ArticleMolecular & cellular proteomics : MCP2014
Time-resolved analysis of the matrix metalloproteinase 10 substrate degradome.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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.
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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
23 citing papers in PubMed, 58 citations in OpenAlex.
- Degradomics for large-scale mechanistic insights on proteases and proteolysis in human health.The FEBS journal · 2026Review
- Data Processing and Analysis in Positional Proteomics.Proteomics · 2025Review
- Substrate O-glycosylation actively regulates extracellular proteolysis.Protein science : a publication of the Protein Society · 2024Article
- Emerging roles for the ADAMTS-like family of matricellular proteins in cardiovascular disease through regulation of the extracellular microenvironment.Molecular biology reports · 2024Review
- Redefining metalloproteases specificity through network proteolysis.Trends in molecular medicine · 2024Review
- Sensitive and High-Throughput Exploration of Protein N-Termini by TMT-TAILS N-Terminomics.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Matrix Metalloproteinase-10 in Kidney Injury Repair and Disease.International journal of molecular sciences · 2022Review
- Article
- The Pharmacological TAILS of Matrix Metalloproteinases and Their Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Matrix Metalloproteinases: How Much Can They Do?International journal of molecular sciences · 2020Article
- Matrix Metalloproteinases Expressed in Response to Bacterial Vaginosis Disrupt the Endocervical Epithelium, Increasing Transmigration of HIV.Infection and immunity · 2020Article
- Degradome of soluble ADAM10 and ADAM17 metalloproteases.Cellular and molecular life sciences : CMLS · 2020Article
- Quantitative Multiplex Substrate Profiling of Peptidases by Mass Spectrometry.Molecular & cellular proteomics : MCP · 2019Article
- Matrix metalloproteinases in emphysema.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners.Scientific reports · 2018Article
- Determinants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.Current protein & peptide science · 2017Review
- Stromelysin-2 (MMP10) Moderates Inflammation by Controlling Macrophage Activation.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Article
- Matrix Metalloproteinase 10 Degradomics in Keratinocytes and Epidermal Tissue Identifies Bioactive Substrates With Pleiotropic Functions.Molecular & cellular proteomics : MCP · 2015Article
- Novel Biological Substrates of Human Kallikrein 7 Identified through Degradomics.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Proteolysis is an irreversible post-translational modification that affects intra- and intercellular communication by modulating the activity of bioactive mediators. Key to understanding protease function is the system-wide identification of cleavage events and their dynamics in physiological contexts. Despite recent advances in mass spectrometry-based proteomics for high-throughput substrate screening, current approaches suffer from high false positive rates and only capture single states of protease activity. Here, we present a workflow based on multiplexed terminal amine isotopic labeling of substrates for time-resolved substrate degradomics in complex proteomes. This approach significantly enhances confidence in substrate identification and categorizes cleavage events by specificity and structural accessibility of the cleavage site. We demonstrate concomitant quantification of cleavage site spanning peptides and neo-N and/or neo-C termini to estimate relative ratios of noncleaved and cleaved forms of substrate proteins. By applying this strategy to dissect the matrix metalloproteinase 10 (MMP10) substrate degradome in fibroblast secretomes, we identified the extracellular matrix protein ADAMTS-like protein 1 (ADAMTSL1) as a direct MMP10 substrate and revealed MMP10-dependent ectodomain shedding of platelet-derived growth factor receptor alpha (PDGFRα) as well as sequential processing of type I collagen. The data have been deposited to the ProteomeXchange Consortium with identifier PXD000503.
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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.