ArticleACS nano2009
Mechanochemistry: one bond at a time.
Article in ACS nano, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
37 citing papers in PubMed, 145 citations in OpenAlex.
- Forces in mechanically interlocked materials.Chemical Society reviews · 2026Review
- Modeling Targeted Mechanochemistry in Polymeric Solids.Chemical reviews · 2026Review
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- High pressure-derived nonsymmetrical [CuScience advances · 2024Article
- Self-Healing Ability of Perovskites Observed via Photoluminescence Response on Nanoscale Local Forces and Mechanical Damage.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Mechanical Activation of Forbidden Photoreactivity in Oxa-di-π-methane Rearrangement.The Journal of organic chemistry · 2022Article
- The Power of Touch: Type 4 Pili, the von Willebrand A Domain, and Surface Sensing by Pseudomonas aeruginosa.Journal of bacteriology · 2022Review
- Protein folding modulates the chemical reactivity of a Gram-positive adhesin.Nature chemistry · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Synthetic oligorotaxanes exert high forces when folding under mechanical load.Nature nanotechnology · 2018Article
- Identification of allosteric disulfides from labile bonds in X-ray structures.Royal Society open science · 2018Article
- Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F.Biophysical journal · 2016Article
- Some studies on generalized coordinate sets for polyatomic molecules.The Journal of chemical physics · 2015Article
- Transport regulation of two-dimensional receptor-ligand association.Biophysical journal · 2015Article
- Inducing and quantifying forbidden reactivity with single-molecule polymer mechanochemistry.Nature chemistry · 2015Article
- Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1.The Journal of biological chemistry · 2014Article
- Identification of allosteric disulfides from prestress analysis.Biophysical journal · 2014Article
- Impact of local compressive stress on the optical transitions of single organic dye molecules.Nature nanotechnology · 2014Article
- Calculation and visualization of atomistic mechanical stresses in nanomaterials and biomolecules.PloS one · 2014Article
- Combined single cell AFM manipulation and TIRFM for probing the molecular stability of multilayer fibrinogen matrices.Ultramicroscopy · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Single-molecule force-clamp spectroscopy offers a novel platform for mechanically denaturing proteins by applying a constant force to a polyprotein. A powerful emerging application of the technique is that, by introducing a disulfide bond in each protein module, the chemical kinetics of disulfide bond cleavage under different stretching forces can be probed at the single-bond level. Even at forces much lower than that which can rupture the chemical bond, the breaking of the S-S bond at the presence of various chemical reducing agents is significantly accelerated. Our previous work demonstrated that the rate of thiol/disulfide exchange reaction is force-dependent and well-described by an Arrhenius term of the form r = A(exp((FΔx(r) - E(a))/k(B)T)[nucleophile]). From Arrhenius fits to the force dependency of the reduction rate, we measured the bond elongation parameter, Δx(r), along the reaction coordinate to the transition state of the S(N)2 reaction cleaved by different nucleophiles and enzymes, never before observed by any other technique. For S-S cleavage by various reducing agents, obtaining the Δx(r) value can help depicting the energy landscapes and elucidating the mechanisms of the reactions at the single-molecule level. Small nucleophiles, such as 1,4-dl-dithiothreitol (DTT), tris(2-carboxyethyl)phosphine (TCEP), and l-cysteine, react with the S-S bond with monotonically increasing rates under the applied force, while thioredoxin enzymes exhibit both stretching-favored and -resistant reaction-rate regimes. These measurements demonstrate the power of the single-molecule force-clamp spectroscopy approach in providing unprecedented access to chemical reactions.
Identifiers
What OpenQuestion holds
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.