ArticleScientific reports2016
Significance of 1B and 2B domains in modulating elastic properties of lamin A.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 2025Article
- Lamin variants cause cardiac arrhythmogenicity in Drosophila.Disease models & mechanisms · 2025Article
- Atypical Progeria Primarily Manifesting as Premature Cardiac Valvular Disease Segregates withJournal of cardiovascular development and disease · 2024Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Crystal structure of progeria mutant S143F lamin A/C reveals increased hydrophobicity driving nuclear deformation.Communications biology · 2022Article
- Bend, Push, Stretch: Remarkable Structure and Mechanics of Single Intermediate Filaments and Meshworks.Cells · 2021Review
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Nuclear filaments: role in chromosomal positioning and gene expression.Nucleus (Austin, Tex.) · 2020Review
- Genotype-phenotype analysis of LMNA-related diseases predicts phenotype-selective alterations in lamin phosphorylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Biomechanical defects and rescue of cardiomyocytes expressing pathologic nuclear lamins.Cardiovascular research · 2018Article
- Nuclear Lamin Protein C Is Linked to Lineage-Specific, Whole-Cell Mechanical Properties.Cellular and molecular bioengineering · 2018Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear lamins are type V intermediate filament proteins which form an elastic meshwork underlying the inner nuclear membrane. Lamins directly contribute to maintain the nuclear shape and elasticity. More than 400 mutations have been reported in lamin A that are involved in diseases known as laminopathies. These mutations are scattered mainly in the lamin rod domain along with some in its C-terminal domain. The contribution of the rod domain towards the elasticity of lamin A molecule was hitherto unknown. Here, we have elucidated the significance of the 1B and 2B domains of the rod in modulating the elastic behavior of lamin A by single-molecule force spectroscopy. In addition, we have also studied the network forming capacity of these domains and their corresponding viscoelastic behavior. We have shown that the 1B domain has the ability to form a lamin-like network and resists larger deformation. However at the single-molecular level, both the domains have comparable mechanical properties. The self-assembly of the 1B domain contributes to the elasticity of the lamin A network.
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