Evidence map›Paper›PMID 31411364›Full record

ArticleAngewandte Chemie (International ed. in English)2019

A Fluorescent Kinase Inhibitor that Exhibits Diagnostic Changes in Emission upon Binding.

Cassandra L Fleming, Patrick A Sandoz, Tord Inghardt, Björn Önfelt, Morten Grøtli, Joakim Andréasson

Open access · bronzeAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. 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
1.6field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
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  6. Article
  7. New insights into the Lck-NF-κB signaling pathway.Frontiers in cell and developmental biology · 2023
    Review
  8. Review
  9. Review
  10. Towards Photochromic Azobenzene-Based Inhibitors for Tryptophan Synthase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    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 at 4 institutions in 2 countries.

Cassandra L FlemingDepartment of Chemistry and Chemical Engineering, Physical Chemistry, Chalmers University of Technology, 41296, Göteborg, Sweden.ORCID 0000-0002-7730-7305
Patrick A SandozDepartment of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, 10691, Stockholm, Sweden.ORCID 0000-0002-8379-7267
Tord InghardtMedicinal Chemistry, Research and Early Development Cardiovascular, Renal and Metabolism, BioPharmaceuticals R&D, AstraZeneca, Gothenburg, Sweden.ORCID 0000-0002-4804-9474
Björn ÖnfeltDepartment of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, 10691, Stockholm, Sweden.ORCID 0000-0001-5178-7593
Morten GrøtliDepartment of Chemistry and Molecular Biology, University of Gothenburg, 41296, Göteborg, Sweden.ORCID 0000-0003-3621-4222
Joakim AndréassonDepartment of Chemistry and Chemical Engineering, Physical Chemistry, Chalmers University of Technology, 41296, Göteborg, Sweden.ORCID 0000-0003-4695-7943
Chalmers University of Technology · SEScience for Life Laboratory · SEAstraZeneca (Finland) · FIUniversity of Gothenburg · SE

Funding

Horizon 2020 Framework Programme 745626Olle Engkvist Byggmästare FoundationVetenskapsrådet 2015-05268Vetenskapsrådet 2016-03601
6 · The paper itself

Abstract

The development of a fluorescent LCK inhibitor that exhibits favourable solvatochromic properties upon binding the kinase is described. Fluorescent properties were realised through the inclusion of a prodan-derived fluorophore into the pharmacophore of an ATP-competitive kinase inhibitor. Fluorescence titration experiments demonstrate the solvatochromic properties of the inhibitor, in which dramatic increase in emission intensity and hypsochromic shift in emission maxima are clearly observed upon binding LCK. Microscopy experiments in cellular contexts together with flow cytometry show that the fluorescence intensity of the inhibitor correlates with the LCK concentration. Furthermore, multiphoton microscopy experiments demonstrate both the rapid cellular uptake of the inhibitor and that the two-photon cross section of the inhibitor is amenable for excitation at 700 nm.

Indexed as

2-NaphthylamineAdenosine TriphosphateBinding, CompetitiveFlow CytometryFluorescent DyesHumansJurkat CellsLymphocyte Specific Protein Tyrosine Kinase p56(lck)Microscopy, Fluorescence, MultiphotonMolecular StructureProtein BindingProtein Kinase Inhibitors2-NaphthylamineAdenosine TriphosphateFluorescent DyesLCK protein, humanLymphocyte Specific Protein Tyrosine Kinase p56(lck)prodanProtein Kinase Inhibitorsfluorescenceinhibitorskinasesolvatochromism

Identifiers

PMID31411364
PMCPMC6851755
OpenAlexW2967620211

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.