ArticleACS chemical biology2017
Targeting the Hemopexin-like Domain of Latent Matrix Metalloproteinase-9 (proMMP-9) with a Small Molecule Inhibitor Prevents the Formation of Focal Adhesion Junctions.
Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- CD177Gut · 2026Article
- Matrix metalloproteinase-9 regulates cell adhesion and membrane protrusive activity of ovarian cancer cells.FEBS open bio · 2026Article
- A guide to the types, structures, and multifaceted functions of matrix metalloproteinases in cancer.The FEBS journal · 2026Review
- The role of ECM mechanics in cancer mechanotransduction through unraveling the molecular machinery of integrins, FAK, and YAP signaling.Cellular & molecular biology letters · 2026Review
- Integrating Single-Cell Profiling with Generative AI forMolecules (Basel, Switzerland) · 2026Article
- The Extracellular Matrix and the Immune System in Acute Lung Injury: Partners in Damage and Repair.Biomedicines · 2025Review
- The hemopexin domain of matrix metalloproteinase-9 attenuates lipopolysaccharide-induced interleukin-6 secretion in liver.Scientific reports · 2025Article
- Using High-Throughput Screening to Identify Crosslinking Peptides That Control Cell-Mediated Matrix Degradation.Advanced healthcare materials · 2025Article
- Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma.Scientific reports · 2025Article
- One-pot synthesis of 4-pyrimidone-2-thioether through base/acid-mediated condensation ofRSC advances · 2024Article
- Ursonic acid inhibits migration and invasion of human osteosarcoma cells through the suppression of mitogen-activated protein kinases and matrix metalloproteinases.Molecular biology reports · 2023Article
- A phase 1b study of andecaliximab in combination with S-1 plus platinum in Japanese patients with gastric adenocarcinoma.Scientific reports · 2022Article
- MMP9: A Tough Target for Targeted Therapy for Cancer.Cancers · 2022Review
- Validating Cell Surface Proteases as Drug Targets for Cancer Therapy: What Do We Know, and Where Do We Go?Cancers · 2022Review
- Downregulation of miR‑29b‑3p promotes α‑tubulin deacetylation by targeting the interaction of matrix metalloproteinase‑9 with integrin β1 in nasal polyps.International journal of molecular medicine · 2021Article
- Inhibition of MMP2-PEX by a novel ester of dihydroxy cinnamic and linoleic acid from the seagrass Cymodocea serrulata.Scientific reports · 2021Article
- Bioguided Fractionation of Local Plants against Matrix Metalloproteinase9 and Its Cytotoxicity against Breast Cancer Cell Models: In Silico and In Vitro Study (Part II).Molecules (Basel, Switzerland) · 2021Article
- The Pharmacological TAILS of Matrix Metalloproteinases and Their Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Bioguided Fractionation of Local Plants against Matrix Metalloproteinase9 and Its Cytotoxicity against Breast Cancer Cell Models: In Silico and In Vitro Study.Molecules (Basel, Switzerland) · 2020Article
- Dental malformations associated with biallelic MMP20 mutations.Molecular genetics & genomic medicine · 2020Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
A lack of target specificity has greatly hindered the success of inhibitor development against matrix metalloproteinases (MMPs) for the treatment of various cancers. The MMP catalytic domains are highly conserved, whereas the hemopexin-like domains of MMPs are unique to each family member. The hemopexin-like domain of MMP-9 enhances cancer cell migration through self-interaction and heterointeractions with cell surface proteins including CD44 and α4β1 integrin. These interactions activate EGFR-MAP kinase dependent signaling that leads to cell migration. In this work, we generated a library of compounds, based on hit molecule N-[4-(difluoromethoxy)phenyl]-2-[(4-oxo-6-propyl-1H-pyrimidin-2-yl)sulfanyl]-acetamide, that target the hemopexin-like domain of MMP-9. We identify N-(4-fluorophenyl)-4-(4-oxo-3,4,5,6,7,8-hexahydroquinazolin-2-ylthio)butanamide, 3c, as a potent lead (K
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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.