ArticleThe Biochemical journal2015
Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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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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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Exploring the Regulatory Function of NGAL in MMP-9 Complexes.Computational and structural biotechnology journal · 2026Article
- ALS Patients Exhibit Altered Levels of Total and Active MMP-9 and Several Other Biomarkers in Serum and CSF Compared to Healthy Controls and Other Neurologic Diseases.International journal of molecular sciences · 2025Article
- Tissue inhibitors of metalloproteinases are proteolytic targets of matrix metalloproteinase 9.Matrix biology : journal of the International Society for Matrix Biology · 2023Article
- Matrix metalloproteinases in arthritis: towards precision medicine.Nature reviews. Rheumatology · 2023Review
- How to place the duality of specific MMP-9 inhibition for treatment of inflammatory bowel diseases into clinical opportunities?Frontiers in immunology · 2022Review
- Extracellular Metalloproteinases in the Plasticity of Excitatory and Inhibitory Synapses.Cells · 2021Review
- Structural characterisation of inhibitory and non-inhibitory MMP-9-TIMP-1 complexes and implications for regulatory mechanisms of MMP-9.Scientific reports · 2021Article
- Inhibition of MMP2-PEX by a novel ester of dihydroxy cinnamic and linoleic acid from the seagrass Cymodocea serrulata.Scientific reports · 2021Article
- Proteoform Analysis of Matrix Metalloproteinase-9/Gelatinase B and Discovery of Its Citrullination in Rheumatoid Arthritis Synovial Fluids.Frontiers in immunology · 2021Article
- Homotrimeric MMP-9 is an active hitchhiker on alpha-2-macroglobulin partially escaping protease inhibition and internalization through LRP-1.Cellular and molecular life sciences : CMLS · 2020Article
- Article
- Molecular Interactions Stabilizing the Promatrix Metalloprotease-9·Serglycin Heteromer.International journal of molecular sciences · 2020Article
- The Role of Matrix Metalloproteinase-9 in Atherosclerotic Plaque Instability.Mediators of inflammation · 2020Review
- Angiopoietin-2 predicts morbidity in adults with Fontan physiology.Scientific reports · 2019Article
- Metalloproteinases mediate diabetes-induced retinal neuropathy and vasculopathy.Cellular and molecular life sciences : CMLS · 2019Review
- Targeted lipid nanoparticle delivery of calcitriol to human monocyte-derived macrophages in vitro and in vivo: investigation of the anti-inflammatory effects of calcitriol.International journal of nanomedicine · 2019Article
- Gelatinase B/Matrix Metalloproteinase-9 as Innate Immune Effector Molecule in Achalasia.Clinical and translational gastroenterology · 2018Article
- Neutrophils and Activated Macrophages Control Mucosal Immunity by Proteolytic Cleavage of Antileukoproteinase.Frontiers in immunology · 2018Article
- Article
- Targeting the Hemopexin-like Domain of Latent Matrix Metalloproteinase-9 (proMMP-9) with a Small Molecule Inhibitor Prevents the Formation of Focal Adhesion Junctions.ACS chemical biology · 2017Article
Corrections and comments
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Authors and funding
18 authors at 6 institutions in 5 countries.
Funding
Abstract
Gelatinase B/matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) cleaves many substrates and is produced by most cell types as a zymogen, proMMP-9, in complex with the tissue inhibitor of metalloproteinases-1 (TIMP-1). Natural proMMP-9 occurs as monomers, homomultimers and heterocomplexes, but our knowledge about the overall structure of proMMP-9 monomers and multimers is limited. We investigated biochemical, biophysical and functional characteristics of zymogen and activated forms of MMP-9 monomers and multimers. In contrast with a conventional notion of a dimeric nature of MMP-9 homomultimers, we demonstrate that these are reduction-sensitive trimers. Based on the information from electrophoresis, AFM and TEM, we generated a 3D structure model of the proMMP-9 trimer. Remarkably, the proMMP-9 trimers possessed a 50-fold higher affinity for TIMP-1 than the monomers. In vivo, this finding was reflected in a higher extent of TIMP-1 inhibition of angiogenesis induced by trimers compared with monomers. Our results show that proMMP-9 trimers constitute a novel structural and functional entity that is differentially regulated by TIMP-1.
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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.