Evidence map›Paper›PMID 29168755›Full record

ReviewMolecules (Basel, Switzerland)2017

Regulation of G2/M Transition by Inhibition of WEE1 and PKMYT1 Kinases.

Matthias Schmidt, Alexander Rohe, Charlott Platzer, Abdulkarim Najjar, Frank Erdmann, Wolfgang Sippl

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed, 2 pooled it
5.3field-weighted citation impact, top 3% 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

122 citing papers in PubMed, 2 syntheses or guidelines pooled it, 196 citations in OpenAlex.

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  5. 7-azaindole as privileged scaffold: Advances in drug design and structural modification.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
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62 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Matthias SchmidtInstitute of Pharmacy, Martin-Luther-University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany. matthias.schmidt@pharmazie.uni-halle.de.
Alexander RoheInstitute of Pharmacy, Martin-Luther-University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany. alexander.rohe@pharmazie.uni-halle.de.
Charlott PlatzerInstitute of Pharmacy, Martin-Luther-University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany. charlott.platzer@pharmazie.uni-halle.de.
Abdulkarim NajjarInstitute of Pharmacy, Martin-Luther-University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany. a.k.najjar@hotmail.com.ORCID 0000-0003-4620-9830
Frank ErdmannInstitute of Pharmacy, Martin-Luther-University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany. frank.erdmann@pharmazie.uni-halle.de.
Wolfgang SipplInstitute of Pharmacy, Martin-Luther-University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120 Halle (Saale), Germany. wolfgang.sippl@pharmazie.uni-halle.de.
Martin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the cell cycle, there are two checkpoint arrests that allow cells to repair damaged DNA in order to maintain genomic integrity. Many cancer cells have defective G1 checkpoint mechanisms, thus depending on the G2 checkpoint far more than normal cells. G2 checkpoint abrogation is therefore a promising concept to preferably damage cancerous cells over normal cells. The main factor influencing the decision to enter mitosis is a complex composed of Cdk1 and cyclin B. Cdk1/CycB is regulated by various feedback mechanisms, in particular inhibitory phosphorylations at Thr14 and Tyr15 of Cdk1. In fact, Cdk1/CycB activity is restricted by the balance between WEE family kinases and Cdc25 phosphatases. The WEE kinase family consists of three proteins: WEE1, PKMYT1, and the less important WEE1B. WEE1 exclusively mediates phosphorylation at Tyr15, whereas PKMYT1 is dual-specific for Tyr15 as well as Thr14. Inhibition by a small molecule inhibitor is therefore proposed to be a promising option since WEE kinases bind Cdk1, altering equilibria and thus affecting G2/M transition.

Indexed as

G2 Phase Cell Cycle CheckpointsAnimalsAntineoplastic AgentsCell Cycle ProteinsEnzyme ActivationHumansMembrane ProteinsMolecular Targeted TherapyMultigene FamilyNeoplasmsNuclear ProteinsProtein Kinase InhibitorsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesStructure-Activity RelationshipAntineoplastic AgentsCell Cycle ProteinsMembrane ProteinsNuclear ProteinsPKMYT1 protein, humanProtein Kinase InhibitorsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesWEE1 protein, humanG2/M transitionPKMYT1WEE1

Identifiers

PMID29168755
PMCPMC6149964
OpenAlexW2770634084

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.