ArticleData in brief2016
Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14.
Article in Data in brief, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Deep learning guided design of protease substrates.Nature communications · 2026Article
- Using High-Throughput Screening to Identify Crosslinking Peptides That Control Cell-Mediated Matrix Degradation.Advanced healthcare materials · 2025Article
- Quantifying and Controlling the Proteolytic Degradation of Cell Adhesion Peptides.ACS biomaterials science & engineering · 2024Article
- Substrate O-glycosylation actively regulates extracellular proteolysis.Protein science : a publication of the Protein Society · 2024Article
- Quantifying and controlling the proteolytic degradation of cell adhesion peptides.bioRxiv : the preprint server for biology · 2024Article
- Matrix metalloproteinase 7 contributes to intestinal barrier dysfunction by degrading tight junction protein Claudin-7.Frontiers in immunology · 2022Article
- Host-Derived Matrix Metalloproteinase-13 Activity Promotes Multiple Myeloma-Induced Osteolysis and Reduces Overall Survival.Cancer research · 2021Article
- Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen.Nature communications · 2021Article
- Quantitative profiling of protease specificity.PLoS computational biology · 2021Article
- Identification and characterization of the proteolytic flagellin from the common freshwater bacterium Hylemonella gracilis.Scientific reports · 2020Article
- Predictive models of protease specificity based on quantitative protease-activity profiling data.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- Matrix metalloproteinases - From the cleavage data to the prediction tools and beyond.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Emerging challenges in the design of selective substrates, inhibitors and activity-based probes for indistinguishable proteases.The FEBS journal · 2017Review
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Authors and funding
19 authors.
Funding
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Abstract
The data described provide a comprehensive resource for the family-wide active site specificity portrayal of the human matrix metalloproteinase family. We used the high-throughput proteomic technique PICS (Proteomic Identification of protease Cleavage Sites) to comprehensively assay 9 different MMPs. We identified more than 4300 peptide cleavage sites, spanning both the prime and non-prime sides of the scissile peptide bond allowing detailed subsite cooperativity analysis. The proteomic cleavage data were expanded by kinetic analysis using a set of 6 quenched-fluorescent peptide substrates designed using these results. These datasets represent one of the largest specificity profiling efforts with subsequent structural follow up for any protease family and put the spotlight on the specificity similarities and differences of the MMP family. A detailed analysis of this data may be found in Eckhard et al. (2015) [1]. The raw mass spectrometry data and the corresponding metadata have been deposited in PRIDE/ProteomeXchange with the accession number PXD002265.
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