ArticleChemistry & biology2015
High-Throughput Multiplexed Peptide-Centric Profiling Illustrates Both Substrate Cleavage Redundancy and Specificity in the MMP Family.
Article in Chemistry & biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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.
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Who cites it
30 citing papers in PubMed, 39 citations in OpenAlex.
- Matrix metalloproteinase-guided targeting of vesicular stomatitis virus to tumors following systemic administration.Signal transduction and targeted therapy · 2026Article
- Chemical basis of fluorogenic substrate probe design: revisiting the past to discover the new in biochemistry.RSC chemical biology · 2026Review
- mRNA Display for Identifying Peptide Substrates of Enzymes.Biochemistry · 2026Review
- Tuning scaffold degradation with non-natural peptidomimetics to control human umbilical vein endothelial cell morphology and vessel formation.Acta biomaterialia · 2026Article
- Proteolysis activity mapping and substrate discovery platform for identifying tumor-activated biosensors.Nature chemical biology · 2026Article
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- Targeting marine jellyfish toxins: development of metalloproteinase inhibitors through a specific method for protease substrate identification.Archives of toxicology · 2026Article
- Deep learning guided design of protease substrates.Nature communications · 2026Article
- Tuning Scaffold Degradation with Non-Natural Peptidomimetics to Control Human Umbilical Vein Endothelial Cell Morphology and Vessel Formation.bioRxiv : the preprint server for biology · 2025Article
- Uncovering hidden protein modifications with native top-down mass spectrometry.Nature methods · 2025Article
- Deep quantification of substrate turnover defines protease subsite cooperativity.Molecular systems biology · 2024Article
- Article
- PepSeq: a fully in vitro platform for highly multiplexed serology using customizable DNA-barcoded peptide libraries.Nature protocols · 2023Review
- Host protease activity classifies pneumonia etiology.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)-A CleavEx Based Analysis.International journal of molecular sciences · 2020Article
- MT1-MMP activatable fluorogenic probes with enhanced specificity via high-affinity peptide conjugation for tumor imaging.Biomaterials science · 2020Article
- Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Biomolecules · 2020Article
- Matrix Metalloproteinase Triple-Helical Peptide Inhibitors: Potential Cross-Reactivity with Caspase-11.Molecules (Basel, Switzerland) · 2019Article
- Engineered materials for organoid systems.Nature reviews. Materials · 2019Article
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Matrix metalloproteinases (MMPs) play incompletely understood roles in health and disease. Knowing the MMP cleavage preferences is essential for a better understanding of the MMP functions and design of selective inhibitors. To elucidate the cleavage preferences of MMPs, we employed a high-throughput multiplexed peptide-centric profiling technology involving the cleavage of 18,583 peptides by 18 proteinases from the main sub-groups of the MMP family. Our results enabled comparison of the MMP substrates on a global scale, leading to the most efficient and selective substrates. The data validated the accuracy of our cleavage prediction software. This software allows us and others to locate, with nearly 100% accuracy, the MMP cleavage sites in the peptide sequences. In addition to increasing our understanding of both the selectivity and the redundancy of the MMP family, our study generated a roadmap for the subsequent MMP structural-functional studies and efficient substrate and inhibitor design.
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What OpenQuestion holds
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.