ArticleJournal of structural biology2011
Structure and stability of the lamin A tail domain and HGPS mutant.
Article in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
- Structural Diversity and Distribution of Nuclear Matrix Constituent Protein Class Nuclear Lamina Proteins in Streptophytic Algae.Genome biology and evolution · 2024Article
- The lamin A/C Ig-fold undergoes cell density-dependent changes that alter epitope binding.Nucleus (Austin, Tex.) · 2023Article
- Article
- Perspective: Controlling Epidermal Terminal Differentiation with Transcriptional Bursting and RNA Bodies.Journal of developmental biology · 2020Review
- Lamin microaggregates lead to altered mechanotransmission in progerin-expressing cells.Nucleus (Austin, Tex.) · 2020Article
- Review
- Skeletal Muscle Dystrophy mutant of lamin A alters the structure and dynamics of the Ig fold domain.Scientific reports · 2018Article
- Hutchinson-Gilford Progeria Syndrome: A Premature Aging Disease.Molecular neurobiology · 2018Review
- Modeling and Experiment Reveal Structure and Nanomechanics across the Inverse Temperature Transition inACS biomaterials science & engineering · 2017Article
- Review
- Article
- The tail domain of lamin B1 is more strongly modulated by divalent cations than lamin A.Nucleus (Austin, Tex.) · 2015Article
- Mechanical Properties and Failure of Biopolymers: Atomistic Reactions to Macroscale Response.Topics in current chemistry · 2015Review
- Interfacial binding and aggregation of lamin A tail domains associated with Hutchinson-Gilford progeria syndrome.Biophysical chemistry · 2014Article
- Nuclear stiffening inhibits migration of invasive melanoma cells.Cellular and molecular bioengineering · 2014Article
- Broken nuclei--lamins, nuclear mechanics, and disease.Trends in cell biology · 2014Review
- The cellular mastermind(?)-mechanotransduction and the nucleus.Progress in molecular biology and translational science · 2014Review
- From lamins to lamina: a structural perspective.Histochemistry and cell biology · 2013Review
- Calcium causes a conformational change in lamin A tail domain that promotes farnesyl-mediated membrane association.Biophysical journal · 2013Article
- Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation.Frontiers in physiology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Hutchinson-Gilford progeria syndrome (HGPS) is a premature aging syndrome caused by the expression and accumulation of a mutant form of lamin A, Δ50 lamin A. As a component of the cell's nucleoskeleton, lamin A plays an important role in the mechanical stabilization of the nuclear envelope and in other nuclear functions. It is largely unknown how the characteristic 50 amino acid deletion affects the conformation of the mostly intrinsically disordered tail domain of lamin A. Here we perform replica exchange molecular dynamics simulations of the tail domain and determine an ensemble of semi-stable structures. Based on these structures we show that the ZMPSTE 24 cleavage site on the precursor form of the lamin A tail domain orients itself in such a way as to facilitate cleavage during the maturation process. We confirm our simulated structures by comparing the thermodynamic properties of the ensemble structures to in vitro stability measurements. Using this combination of experimental and computational techniques, we compare the size, heterogeneity of size, thermodynamic stability of the Ig-fold, as well as the mechanisms of force-induced denaturation. Our data shows that the Δ50 lamin A tail domain is more compact and displays less heterogeneity than the mature lamin A tail domain. Altogether these results suggest that the altered structure and stability of the tail domain can explain changed protein-protein and protein-DNA interactions and may represent an etiology of the disease. Also, this study provides the first molecular structure(s) of the lamin A tail domain, which is confirmed by thermodynamic tests in experiment.
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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 OpenQuestion graph.