Evidence map›Paper›PMID 32245944›Full record

ArticleNature communications2020

Kinase inhibition profiles as a tool to identify kinases for specific phosphorylation sites.

Nikolaus A Watson, Tyrell N Cartwright, Conor Lawless, Marcos Cámara-Donoso, Onur Sen, Kosuke Sako, Toru Hirota, Hiroshi Kimura, Jonathan M G Higgins

Open access · goldAbstract readValidation Study
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Phytochemical study ofPharmaceutical biology · 2026
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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

9 authors at 4 institutions in 2 countries.

Nikolaus A WatsonBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.ORCID http://orcid.org/0000-0001-6459-722X
Tyrell N CartwrightBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.ORCID http://orcid.org/0000-0001-9406-9030
Conor LawlessWellcome Centre for Mitochondrial Research, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.ORCID http://orcid.org/0000-0002-4186-8506
Marcos Cámara-DonosoBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Onur SenBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.ORCID http://orcid.org/0000-0002-6685-7010
Kosuke SakoThe Cancer Institute, Japanese Foundation for Cancer Research, Koto, Tokyo, 135-8550, Japan.ORCID http://orcid.org/0000-0002-3874-2072
Toru HirotaThe Cancer Institute, Japanese Foundation for Cancer Research, Koto, Tokyo, 135-8550, Japan.
Hiroshi KimuraCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Kanagawa, 226-8503, Japan.ORCID http://orcid.org/0000-0003-0854-083X
Jonathan M G HigginsBiosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK. jonathan.higgins@newcastle.ac.uk.ORCID http://orcid.org/0000-0001-6622-8268
Newcastle University · GBJapanese Foundation For Cancer Research · JPTokyo Institute of Technology · JPWellcome Centre for Mitochondrial Research · GB

Funding

Medical Research Council MC_PC_17198Wellcome Trust
6 · The paper itself

Abstract

There are thousands of known cellular phosphorylation sites, but the paucity of ways to identify kinases for particular phosphorylation events remains a major roadblock for understanding kinase signaling. To address this, we here develop a generally applicable method that exploits the large number of kinase inhibitors that have been profiled on near-kinome-wide panels of protein kinases. The inhibition profile for each kinase provides a fingerprint that allows identification of unknown kinases acting on target phosphosites in cell extracts. We validate the method on diverse known kinase-phosphosite pairs, including histone kinases, EGFR autophosphorylation, and Integrin β1 phosphorylation by Src-family kinases. We also use our approach to identify the previously unknown kinases responsible for phosphorylation of INCENP at a site within a commonly phosphorylated motif in mitosis (a non-canonical target of Cyclin B-Cdk1), and of BCL9L at S915 (PKA). We show that the method has clear advantages over in silico and genetic screening.

Indexed as

Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsEnzyme AssaysGenetic TestingHeLa CellsHigh-Throughput Screening AssaysHumansMitosisPhosphorylationProtein Kinase InhibitorsProtein KinasesRecombinant ProteinsTranscription FactorsBCL9L protein, humanChromosomal Proteins, Non-HistoneDNA-Binding ProteinsINCENP protein, humanProtein Kinase InhibitorsProtein KinasesRecombinant ProteinsTranscription Factors

Identifiers

PMID32245944
PMCPMC7125195
OpenAlexW3014968587

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.