ArticlePloS one2012
Using bacteria to determine protein kinase specificity and predict target substrates.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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
18 citing papers in PubMed.
- Polypharmacology-Driven Discovery and Design of Highly Selective, Dual and Multitargeting Inhibitors ofCurrent drug targets · 2024Review
- Article
- The Okur-Chung Neurodevelopmental Syndrome Mutation CK2Frontiers in molecular biosciences · 2022Article
- Structural and Enzymological Evidence for an Altered Substrate Specificity in Okur-Chung Neurodevelopmental Syndrome Mutant CK2αFrontiers in molecular biosciences · 2022Article
- Illuminating the kinome: Visualizing real-time kinase activity in biological systems using genetically encoded fluorescent protein-based biosensors.Current opinion in chemical biology · 2020Review
- Kinase Substrate Profiling Using a Proteome-wide Serine-Oriented Human Peptide Library.Biochemistry · 2018Article
- Characterizing Protein Kinase Substrate Specificity Using the Proteomic Peptide Library (ProPeL) Approach.Current protocols in chemical biology · 2018Article
- Mtb PKNA/PKNB Dual Inhibition Provides Selectivity Advantages for Inhibitor Design To Minimize Host Kinase Interactions.ACS medicinal chemistry letters · 2017Article
- Defining Human Tyrosine Kinase Phosphorylation Networks Using Yeast as an In Vivo Model Substrate.Cell systems · 2017Article
- Ssp2 Binding Activates the Smk1 Mitogen-Activated Protein Kinase.Molecular and cellular biology · 2017Article
- Cushing's syndrome mutant PKAFEBS letters · 2017Article
- Protein networks and activation of lymphocytes.Current opinion in immunology · 2015Review
- Article
- Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog.Frontiers in microbiology · 2015Article
- The Carboxy-terminus of BAK1 regulates kinase activity and is required for normal growth of Arabidopsis.Frontiers in plant science · 2014Article
- Toward a systems-level view of dynamic phosphorylation networks.Frontiers in genetics · 2014Review
- pLogo: a probabilistic approach to visualizing sequence motifs.Nature methods · 2013Article
- Profiling the substrate specificity of protein kinases by on-bead screening of peptide libraries.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The identification of protein kinase targets remains a significant bottleneck for our understanding of signal transduction in normal and diseased cellular states. Kinases recognize their substrates in part through sequence motifs on substrate proteins, which, to date, have most effectively been elucidated using combinatorial peptide library approaches. Here, we present and demonstrate the ProPeL method for easy and accurate discovery of kinase specificity motifs through the use of native bacterial proteomes that serve as in vivo libraries for thousands of simultaneous phosphorylation reactions. Using recombinant kinases expressed in E. coli followed by mass spectrometry, the approach accurately recapitulated the well-established motif preferences of human basophilic (Protein Kinase A) and acidophilic (Casein Kinase II) kinases. These motifs, derived for PKA and CK II using only bacterial sequence data, were then further validated by utilizing them in conjunction with the scan-x software program to computationally predict known human phosphorylation sites with high confidence.
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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.