ArticleBiophysical journal2018
Single-Molecule Assay for Proteolytic Susceptibility: Force-Induced Collagen Destabilization.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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
20 citing papers in PubMed.
- Beyond the Single Molecule: Multiplexed Methods in Force Spectroscopy.Annual review of biophysics · 2026Review
- Collagen Mechanics.Sub-cellular biochemistry · 2026Review
- Probing the Dynamic Strength of Biomolecular Interactions with Single-Cell Centrifugation.ACS central science · 2025Article
- A guide to building a low-cost centrifuge force microscope module for single-molecule force experiments.Nature protocols · 2025Review
- High-Throughput Centrifuge Force Microscopy Reveals Dynamic Immune-Cell Avidity at the Single-Cell Level.bioRxiv : the preprint server for biology · 2025Article
- Mechanochemistry of collagen.Acta biomaterialia · 2023Review
- High-throughput single-molecule quantification of individual base stacking energies in nucleic acids.Nature communications · 2023Article
- Discovering design principles of collagen molecular stability using a genetic algorithm, deep learning, and experimental validation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Optimization of a Calcium-Based Treatment Method for Jellyfish to Design Food for the Future.Foods (Basel, Switzerland) · 2022Article
- Ensemble Force Spectroscopy by Shear Forces.Journal of visualized experiments : JoVE · 2022Article
- Sequence-dependent mechanics of collagen reflect its structural and functional organization.Biophysical journal · 2021Article
- Mechanical unfolding of ensemble biomolecular structures by shear force.Chemical science · 2021Article
- Wi-Fi Live-Streaming Centrifuge Force Microscope for Benchtop Single-Molecule Experiments.Biophysical journal · 2020Article
- Optical Tweezers Approaches for Probing Multiscale Protein Mechanics and Assembly.Frontiers in molecular biosciences · 2020Review
- Tension in fibrils suppresses their enzymatic degradation - A molecular mechanism for 'use it or lose it'.Matrix biology : journal of the International Society for Matrix Biology · 2020Review
- Article
- Facile single-molecule pull-down assay for analysis of endogenous proteins.Physical biology · 2019Article
- Force Spectroscopy and Beyond: Innovations and Opportunities.Biophysical journal · 2018Review
- Environmentally Controlled Curvature of Single Collagen Proteins.Biophysical journal · 2018Article
- Unlocking Collagen Proteolysis with a Gentle Pull.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Force plays a key role in regulating dynamics of biomolecular structure and interactions, yet techniques are lacking to manipulate and continuously read out this response with high throughput. We present an enzymatic assay for force-dependent accessibility of structure that makes use of a wireless mini-radio centrifuge force microscope to provide a real-time readout of kinetics. The microscope is designed for ease of use, fits in a standard centrifuge bucket, and offers high-throughput, video-rate readout of individual proteolytic cleavage events. Proteolysis measurements on thousands of tethered collagen molecules show a load-enhanced trypsin sensitivity, indicating destabilization of the triple helix.
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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.