ArticleThe Journal of biological chemistry2009
Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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.
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Who cites it
50 citing papers in PubMed, 86 citations in OpenAlex.
- Nisin bacteriocin blocks T. denticola-triggered MMP2 activation and pathogen internalization via TLR2.Scientific reports · 2026Article
- Membrane-Type 5 Matrix Metalloproteinase (MT5-MMP): Background and Proposed Roles in Normal Physiology and Disease.Biomolecules · 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
- Mechanistic Insight into the Fragmentation of Type I Collagen Fibers into Peptides and Amino Acids by aApplied and environmental microbiology · 2022Article
- 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
- Review
- Matrix Metalloproteinase Triple-Helical Peptide Inhibitors: Potential Cross-Reactivity with Caspase-11.Molecules (Basel, Switzerland) · 2019Article
- Review
- Characterization and regulation of MT1-MMP cell surface-associated activity.Chemical biology & drug design · 2019Article
- MT1-MMP Binds Membranes by Opposite Tips of Its β Propeller to Position It for Pericellular Proteolysis.Structure (London, England : 1993) · 2019Article
- Mechanisms of Action of Novel Drugs Targeting Angiogenesis-Promoting Matrix Metalloproteinases.Frontiers in immunology · 2019Review
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- Tricine as a convenient scaffold for the synthesis ofTetrahedron letters · 2018Article
- Second Generation Triple-Helical Peptide Inhibitors of Matrix Metalloproteinases.Journal of medicinal chemistry · 2017Article
- Effects of Mutations on Structure-Function Relationships of Matrix Metalloproteinase-1.International journal of molecular sciences · 2016Article
- Importance of the Linker Region in Matrix Metalloproteinase-1 Domain Interactions.RSC advances · 2016Article
- Modified platelet deposition on matrix metalloproteinase 13 digested collagen I.Journal of thrombosis and haemostasis : JTH · 2015Article
- Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Frontiers in bioscience (Landmark edition) · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Collagen serves as a structural scaffold and a barrier between tissues, and thus collagen catabolism (collagenolysis) is required to be a tightly regulated process in normal physiology. In turn, the destruction or damage of collagen during pathological states plays a role in tumor growth and invasion, cartilage degradation, or atherosclerotic plaque formation and rupture. Several members of the matrix metalloproteinase (MMP) family catalyze the hydrolysis of collagen triple helical structure. This study has utilized triple helical peptide (THP) substrates and inhibitors to dissect MMP-1 collagenolytic behavior. Analysis of MMP-1/THP interactions by hydrogen/deuterium exchange mass spectrometry followed by evaluation of wild type and mutant MMP-1 kinetics led to the identification of three noncatalytic regions in MMP-1 (residues 285-295, 302-316, and 437-457) and two specific residues (Ile-290 and Arg-291) that participate in collagenolysis. Ile-290 and Arg-291 contribute to recognition of triple helical structure and facilitate both the binding and catalysis of the triple helix. Evidence from this study and prior studies indicates that the MMP-1 catalytic and hemopexin-like domains collaborate in collagen catabolism by properly aligning the triple helix and coupling conformational states to facilitate hydrolysis. This study is the first to document the roles of specific residues within the MMP-1 hemopexin-like domain in substrate binding and turnover. Noncatalytic sites, such as those identified here, can ultimately be utilized to create THP inhibitors that target MMPs implicated in disease progression while sparing proteases with host-beneficial functions.
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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.