ArticleCellular and molecular bioengineering2010
Stabilization of the spectrin-like domains of nesprin-1α by the evolutionarily conserved "adaptive" domain.
Article in Cellular and molecular bioengineering, 2010. 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.
The trial behind it
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, 27 citations in OpenAlex.
- NUAK1 Inhibition Alleviates Ischemia-Reperfusion Injury via SYNE1-YAP1.Circulation research · 2026Article
- Cargo Recognition of Nesprin-2 by the Dynein Adapter Bicaudal D2 for a Nuclear Positioning Pathway That Is Important for Brain Development.Biochemistry · 2026Article
- KASH proteins transform from passive tethers to dynamic conductors of motor-driven nuclear dynamics.Current opinion in cell biology · 2025Review
- Active microtubule-actin cross-talk mediated by a nesprin-2G-kinesin complex.Science advances · 2025Article
- Nesprin-1: novel regulator of striated muscle nuclear positioning and mechanotransduction.Biochemical Society transactions · 2023Review
- A Multisensory Network Drives Nuclear Mechanoadaptation.Biomolecules · 2022Review
- Nesprin-1 impact on tumorigenic cell phenotypes.Molecular biology reports · 2020Article
- Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.BMC structural biology · 2018Article
- Nesprins and Lamins in Health and Diseases of Cardiac and Skeletal Muscles.Frontiers in physiology · 2018Review
- Centrifugal Displacement of Nuclei Reveals Multiple LINC Complex Mechanisms for Homeostatic Nuclear Positioning.Current biology : CB · 2017Article
- The nesprin-cytoskeleton interface probed directly on single nuclei is a mechanically rich system.Nucleus (Austin, Tex.) · 2017Article
- Lamin A/C Is Required for ChAT-Dependent Neuroblastoma Differentiation.Molecular neurobiology · 2017Article
- Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis.Human molecular genetics · 2017Article
- Nesprin-2-dependent ERK1/2 compartmentalisation regulates the DNA damage response in vascular smooth muscle cell ageing.Cell death and differentiation · 2015Article
- Nesprins anchor kinesin-1 motors to the nucleus to drive nuclear distribution in muscle cells.Development (Cambridge, England) · 2015Article
- Cytoskeletal interactions at the nuclear envelope mediated by nesprins.International journal of cell biology · 2012Article
- Nucleoskeleton mechanics at a glance.Journal of cell science · 2011Article
- Beyond lamins other structural components of the nucleoskeleton.Methods in cell biology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Nesprins are located at the outer and inner membranes of the nuclear envelope and help link the cytoskeleton to the nucleoskeleton. Nesprin-1α, located at the inner nuclear membrane, binds to A-type lamins and emerin and has homology to spectrin-repeat proteins. However, the mechanical and thermodynamic properties of the spectrin-like repeats (SLRs) of nesprin-1α and the potential structural contributions of the unique central domain were untested. In other spectrin superfamily proteins, tandem spectrin-repeat domains undergo cooperatively coupled folding and unfolding. We hypothesized that the large central domain, which interrupts SLRs and is conserved in other nesprin isoforms, might confer unique structural properties. To test this model we measured the thermal unfolding of nesprin-1α fragments using circular dichroism and dynamic light scattering. The SLRs in nesprin-1α were found to have structural and thermodynamic properties typical of spectrins. The central domain had relatively little secondary structure as an isolated fragment, but significantly stabilized larger SLR-containing molecules by increasing their overall helicity, thermal stability and cooperativity of folding. We suggest this domain, now termed the 'adaptive' domain (AD), also strengthens dimerization and inhibits unfolding. Further engineering of the isolated AD, and AD-containing nesprin molecules, may yield new information about the higher-order association of cooperative protein motifs.
Identifiers
What OpenQuestion holds
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 OpenQuestion graph.