ArticleBiophysical journal2006
Extending a spectrin repeat unit. II: rupture behavior.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed.
- Viscoelasticity of ECM and cells-origin, measurement and correlation.Mechanobiology in medicine · 2024Review
- Sub-region analysis of DMD gene in cases with idiopathic generalized epilepsy.Neurogenetics · 2023Article
- Review
- Mechanical Unfolding of Spectrin Repeats Induces Water-Molecule Ordering.Biophysical journal · 2020Article
- Empirical and Computational Comparison of Alternative Therapeutic Exon Skip Repairs for Duchenne Muscular Dystrophy.Biochemistry · 2019Article
- Stability of dystrophin STR fragments in relation to junction helicity.Biochimica et biophysica acta · 2008Article
- Unique elastic properties of the spectrin tetramer as revealed by multiscale coarse-grained modeling.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Spectrin domains lose cooperativity in forced unfolding.Biophysical journal · 2007Article
- Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Biophysical journal · 2006Article
- Extending a spectrin repeat unit. I: linear force-extension response.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A spectrin repeat unit was subject to extension using cyclic expansion nonequilibrium molecular dynamics. Periodic boundary conditions were used to examine the effects of the contiguous alpha-helical linker on the force response. The measured force-extension curve shows a linear increase in the force response when the spectrin repeat unit is extended by approximately 0.4 nm. After that point, the force response peaks and subsequently declines. The peak in the force response marks the point where the spectrin repeat unit undergoes a change in its material properties from a strongly elastic material to a mostly viscous one, on the timescales of the simulations. The force peak is also correlated with rupture of the alpha-helical linker, and is likely the event responsible for the peaks in the sawtooth-pattern force-extension curves measured by atomic force microscopy experiments. Rupture of the linker involves simultaneously breaking approximately four hydrogen bonds that maintain the alpha-helical linker. After this initial rupture, the linker undergoes simple helix-to-coil transitions as the spectrin repeat unit continues to be extended. The implications of linker rupture in the interpretation of unfolding and atomic force microscopy experiments are also discussed.
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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.