Evidence map›Paper›PMID 24260399›Full record

ArticlePloS one2013

A novel quantitative kinase assay using bacterial surface display and flow cytometry.

Sónia Troeira Henriques, Louise Thorstholm, Yen-Hua Huang, Jennifer A Getz, Patrick S Daugherty, David J Craik

Abstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Nanomolar inhibition of SARS-CoV-2 infection by an unmodified peptide targeting the prehairpin intermediate of the spike protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  6. Deep mutational analysis reveals functional trade-offs in the sequences of EGFR autophosphorylation sites.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Sónia Troeira HenriquesInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, Australia.
Louise Thorstholm
Yen-Hua Huang
Jennifer A Getz
Patrick S Daugherty
David J Craik

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inhibition of tyrosine kinases is a successful approach for the treatment of cancers and the discovery of kinase inhibitor drugs is the focus of numerous academic and pharmaceutical laboratories. With this goal in mind, several strategies have been developed to measure kinase activity and to screen novel tyrosine kinase inhibitors. Nevertheless, a general non-radioactive and inexpensive approach, easy to implement and adapt to a range of applications, is still missing. Herein, using Bcr-Abl tyrosine kinase, an oncogenic target and a model protein for cancer studies, we describe a novel cost-effective high-throughput screening kinase assay. In this approach, named the BacKin assay, substrates displayed on a Bacterial cell surface are incubated with Kinase and their phosphorylation is examined and quantified by flow cytometry. This approach has several advantages over existing approaches, as using bacteria (i.e. Escherichia coli) to display peptide substrates provides a self renewing solid support that does not require laborious chemical strategies. Here we show that the BacKin approach can be used for kinetic and mechanistic studies, as well as a platform to characterize and identify small-molecule or peptide-based kinase inhibitors with potential applications in drug development.

Indexed as

Cell Surface Display TechniquesFlow CytometryBacteriaEnzyme ActivationEnzyme AssaysFusion Proteins, bcr-ablKineticsModels, MolecularPeptide FragmentsPhosphotransferasesProtein BindingProtein ConformationProtein Kinase InhibitorsProtein-Tyrosine KinasesReproducibility of ResultsSubstrate SpecificityFusion Proteins, bcr-ablPeptide FragmentsPhosphotransferasesProtein Kinase InhibitorsProtein-Tyrosine Kinases

Identifiers

PMID24260399
PMCPMC3829888

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Registered trials

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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.