ArticleCurrent protocols in chemical biology2018
Characterizing Protein Kinase Substrate Specificity Using the Proteomic Peptide Library (ProPeL) Approach.
Article in Current protocols in chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
6 citing papers in PubMed, 12 citations in OpenAlex.
- Salivary Proteomics & Gene Expression Analysis: Applications in Orthodontics and Oral Health Care Research-A Pilot Project.Biomarker insights · 2025Article
- Article
- Structural and Enzymological Evidence for an Altered Substrate Specificity in Okur-Chung Neurodevelopmental Syndrome Mutant CK2αFrontiers in molecular biosciences · 2022Article
- The Okur-Chung Neurodevelopmental Syndrome Mutation CK2Frontiers in molecular biosciences · 2022Article
- Repurposing approved drugs on the pathway to novel therapies.Medicinal research reviews · 2020Review
- High-throughput Identification of FLT3 Wild-type and Mutant Kinase Substrate Preferences and Application to Design of SensitiveMolecular & cellular proteomics : MCP · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Characterizing protein kinase substrate specificity motifs represents a powerful step in elucidating kinase-signaling cascades. The protocol described here uses a bacterial system to evaluate kinase specificity motifs in vivo, without the need for radioactive ATP. The human kinase of interest is cloned into a heterologous bacterial expression vector and allowed to phosphorylate E. coli proteins in vivo, consistent with its endogenous substrate preferences. The cells are lysed, and the bacterial proteins are digested into peptides and phosphoenriched using bulk TiO
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Registered trials
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