ArticleJournal of the American Chemical Society2015
KINATEST-ID: a pipeline to develop phosphorylation-dependent terbium sensitizing kinase assays.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026Review
- Subtimizer: Computational Workflow for Structure-Guided Design of Potent and Selective Kinase Peptide Substrates.Journal of chemical information and modeling · 2026Article
- Accessing Self-Illuminated, Luminescent Lanthanide Probes by Enzymatic Radiophosphorylation.Inorganic chemistry · 2025Article
- Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays.RSC chemical biology · 2025Article
- Acetyl-Click Screening Platform Identifies Small-Molecule Inhibitors of Histone Acetyltransferase 1 (HAT1).Journal of medicinal chemistry · 2023Article
- Novel Bruton's Tyrosine Kinase (BTK) Substrates for Time-Resolved Luminescence Assays.ACS chemical biology · 2022Article
- Shining Light on Protein Kinase Biomarkers with Fluorescent Peptide Biosensors.Life (Basel, Switzerland) · 2022Review
- A Novel ELISA-Based Peptide Biosensor Assay for Screening ABL1 ActivityFrontiers in pharmacology · 2021Article
- Multiplexable fluorescence lifetime imaging (FLIM) probes for Abl and Src-family kinases.Chemical communications (Cambridge, England) · 2020Article
- Design of a Protein Motif Responsive to Tyrosine Nitration and an Encoded Turn-Off Sensor of Tyrosine Nitration.Biochemistry · 2019Article
- Phosphorylation-dependent protein design: design of a minimal protein kinase-inducible domain.Organic & biomolecular chemistry · 2019Article
- High-throughput Identification of FLT3 Wild-type and Mutant Kinase Substrate Preferences and Application to Design of SensitiveMolecular & cellular proteomics : MCP · 2019Article
- Assays for tyrosine phosphorylation in human cells.Methods in enzymology · 2019Article
- Redox-Responsive Protein Design: Design of a Small Protein Motif Dependent on Glutathionylation.Biochemistry · 2018Article
- In Silico Design and in Vitro Characterization of Universal Tyrosine Kinase Peptide Substrates.Biochemistry · 2018Article
- Progress towards a public chemogenomic set for protein kinases and a call for contributions.PloS one · 2017Article
- Modular, Antibody-free Time-Resolved LRET Kinase Assay Enabled by Quantum Dots and Tb(3+)-sensitizing Peptides.Scientific reports · 2016Article
- A dual-functional lanthanide nanoprobe for both living cell imaging and ICP-MS quantification of active protease.Chemical science · 2016Article
- Selective Sensing of Tyrosine Phosphorylation in Peptides Using Terbium(III) Complexes.International journal of analytical chemistry · 2016Review
- A Cell-Based Assay for Measuring Endogenous BcrAbl Kinase Activity and Inhibitor Resistance.PloS one · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Nonreceptor protein tyrosine kinases (NRTKs) are essential for cellular homeostasis and thus are a major focus of current drug discovery efforts. Peptide substrates that can enhance lanthanide ion luminescence upon tyrosine phosphorylation enable rapid, sensitive screening of kinase activity, however design of suitable substrates that can distinguish between tyrosine kinase families is a huge challenge. Despite their different substrate preferences, many NRTKs are structurally similar even between families. Furthermore, the development of lanthanide-based kinase assays is hampered by incomplete understanding of how to integrate sequence selectivity with metal ion binding, necessitating laborious iterative substrate optimization. We used curated proteomic data from endogenous kinase substrates and known Tb(3+)-binding sequences to build a generalizable in silico pipeline with tools to generate, screen, align, and select potential phosphorylation-dependent Tb(3+)-sensitizing substrates that are most likely to be kinase specific. We demonstrated the approach by developing several substrates that are selective within kinase families and amenable to high-throughput screening (HTS) applications. Overall, this strategy represents a pipeline for developing efficient and specific assays for virtually any tyrosine kinase that use HTS-compatible lanthanide-based detection. The tools provided in the pipeline also have the potential to be adapted to identify peptides for other purposes, including other enzyme assays or protein-binding ligands.
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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.