterization of a Drosophila model of Snyder-Robinson syndrome.Methods in enzymology · 2025Article
- Article
- Structural Insights into the Mechanisms Underlying Polyaminopathies.International journal of molecular sciences · 2024Review
- Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder-Robinson syndrome.EMBO molecular medicine · 2023Article
- Electrostatics in Computational Biophysics and Its Implications for Disease Effects.International journal of molecular sciences · 2022Review
- Snyder-Robinson syndrome: differential diagnosis of osteogenesis imperfecta.Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA · 2022Article
- Novel Hemizygous Missense Variant of Spermine Synthase (Molecular syndromology · 2021Article
- PremPS: Predicting the impact of missense mutations on protein stability.PLoS computational biology · 2020Article
- Structural Perspective on Revealing and Altering Molecular Functions of Genetic Variants Linked with Diseases.International journal of molecular sciences · 2019Review
- DFMD: Fast and Effective DelPhiForce Steered Molecular Dynamics Approach to Model Ligand Approach Toward a Receptor: Application to Spermine Synthase Enzyme.Frontiers in molecular biosciences · 2019Article
- Computational Approaches to Prioritize Cancer Driver Missense Mutations.International journal of molecular sciences · 2018Review
- Computational Investigation of the Missense Mutations in DHCR7 Gene Associated with Smith-Lemli-Opitz Syndrome.International journal of molecular sciences · 2018Article
- Comparative computational assessment of the pathogenicity of mutations in the Aspartoacylase enzyme.Metabolic brain disease · 2017Article
- Functions of Polyamines in Mammals.The Journal of biological chemistry · 2016Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Missense mutations in spermine synthase (SpmSyn) protein have been shown to cause the Snyder-Robinson syndrome (SRS). Depending on the location within the structure of SpmSyn and type of amino acid substitution, different mechanisms resulting in SRS were proposed. Here we focus on naturally occurring amino acid substitutions causing SRS, which are situated away from the active center of SpmSyn and thus are not directly involved in the catalysis. Two of the mutations, M35R and P112L, are reported for the first time in this study. It is demonstrated, both experimentally and computationally, that for such mutations the major effect resulting in dysfunctional SpmSyn is the destabilization of the protein. In vitro experiments indicated either no presence or very little amount of the mutant SpmSyn in patient cells. In silico modeling predicted that all studied mutations in this work destabilize SpmSyn and some of them abolish homo-dimer formation. Since dimerization and structural stability are equally important for the wild type function of SpmSyn, it is proposed that the SRS caused by mutations occurring in the N-domain of SpmSyn is a result of dysfunctional mutant proteins being partially unfolded and degraded by the proteomic machinery of the cell or being unable to form a homo-dimer.
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