Evidence map›Paper›PMID 32027084›Full record

ArticleIUBMB life2020

KinCon: Cell-based recording of full-length kinase conformations.

Florian Enzler, Philipp Tschaikner, Rainer Schneider, Eduard Stefan

Open access · hybridAbstract read
In one paragraph

Article in IUBMB life, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mutation-oriented profiling of autoinhibitory kinase conformations predicts RAF inhibitor efficacies.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. 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

4 authors at 1 institution in 1 country.

Florian EnzlerInstitute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, Innsbruck, Austria.ORCID 0000-0003-3891-5831
Philipp TschaiknerInstitute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, Innsbruck, Austria.
Rainer SchneiderInstitute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, Innsbruck, Austria.
Eduard StefanInstitute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, Innsbruck, Austria.ORCID 0000-0003-3650-4713
Universität Innsbruck · AT

Funding

Austrian Science Fund FWF P 30441
6 · The paper itself

Abstract

The spectrum of kinase alterations displays distinct functional characteristics and requires kinase mutation-oriented strategies for therapeutic interference. Besides phosphotransferase activity, protein abundance, and intermolecular interactions, particular patient-mutations promote pathological kinase conformations. Despite major advances in identifying lead molecules targeting clinically relevant oncokinase functions, still many kinases are neglected and not part of drug discovery efforts. One explanation is attributed to challenges in tracking kinase activities. Chemical probes are needed to functionally annotate kinase functions, whose activities may not always depend on catalyzing phospho-transfer. Such non-catalytic kinase functions are related to transitions of full-length kinase conformations. Recent findings underline that cell-based reporter systems can be adapted to record conformation changes of kinases. Here, we discuss the possible applications of an extendable kinase conformation (KinCon) reporter toolbox for live-cell recording of kinase states. KinCon is a genetically encoded bioluminescence-based biosensor platform, which can be subjected for measurements of conformation dynamics of mutated kinases upon small molecule inhibitor exposure. We hypothesize that such biosensors can be utilized to delineate the molecular modus operandi for kinase and pseudokinase regulation. This should pave the path for full-length kinase-targeted drug discovery efforts aiming to identify single and combinatory kinase inhibitor therapies with increased specificity and efficacy.

Indexed as

Biosensing TechniquesGenes, ReporterHumansLuciferasesLuminescent MeasurementsMolecular BiologyProtein ConformationProtein KinasesLuciferasesProtein Kinasesallosteric inhibitorAMPKbiosensorBRAFCRAFdrug side effectkinase conformationskinase dimerkinase drug efficaciesKSRLKB1MAPKMEKmolecular interactiononcokinasePKApseudoenzymepseudokinaseRAFRASscaffolding functionSTRADαundruggable

Identifiers

PMID32027084
PMCPMC7318358
OpenAlexW3004984160

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.