ArticleJournal of the American Chemical Society2012
Conformational dynamics accompanying the proteolytic degradation of trimeric collagen I by collagenases.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 62 citations in OpenAlex.
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- Modeling collagen fibril degradation as a function of matrix microarchitecture.bioRxiv : the preprint server for biology · 2024Article
- Unlocking the Potential of Collagenases: Structures, Functions, and Emerging Therapeutic Horizons.Biodesign research · 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
- An Update on the Clinical Efficacy and Safety of Collagen Injectables for Aesthetic and Regenerative Medicine Applications.Polymers · 2023Review
- Cryptic collagen elements as signaling hubs in the regulation of tumor growth and metastasis.Journal of cellular physiology · 2020Review
- 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
- Multiplexed protein force spectroscopy reveals equilibrium protein folding dynamics and the low-force response of von Willebrand factor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- 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
3 authors at 1 institution in 1 country.
Funding
Abstract
Collagenases are the principal enzymes responsible for the degradation of collagens during embryonic development, wound healing, and cancer metastasis. However, the mechanism by which these enzymes disrupt the highly chemically and structurally stable collagen triple helix remains incompletely understood. We used a single-molecule magnetic tweezers assay to characterize the cleavage of heterotrimeric collagen I by both the human collagenase matrix metalloproteinase-1 (MMP-1) and collagenase from Clostridium histolyticum. We observe that the application of 16 pN of force causes an 8-fold increase in collagen proteolysis rates by MMP-1 but does not affect cleavage rates by Clostridium collagenase. Quantitative analysis of these data allows us to infer the structural changes in collagen associated with proteolytic cleavage by both enzymes. Our data support a model in which MMP-1 cuts a transient, stretched conformation of its recognition site. In contrast, our findings suggest that Clostridium collagenase is able to cleave the fully wound collagen triple helix, accounting for its lack of force sensitivity and low sequence specificity. We observe that the cleavage of heterotrimeric collagen is less force sensitive than the proteolysis of a homotrimeric collagen model peptide, consistent with studies suggesting that the MMP-1 recognition site in heterotrimeric collagen I is partially unwound at equilibrium.
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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.