ArticleProceedings of the National Academy of Sciences of the United States of America2014
Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 2025Article
- Neurofilament Light Protein Rod Domain Exhibits Structural Heterogeneity.Biomolecules · 2024Article
- Single-molecule experiments reveal the elbow as an essential folding guide in SMC coiled-coil arms.Biophysical journal · 2022Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Slow Transition Path Times Reveal a Complex Folding Barrier in a Designed Protein.Frontiers in chemistry · 2020Article
- Molecular mechanics of coiled coils loaded in the shear geometry.Chemical science · 2018Article
- Intermediate filament mechanics in vitro and in the cell: from coiled coils to filaments, fibers and networks.Current opinion in cell biology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Intermediate filaments (IFs) are key to the mechanical strength of metazoan cells. Their basic building blocks are dimeric coiled coils mediating hierarchical assembly of the full-length filaments. Here we use single-molecule force spectroscopy by optical tweezers to assess the folding and stability of coil 2B of the model IF protein vimentin. The coiled coil was unzipped from its N and C termini. When pulling from the C terminus, we observed that the coiled coil was resistant to force owing to the high stability of the C-terminal region. Pulling from the N terminus revealed that the N-terminal half is considerably less stable. The mechanical pulling assay is a unique tool to study and control seed formation and structure propagation of the coiled coil. We then used rigorous theory-based deconvolution for a model-free extraction of the energy landscape and local stability profiles. The data obtained from the two distinct pulling directions complement each other and reveal a tripartite stability of the coiled coil: a labile N-terminal half, followed by a medium stability section and a highly stable region at the far C-terminal end. The different stability regions provide important insight into the mechanics of IF assembly.
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Registered trials
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