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• W1680787172 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. • Knowing the cleavage preferences is essential for understanding the functions of MMPs • Profiling of >18,500 peptide sequences determined the cleavage preferences of 18 MMPs • Our results enabled comparison of the cleavage preferences of MMPs on a global scale • This study generated a roadmap for the structural-functional studies of MMPs Kukreja et al. present the results of the high-throughput multiplexed profiling of the cleavage preferences of 18 proteinases from the main sub-groups of the MMP family that lead to defining the substrate cleavage redundancy and specificity in the MMP family, to a better foundation for the follow-on structural-functional studies of MMPs, and to a means to predict in silico the cleavage targets of the individual MMPs." @default.
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• W1680787172 date "2015-08-01" @default.
• W1680787172 modified "2023-09-27" @default.
• W1680787172 title "High-Throughput Multiplexed Peptide-Centric Profiling Illustrates Both Substrate Cleavage Redundancy and Specificity in the MMP Family" @default.
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• W1680787172 doi "https://doi.org/10.1016/j.chembiol.2015.07.008" @default.
• W1680787172 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4546507" @default.
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