ArticleJournal of proteome research2014
Global analysis of human nonreceptor tyrosine kinase specificity using high-density peptide microarrays.
Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Substrate-Derived Peptides for Selective Covalent Inhibition of Protein Tyrosine Kinases.ACS chemical biology · 2026Article
- Context-dependent peptide recognition shapes tyrosine kinase substrate specificity beyond consensus motifs.bioRxiv : the preprint server for biology · 2026Article
- Substrate-derived peptides for selective covalent inhibition of protein tyrosine kinases.bioRxiv : the preprint server for biology · 2026Article
- Molecular determinants of differential substrate selection between the Src family kinases Lck and Src.Frontiers in immunology · 2026Article
- Profiling tyrosine kinase substrate recognition using bacterial peptide display and deep sequencing.bioRxiv : the preprint server for biology · 2025Article
- Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The fitness cost of spurious phosphorylation.The EMBO journal · 2024Article
- DNA-encoded probe-based assay for profiling plant kinase activities.PNAS nexus · 2024Article
- Sulfoproteomics Workflow with Precursor Ion Accurate Mass Shift Analysis Reveals Novel Tyrosine Sulfoproteins in the Golgi.Journal of proteome research · 2024Article
- The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023Article
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- Dissection of the catalytic and regulatory structure-function relationships of Csk protein tyrosine kinase.Frontiers in cell and developmental biology · 2023Review
- Saturation mutagenesis of a predicted ancestral Syk-family kinase.Protein science : a publication of the Protein Society · 2022Article
- Novel Bruton's Tyrosine Kinase (BTK) Substrates for Time-Resolved Luminescence Assays.ACS chemical biology · 2022Article
- Fluorescence Lifetime Imaging Probes for Cell-Based Measurements of Enzyme Activity.Methods in molecular biology (Clifton, N.J.) · 2022Article
- ExploringMicrobial cell (Graz, Austria) · 2021Review
- Structure, Function, and Regulation of the SRMS Tyrosine Kinase.International journal of molecular sciences · 2020Review
- Application of a Substrate-Mediated Selection with c-Src Tyrosine Kinase to a DNA-Encoded Chemical Library.Molecules (Basel, Switzerland) · 2019Article
- Assays for tyrosine phosphorylation in human cells.Methods in enzymology · 2019Article
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8 authors.
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Abstract
Protein kinases phosphorylate substrates in the context of specific phosphorylation site sequence motifs. The knowledge of the specific sequences that are recognized by kinases is useful for mapping sites of phosphorylation in protein substrates and facilitates the generation of model substrates to monitor kinase activity. Here, we have adapted a positional scanning peptide library method to a microarray format that is suitable for the rapid determination of phosphorylation site motifs for tyrosine kinases. Peptide mixtures were immobilized on glass slides through a layer of a tyrosine-free Y33F mutant avidin to facilitate the analysis of phosphorylation by radiolabel assay. A microarray analysis provided qualitatively similar results in comparison with the solution phase peptide library "macroarray" method. However, much smaller quantities of kinases were required to phosphorylate peptides on the microarrays, which thus enabled a proteome scale analysis of kinase specificity. We illustrated this capability by microarray profiling more than 80% of the human nonreceptor tyrosine kinases (NRTKs). Microarray results were used to generate a universal NRTK substrate set of 11 consensus peptides for in vitro kinase assays. Several substrates were highly specific for their cognate kinases, which should facilitate their incorporation into kinase-selective biosensors.
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