ArticleThe Journal of biological chemistry2013
Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.
- Collagenase-mediated extracellular matrix targeting for enhanced drug penetration and therapeutic efficacy in nanoscale delivery systems for cancer therapy.Journal of nanobiotechnology · 2025Pooled it
- Article
- Bacterial collagenase harnesses collagen geometry for processive cleavage.Nature communications · 2026Article
- Optimizing chicken muscle stem cell isolation using recombinant proteolytic enzymes for cultured meat production.Food science of animal resources · 2026Article
- Dupuytren's disease cords are weakened ex vivo by injection of recombinant collagenase G - A proof-of-concept study.PloS one · 2026Article
- ARSC advances · 2025Article
- Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.Biomolecules · 2024Article
- Thermostable Bacterial Collagenolytic Proteases: A Review.Journal of microbiology and biotechnology · 2024Review
- A conserved strategy to attack collagen: The activator domain in bacterial collagenases unwinds triple-helical collagen.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Unlocking the Potential of Collagenases: Structures, Functions, and Emerging Therapeutic Horizons.Biodesign research · 2024Article
- Novel marine metalloprotease-new approaches for inhibition of biofilm formation of Stenotrophomonas maltophilia.Applied microbiology and biotechnology · 2023Article
- Dual function of the O-antigen WaaL ligase of Aggregatibacter actinomycetemcomitans.Molecular oral microbiology · 2023Article
- A novel computationally engineered collagenase reduces the force required for tooth extraction in an ex-situ porcine jaw model.Journal of biological engineering · 2023Article
- Alpinetin: anti-human gastric cancer potential and urease inhibition activityArchives of medical science : AMS · 2023Article
- Discovery of New Microbial Collagenase Inhibitors.Life (Basel, Switzerland) · 2022Article
- Discovery and Characterization of Synthesized and FDA-Approved Inhibitors of Clostridial and Bacillary Collagenases.Journal of medicinal chemistry · 2022Article
- Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation.Biotechnology for biofuels and bioproducts · 2022Article
- Coarse-grained modeling of the calcium, sodium, magnesium and potassium cations interacting with proteins.Journal of molecular modeling · 2022Article
- An Introduction to Bacterial Biofilms and Their Proteases, and Their Roles in Host Infection and Immune Evasion.Biomolecules · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Clostridial collagenases are among the most efficient enzymes to degrade by far the most predominant protein in the biosphere. Here we present crystal structures of the peptidases of three clostridial collagenase isoforms (ColG, ColH, and ColT). The comparison of unliganded and liganded structures reveals a quaternary subdomain dynamics. In the unliganded ColH structure, this globular dynamics is modulated by an aspartate switch motion that binds to the catalytic zinc. We further identified a calcium binding site in proximity to the catalytic zinc. Both ions are required for full activity, explaining why calcium critically affects the enzymatic activity of clostridial collagenases. Our studies further reveal that loops close to the active site thus serve as characteristic substrate selectivity filter. These elements explain the distinct peptidolytic and collagenolytic activities of these enzymes and provide a rational framework to engineer collagenases with customized substrate specificity as well as for inhibitor design.
Indexed as
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.