ArticleMethods in enzymology2014
Global analysis of cellular proteolysis by selective enzymatic labeling of protein N-termini.
Article in Methods in enzymology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Caspase-mediated cleavage events hidden by secondary proteolysis during apoptosis.Protein science : a publication of the Protein Society · 2026Article
- In-Depth Specificity Profiling of Endopeptidases Using Dedicated Mix-and-Split Synthetic Peptide Libraries and Mass Spectrometry.Analytical chemistry · 2023Article
- Multiplex substrate profiling by mass spectrometry for proteases.Methods in enzymology · 2023Article
- N-Terminomics Strategies for Protease Substrates Profiling.Molecules (Basel, Switzerland) · 2021Review
- The proteolytic landscape of cells exposed to non-lethal stresses is shaped by executioner caspases.Cell death discovery · 2021Article
- An optimized quantitative proteomics method establishes the cell type-resolved mouse brain secretome.The EMBO journal · 2020Article
- Deep profiling of protease substrate specificity enabled by dual random and scanned human proteome substrate phage libraries.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Defining the proteolytic landscape during enterovirus infection.PLoS pathogens · 2020Article
- Protease-responsive mass barcoded nanotranslators for simultaneously quantifying the intracellular activity of cascaded caspases in apoptosis pathways.Chemical science · 2020Article
- New beginnings and new ends: methods for large-scale characterization of protein termini and their use in plant biology.Journal of experimental botany · 2019Review
- Engineering peptide ligase specificity by proteomic identification of ligation sites.Nature chemical biology · 2018Article
- Monitoring proteolytic processing events by quantitative mass spectrometry.Expert review of proteomics · 2017Review
- Comparative Analysis of Mitochondrial N-Termini from Mouse, Human, and Yeast.Molecular & cellular proteomics : MCP · 2017Article
- Proteomic Substrate Identification for Membrane Proteases in the Brain.Frontiers in molecular neuroscience · 2016Review
- Mass spectrometry-based detection and assignment of protein posttranslational modifications.ACS chemical biology · 2015Review
- Unraveling the mechanism of cell death induced by chemical fibrils.Nature chemical biology · 2014Article
- Circulating proteolytic signatures of chemotherapy-induced cell death in humans discovered by N-terminal labeling.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proteolysis is a critical modification leading to alteration of protein function with important outcomes in many biological processes. However, for the majority of proteases, we have an incomplete understanding of both cellular substrates and downstream effects. Here, we describe detailed protocols and applications for using the rationally engineered peptide ligase, subtiligase, to specifically label and capture protein N-termini generated by proteases either induced or added to complex biological samples. This method allows identification of the protein targets as well as their precise cleavage locations. This approach has revealed >8000 proteolytic sites in healthy and apoptotic cells including >1700 caspase cleavages. One can further determine substrate preferences through rate analysis with quantitative mass spectrometry, physiological substrate specificities, and even infer the identity of proteases operating in the cell. In this chapter, we also describe how this experimental method can be generalized to investigate proteolysis in any biological sample.
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Registered trials
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