ArticleThe Journal of biological chemistry2013
Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state.
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 34 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
34 citing papers in PubMed, 74 citations in OpenAlex.
- High-Resolution Relaxometry for Fragment Screening.Journal of medicinal chemistry · 2026Article
- Membrane-Type 5 Matrix Metalloproteinase (MT5-MMP): Background and Proposed Roles in Normal Physiology and Disease.Biomolecules · 2025Review
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Novel Insights into the Catalytic Mechanism of Collagenolysis by Zn(II)-Dependent Matrix Metalloproteinase-1.Biochemistry · 2024Article
- Catalytic Mechanism of Collagen Hydrolysis by Zinc(II)-Dependent Matrix Metalloproteinase-1.The journal of physical chemistry. B · 2023Article
- Mechanism of the Early Catalytic Events in the Collagenolysis by Matrix Metalloproteinase-1.Chemphyschem : a European journal of chemical physics and physical chemistry · 2023Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints.Biophysical reviews · 2022Review
- Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.Nature communications · 2022Article
- A synergy between the catalytic and structural Zn(II) ions and the enzyme and substrate dynamics underlies the structure-function relationships of matrix metalloproteinase collagenolysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Allosteric Communications between Domains Modulate the Activity of Matrix Metalloprotease-1.Biophysical journal · 2020Article
- The Photocatalyzed Thiol-ene reaction: A New Tag to Yield Fast, Selective and reversible Paramagnetic Tagging of Proteins.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Integrative Approaches in Structural Biology: A More Complete Picture from the Combination of Individual Techniques.Biomolecules · 2019Review
- Joint X-ray/NMR structure refinement of multidomain/multisubunit systems.Journal of biomolecular NMR · 2019Article
- Characterization and regulation of MT1-MMP cell surface-associated activity.Chemical biology & drug design · 2019Article
- Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains.Frontiers in molecular biosciences · 2018Review
- Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Regulation of HuR structure and function by dihydrotanshinone-I.Nucleic acids research · 2017Article
- Combining NMR and small angle X-ray scattering for the study of biomolecular structure and dynamics.Archives of biochemistry and biophysics · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Catalysis of collagen degradation by matrix metalloproteinase 1 (MMP-1) has been proposed to critically rely on flexibility between the catalytic (CAT) and hemopexin-like (HPX) domains. A rigorous assessment of the most readily accessed conformations in solution is required to explain the onset of substrate recognition and collagenolysis. The present study utilized paramagnetic NMR spectroscopy and small angle x-ray scattering (SAXS) to calculate the maximum occurrence (MO) of MMP-1 conformations. The MMP-1 conformations with large MO values (up to 47%) are restricted into a relatively small conformational region. All conformations with high MO values differ largely from the closed MMP-1 structures obtained by x-ray crystallography. The MO of the latter is ~20%, which represents the upper limit for the presence of this conformation in the ensemble sampled by the protein in solution. In all the high MO conformations, the CAT and HPX domains are not in tight contact, and the residues of the HPX domain reported to be responsible for the binding to the collagen triple-helix are solvent exposed. Thus, overall analysis of the highest MO conformations indicated that MMP-1 in solution was poised to interact with collagen and then could readily proceed along the steps of collagenolysis.
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.