ReviewBritish journal of pharmacology2019
Monoclonal antibodies against metzincin targets.
Review in British journal of pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 41 citations in OpenAlex.
- Proteolytic remodelling of the extracellular matrix by pericytes.The FEBS journal · 2026Review
- Fabrication and application of targeted ciprofloxacin nanocarriers for the treatment of chronic bacterial prostatitis.International journal of pharmaceutics: X · 2024Article
- Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease.International journal of molecular sciences · 2023Review
- Novel Approaches for Targeting Metalloproteinases.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Editorial: Advances in the therapeutic targeting of human matrix metalloproteinases in health and disease.Frontiers in molecular biosciences · 2023Article
- Targeting Aggrecanases for Osteoarthritis Therapy: From Zinc Chelation to Exosite Inhibition.Journal of medicinal chemistry · 2022Review
- Metalloproteinase inhibition reduces AML growth, prevents stem cell loss, and improves chemotherapy effectiveness.Blood advances · 2022Article
- Immunomodulatory role of metalloproteases in cancers: Current progress and future trends.Frontiers in immunology · 2022Review
- Endothelial Glycocalyx Degradation in Critical Illness and Injury.Frontiers in medicine · 2022Review
- ADAM and ADAMTS disintegrin and metalloproteinases as major factors and molecular targets in vascular malfunction and disease.Advances in pharmacology (San Diego, Calif.) · 2022Article
- Coronary Disease Association With ADAMTS7 Is Due to Protease Activity.Circulation research · 2021Article
- Metalloproteinases in Ovarian Cancer.International journal of molecular sciences · 2021Review
- Hyalectanase Activities by the ADAMTS Metalloproteases.International journal of molecular sciences · 2021Review
- Exosite inhibition of ADAMTS-5 by a glycoconjugated arylsulfonamide.Scientific reports · 2021Article
- Peptide-Based Inhibitors of ADAM and ADAMTS Metalloproteinases.Frontiers in molecular biosciences · 2021Review
- Targeting the Host Response: Can We Manipulate Extracellular Matrix Metalloproteinase Activity to Improve Influenza Virus Infection Outcomes?Frontiers in molecular biosciences · 2021Review
- ADAMTS5 in Osteoarthritis: Biological Functions, Regulatory Network, and Potential Targeting Therapies.Frontiers in molecular biosciences · 2021Review
- Extracellular Matrix Enzymes and Immune Cell Biology.Frontiers in molecular biosciences · 2021Review
- Editorial: ADAM, ADAMTS and Astacin Proteases: Challenges and Breakthroughs in the -Omics Era.Frontiers in molecular biosciences · 2021Article
- ADAMTS proteases in cardiovascular physiology and disease.Open biology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The metzincin clan of metalloproteinases includes the MMP, disintegrin and metalloproteinase (ADAM) and ADAM with thrombospondin motifs families, which cleave extracellular targets in a wide range of (patho)physiological processes. Antibodies constitute a powerful tool to modulate the activity of these enzymes for both therapeutic and research purposes. In this review, we give an overview of monoclonal antibodies (mAbs) that have been tested in preclinical disease models, human trials and important studies of metzincin structure and function. Initial attempts to develop therapeutic small molecule inhibitors against MMPs were hampered by structural similarities between metzincin active sites and, consequently, off-target effects. Therefore, more recently, mAbs have been developed that do not bind to the active site but bind to surface-exposed loops that are poorly conserved in closely related family members. Inhibition of protease activity by these mAbs occurs through a variety of mechanisms, including (i) barring access to the active site, (ii) disruption of exosite binding, and (iii) prevention of protease activation. These different modes of inhibition are discussed in the context of the antibodies' potency, selectivity and, importantly, the effects in models of disease and clinical trials. In addition, various innovative strategies that were used to generate anti-metzincin mAbs are discussed. LINKED ARTICLES: This article is part of a themed section on Translating the Matrix. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.1/issuetoc.
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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.