Evidence map›Paper›PMID 28484215›Full record

ArticleScientific reports2017

Expression proteomics study to determine metallodrug targets and optimal drug combinations.

Ronald F S Lee, Alexey Chernobrovkin, Dorothea Rutishauser, Claire S Allardyce, David Hacker, Kai Johnsson, Roman A Zubarev, Paul J Dyson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.8field-weighted citation impact, top 14% 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, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Dienone Compounds: Targets and Pharmacological Responses.Journal of medicinal chemistry · 2020
    Article
  7. Article
  8. Article
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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

8 authors at 3 institutions in 2 countries.

Ronald F S LeeInstitute of Chemical Sciences and Engineering, Swiss Federal Institute of Technology Lausanne (EPFL), CH-1015, Lausanne, Switzerland.
Alexey ChernobrovkinKarolinska Institute, Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Scheeles väg 2, S-171 77, Stockholm, Sweden.
Dorothea RutishauserKarolinska Institute, Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Scheeles väg 2, S-171 77, Stockholm, Sweden.
Claire S AllardyceInstitute of Chemical Sciences and Engineering, Swiss Federal Institute of Technology Lausanne (EPFL), CH-1015, Lausanne, Switzerland.
David HackerProtein Expression Core Facility, Swiss Federal Institute of Technology Lausanne (EPFL), CH-1015, Lausanne, Switzerland.
Kai JohnssonInstitute of Chemical Sciences and Engineering, Swiss Federal Institute of Technology Lausanne (EPFL), CH-1015, Lausanne, Switzerland.
Roman A ZubarevKarolinska Institute, Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Scheeles väg 2, S-171 77, Stockholm, Sweden.
Paul J DysonInstitute of Chemical Sciences and Engineering, Swiss Federal Institute of Technology Lausanne (EPFL), CH-1015, Lausanne, Switzerland. paul.dyson@epfl.ch.
École Polytechnique Fédérale de Lausanne · CHKarolinska Institutet · SEScience for Life Laboratory · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emerging technique termed functional identification of target by expression proteomics (FITExP) has been shown to identify the key protein targets of anti-cancer drugs. Here, we use this approach to elucidate the proteins involved in the mechanism of action of two ruthenium(II)-based anti-cancer compounds, RAPTA-T and RAPTA-EA in breast cancer cells, revealing significant differences in the proteins upregulated. RAPTA-T causes upregulation of multiple proteins suggesting a broad mechanism of action involving suppression of both metastasis and tumorigenicity. RAPTA-EA bearing a GST inhibiting ethacrynic acid moiety, causes upregulation of mainly oxidative stress related proteins. The approach used in this work could be applied to the prediction of effective drug combinations to test in cancer chemotherapy clinical trials.

Indexed as

Drug DiscoveryDrug InteractionsProteomicsAlgorithmsAntineoplastic AgentsCell Line, TumorChromatography, LiquidDrug CombinationsDrug Screening Assays, AntitumorHumansModels, TheoreticalMolecular StructureOrganometallic CompoundsProteomeRutheniumTandem Mass SpectrometryAntineoplastic AgentsDrug CombinationsOrganometallic CompoundsProteomeRuthenium

Identifiers

PMID28484215
PMCPMC5431558
OpenAlexW2610192203

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.