ArticleNano letters2015
Mapping Mechanical Force Propagation through Biomolecular Complexes.
Article in Nano letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
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Who cites it
45 citing papers in PubMed, 108 citations in OpenAlex.
- Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026Article
- Force-Induced Ankle Opening Reveals Mechanical Stabilization of the Ankle of Human β-Cardiac Myosin.ACS nano · 2026Article
- Cadherin-23 mutations cause calcium-dependent, allele-sensitive mechanosensory defects.iScience · 2026Article
- Framework for Quantifying the Efficiency of Competing Signal Transmission Modes in Proteins.Journal of the American Chemical Society · 2026Article
- A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.bioRxiv : the preprint server for biology · 2026Article
- Dynamic Coupling between Tom22 Motions and Tom40 Pore Dynamics Modulates Ion Transport in the Mitochondrial TOM Complex.Journal of chemical information and modeling · 2025Article
- UltrastrongScience advances · 2025Article
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- Article
- Engineering the Mechanical Stability of a Therapeutic Affibody/PD-L1 Complex by Anchor Point Selection.bioRxiv : the preprint server for biology · 2024Article
- Engineering an artificial catch bond using mechanical anisotropy.Nature communications · 2024Article
- Single-molecule force stability of the SARS-CoV-2-ACE2 interface in variants-of-concern.Nature nanotechnology · 2024Article
- Anisotropic Friction in a Ligand-Protein Complex.Nano letters · 2023Article
- May the force be with you: The role of hyper-mechanostability of the bone sialoprotein binding protein during early stages ofFrontiers in chemistry · 2023Article
- Revealing a Hidden Intermediate of Rotatory Catalysis with X-ray Crystallography and Molecular Simulations.ACS central science · 2022Article
- Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022Article
- Angle-dependent strength of a single chemical bond by stereographic force spectroscopy.Chemical science · 2022Article
- Mapping Mechanostable Pulling Geometries of a Therapeutic Anticalin/CTLA-4 Protein Complex.Nano letters · 2022Article
- Model systems for optical trapping: the physical basis and biological applications.Biophysical reviews · 2021Review
- Anisotropy in mechanical unfolding of protein upon partner-assisted pulling and handle-assisted pulling.Communications biology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
Here we employ single-molecule force spectroscopy with an atomic force microscope (AFM) and steered molecular dynamics (SMD) simulations to reveal force propagation pathways through a mechanically ultrastable multidomain cellulosome protein complex. We demonstrate a new combination of network-based correlation analysis supported by AFM directional pulling experiments, which allowed us to visualize stiff paths through the protein complex along which force is transmitted. The results implicate specific force-propagation routes nonparallel to the pulling axis that are advantageous for achieving high dissociation forces.
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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.