ArticleScientific reports2018
Skeletal Muscle Dystrophy mutant of lamin A alters the structure and dynamics of the Ig fold domain.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- A predictive mechanochemical modeling framework for the deformation and remodeling of the nuclear lamina.bioRxiv : the preprint server for biology · 2026Article
- Computational Characterization of Pathogenic LMNA Missense Variants: Structural Instability, Altered Binding, and Conformational Dynamics.Human mutation · 2026Article
- Nuclear pore dysfunction and disease: a complex opportunity.Nucleus (Austin, Tex.) · 2024Review
- Computational modeling establishes mechanotransduction as a potent modulator of the mammalian circadian clock.Journal of cell science · 2024Article
- PIGB maintains nuclear lamina organization in skeletal muscle of Drosophila.The Journal of cell biology · 2024Article
- The lamin A/C Ig-fold undergoes cell density-dependent changes that alter epitope binding.Nucleus (Austin, Tex.) · 2023Article
- Slower diffusion and anomalous association of R453W lamin A protein alter nuclear architecture in AD-EDMD.RSC advances · 2022Article
- Recent insight into intermediate filament structure.Current opinion in cell biology · 2021Review
- Lamin A/C Mechanotransduction in Laminopathies.Cells · 2020Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in the different domains of A-type lamin proteins cause a diverse plethora of diseases collectively termed as laminopathies which can affect multiple organs. Ig fold is one such domain of lamin A which is implicated in numerous nuclear interactions wherein the mutations lead to different laminopathies. W514R is one such mutation in the Ig fold which leads to severe phenotypes in Skeletal Muscle Dystrophy (SMD) which is a class of laminopathies. In this report, we elucidated gross alterations in structure and dynamics at the level of individual amino acids. These studies indicate altered conformational features of residues in the close vicinity of W514. Imaging of mammalian cells transfected with the mutant have shown distinct perturbation of the nuclear meshwork with concomitant alteration in nuclear interactions as a result of increased oligomerization of Ig W514R. Hence, this novel approach of amalgamating theoretical and experimental procedures to predict the severity of a mutant in the context of laminopathies could be extended for numerous lamin A mutants.
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