ArticlePLoS computational biology2009
Molecular mechanics of the alpha-actinin rod domain: bending, torsional, and extensional behavior.
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 52 citations in OpenAlex.
- SimHS-AFMfit-MD: An Integrative Approach for Inferring Alpha-Actinin Atomic Conformational Dynamics.Nano letters · 2026Article
- The Importance of Alpha-Actinin Proteins in Platelet Formation and Function, and Their Causative Role in Congenital Macrothrombocytopenia.International journal of molecular sciences · 2021Review
- Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin.Science advances · 2021Article
- Novel ACTN1 variants in cases of thrombocytopenia.Human mutation · 2019Article
- Dynamic Regulation of α-Actinin's Calponin Homology Domains on F-Actin.Biophysical journal · 2016Article
- Hypoxia alters the recruitment of tropomyosins into the actin stress fibres of neuroblastoma cells.BMC cancer · 2015Article
- WEBnm@ v2.0: Web server and services for comparing protein flexibility.BMC bioinformatics · 2014Article
- Role of sequence and structural polymorphism on the mechanical properties of amyloid fibrils.PloS one · 2014Article
- On the activation of integrin αIIbβ3: outside-in and inside-out pathways.Biophysical journal · 2013Article
- Article
- The interaction of vinculin with actin.PLoS computational biology · 2013Article
- Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins.PloS one · 2013Article
- Localized lipid packing of transmembrane domains impedes integrin clustering.PLoS computational biology · 2013Article
- A molecular trajectory of α-actinin activation.Biophysical journal · 2012Article
- Phosphorylation primes vinculin for activation.Biophysical journal · 2012Article
- Electron microscopy and x-ray diffraction evidence for two Z-band structural states.Biophysical journal · 2011Article
- Visualizing dynamic cytoplasmic forces with a compliance-matched FRET sensor.Journal of cell science · 2011Article
- Limited digestion of α-actinin in the presence of F-actin.Biophysics (Nagoya-shi, Japan) · 2011Article
- A molecular dynamics investigation of vinculin activation.Biophysical journal · 2010Article
- Phosphorylation facilitates the integrin binding of filamin under force.Biophysical journal · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
alpha-Actinin is an actin crosslinking molecule that can serve as a scaffold and maintain dynamic actin filament networks. As a crosslinker in the stressed cytoskeleton, alpha-actinin can retain conformation, function, and strength. alpha-Actinin has an actin binding domain and a calmodulin homology domain separated by a long rod domain. Using molecular dynamics and normal mode analysis, we suggest that the alpha-actinin rod domain has flexible terminal regions which can twist and extend under mechanical stress, yet has a highly rigid interior region stabilized by aromatic packing within each spectrin repeat, by electrostatic interactions between the spectrin repeats, and by strong salt bridges between its two anti-parallel monomers. By exploring the natural vibrations of the alpha-actinin rod domain and by conducting bending molecular dynamics simulations we also predict that bending of the rod domain is possible with minimal force. We introduce computational methods for analyzing the torsional strain of molecules using rotating constraints. Molecular dynamics extension of the alpha-actinin rod is also performed, demonstrating transduction of the unfolding forces across salt bridges to the associated monomer of the alpha-actinin rod domain.
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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.