ArticleJournal of the American Chemical Society2011
Molecular mechanochemistry: low force switch slows enzymatic cleavage of human type I collagen monomer.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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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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
44 citing papers in PubMed, 92 citations in OpenAlex.
- Article
- Bacterial collagenase harnesses collagen geometry for processive cleavage.Nature communications · 2026Article
- Collagen Mechanics.Sub-cellular biochemistry · 2026Review
- Physiological mechanical forces accelerate the degradation of bovine lung collagen fibers by bacterial collagenase.Scientific reports · 2024Article
- Modeling collagen fibril degradation as a function of matrix microarchitecture.bioRxiv : the preprint server for biology · 2024Article
- Mechanochemistry of collagen.Acta biomaterialia · 2023Review
- Mechanical strain modulates extracellular matrix degradation and byproducts in an isoform-specific manner.Biochimica et biophysica acta. General subjects · 2023Article
- Stiffening of the extracellular matrix is a sufficient condition for airway hyperreactivity.Journal of applied physiology (Bethesda, Md. : 1985) · 2021Article
- Does the Heart Want What It Wants? A Case for Self-Adapting, Mechano-Sensitive Therapies After Infarction.Frontiers in cardiovascular medicine · 2021Article
- Connective Tissue Remodeling in Myopia and its Potential Role in Increasing Risk of Glaucoma.Current opinion in biomedical engineering · 2020Article
- 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
- Optical Tweezers Approaches for Probing Multiscale Protein Mechanics and Assembly.Frontiers in molecular biosciences · 2020Review
- The Relationship Between Scleral Strain Change and Differential Cumulative Intraocular Pressure Exposure in the Nonhuman Primate Chronic Ocular Hypertension Model.Investigative ophthalmology & visual science · 2019Article
- Models of tendon development and injury.BMC biomedical engineering · 2019Article
- Environmentally Controlled Curvature of Single Collagen Proteins.Biophysical journal · 2018Article
- Non-enzymatic cross-linking of collagen type II fibrils is tuned via osmolality switch.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2018Article
- Single-Molecule Assay for Proteolytic Susceptibility: Force-Induced Collagen Destabilization.Biophysical journal · 2018Article
- Unlocking Collagen Proteolysis with a Gentle Pull.Biophysical journal · 2018Article
- A biochemo-mechano coupled, computational model combining membrane transport and pericellular proteolysis in tissue mechanics.Proceedings. Mathematical, physical, and engineering sciences · 2017Article
- Internal strain drives spontaneous periodic buckling in collagen and regulates remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
In vertebrate animals, fibrillar collagen accumulates, organizes, and persists in structures which resist mechanical force. This antidissipative behavior is possibly due to a mechanochemical force-switch which converts collagen from enzyme-susceptible to enzyme-resistant. Degradation experiments on native tissue and reconstituted fibrils suggest that collagen/enzyme kinetics favor the retention of loaded collagen. We used a massively parallel, single molecule, mechanochemical reaction assay to demonstrate that the effect is derivative of molecular mechanics. Tensile loads higher than 3 pN dramatically reduced (10×) the enzymatic degradation rate of recombinant human type I collagen monomers by Clostridium histolyticum compared to unloaded controls. Because bacterial collagenase accesses collagen at multiple sites and is an aggressive cleaver of the collagen triple helical domain, the results suggest that collagen molecular architecture is generally more stable when mechanically strained in tension. Thus the tensile mechanical state of collagen monomers is likely to be correlated to their longevity in tissues. Further, strain-actuated molecular stability of collagen may constitute the fundamental basis of a smart structural mechanism which enhances the ability of animals to place, retain, and load-optimize material in the path of mechanical 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.