Evidence map›Paper›PMID 29642594›Full record

ArticleInternational journal of molecular sciences2018

Allosteric Activation of GDP-Bound Ras Isoforms by Bisphenol Derivative Plasticisers.

Miriam Schöpel, Oleksandr Shkura, Jana Seidel, Klaus Kock, Xueyin Zhong, Stefanie Löffek, Iris Helfrich, Hagen S Bachmann, Jürgen Scherkenbeck, Christian Herrmann and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Targeting the "undruggable" RAS - new strategies - new hope?Cancer drug resistance (Alhambra, Calif.) · 2019
    Review
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

11 authors at 6 institutions in 1 country.

Miriam SchöpelFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. miriam.schoepel@rub.de.
Oleksandr ShkuraFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. Oleksandr.Shkura@ruhr-uni-bochum.de.
Jana SeidelFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. jana.seidel@rub.de.
Klaus KockFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. Klaus.Kock@ruhr-uni-bochum.de.
Xueyin ZhongFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. xueyin.zhong@rub.de.
Stefanie LöffekSkin Cancer Unit of the Dermatology Department, West German Cancer Center, University Hospital Essen, University Duisburg-Essen and the German Cancer Consortium (DKTK), D-45147 Essen, Germany. Stefanie.Loeffek@uk-essen.de.
Iris HelfrichSkin Cancer Unit of the Dermatology Department, West German Cancer Center, University Hospital Essen, University Duisburg-Essen and the German Cancer Consortium (DKTK), D-45147 Essen, Germany. Iris.Helfrich@uk-essen.de.
Hagen S BachmannInstitute of Pharmacology and Toxicology, Witten/Herdecke University, Stockumer Str. 10, D-58453 Witten, Germany. hagen.bachmann@uni-wh.de.
Jürgen ScherkenbeckFaculty of Mathematics and Natural Sciences, University of Wuppertal, Gaußstr. 20, D-42119 Wuppertal, Germany. Scherkenbeck@uni-wuppertal.de.
Christian HerrmannFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. chr.herrmann@rub.de.ORCID 0000-0002-1824-3647
Raphael StollFaculty of Chemistry and Biochemistry, Ruhr University of Bochum, Universitätsstr. 150, D-44780 Bochum, Germany. raphael.stoll@ruhr-uni-bochum.de.
University Hospitals of the Ruhr-University of Bochum · DERuhr University Bochum · DEEssen University Hospital · DEUniversity of Wuppertal · DEWest German Heart and Vascular Center Essen · DEWitten/Herdecke University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein family of small GTPases controls cellular processes by acting as a binary switch between an active and an inactive state. The most prominent family members are H-Ras, N-Ras, and K-Ras isoforms, which are highly related and frequently mutated in cancer. Bisphenols are widespread in modern life because of their industrial application as plasticisers. Bisphenol A (BPA) is the best-known member and has gained significant scientific as well as public attention as an endocrine disrupting chemical, a fact that eventually led to its replacement. However, compounds used to replace BPA still contain the molecular scaffold of bisphenols. BPA, BPAF, BPB, BPE, BPF, and an amine-substituted BPAF-derivate all interact with all GDP-bound Ras-Isoforms through binding to a common site on these proteins. NMR-, SOS

Indexed as

Allosteric SiteAllosteric RegulationBenzhydryl CompoundsBisphenol A CompoundsEndocrine DisruptorsGuanosine DiphosphateHeLa CellsHumansPhenolsProtein Bindingras ProteinsBenzhydryl Compoundsbisphenol ABisphenol A CompoundsEndocrine DisruptorsGuanosine DiphosphatePhenolsras Proteinsactive conformation/allosteric agonistsbisphenolsK-Ras4BNMR spectroscopyRap-1A

Identifiers

PMID29642594
PMCPMC5979466
OpenAlexW2796470381

What OpenQuestion holds

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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.