Evidence map›Paper›PMID 30658435›Full record

ArticleInternational journal of molecular sciences2019

Oxazole-Bridged Combretastatin A-4 Derivatives with Tethered Hydroxamic Acids: Structure⁻Activity Relations of New Inhibitors of HDAC and/or Tubulin Function.

Florian Schmitt, Lisa Chiara Gosch, Alexandra Dittmer, Matthias Rothemund, Thomas Mueller, Rainer Schobert, Bernhard Biersack, Andrea Volkamer, Michael Höpfner

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. 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
1.7field-weighted citation impact, top 16% 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, 30 citations in OpenAlex.

  1. O-methylation of phenolic natural products: translational insights from resveratrol.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
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  9. HybridInternational journal of molecular sciences · 2019
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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

9 authors at 3 institutions in 1 country.

Florian SchmittDepartment of Chemistry, University of Bayreuth, Universitaetsstrasse 30, 95447 Bayreuth, Germany. florian1.schmitt@uni-bayreuth.de.
Lisa Chiara GoschInstitute of Physiology, Charité⁻Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. lisa-chiara.gosch@charite.de.
Alexandra DittmerInstitute of Physiology, Charité⁻Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. alexandra.dittmer@charite.de.
Matthias RothemundDepartment of Chemistry, University of Bayreuth, Universitaetsstrasse 30, 95447 Bayreuth, Germany. matthias.rothemund@uni-bayreuth.de.ORCID 0000-0003-0199-9621
Thomas MuellerInternal Medicine IV, University Hospital Halle (Saale), Ernst-Grube-Str. 40, 06120 Halle, Germany. thomas.mueller@medizin.uni-halle.de.
Rainer SchobertDepartment of Chemistry, University of Bayreuth, Universitaetsstrasse 30, 95447 Bayreuth, Germany. rainer.schobert@uni-bayreuth.de.
Bernhard BiersackDepartment of Chemistry, University of Bayreuth, Universitaetsstrasse 30, 95447 Bayreuth, Germany. bernhard.biersack@yahoo.com.
Andrea VolkamerIn Silico Toxicology Group, Institute of Physiology, Charité⁻Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. andrea.volkamer@charite.de.ORCID 0000-0002-3760-580X
Michael HöpfnerInstitute of Physiology, Charité⁻Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. michael.hoepfner@charite.de.
Charité - Universitätsmedizin Berlin · DEUniversity of Bayreuth · DEUniversity Hospital in Halle · DE

Funding

Bundesministerium für Bildung und Forschung 031A262CDeutsche Forschungsgemeinschaft Scho 402/12-1Else-Kroener Fresenius Stiftung 2016-A47
6 · The paper itself

Abstract

New inhibitors of tubulin polymerization and/or histone deacetylase (HDAC) activity were synthesized by attaching alkyl tethered hydroxamic acid appendages of varying length to oxazole-bridged combretastatin A-4 analogous caps. While their antiproliferative and microtubule disrupting effect was most pronounced for derivatives with short spacers, HDAC inhibition was strongest for those with longer spacers. These findings were further supported by computational methods such as structure-based docking experiments exploring the target interactions of the derivatives with varying linkers. For instance, compounds featuring short four-atom spacers between cap and hydroxamic acid inhibited the growth of various cancer cell lines and human endothelial hybrid cells with IC

Indexed as

Antineoplastic AgentsBibenzylsBinding SitesCell CycleCell Line, TumorCell ProliferationDose-Response Relationship, DrugFluorescent Antibody TechniqueHistone Deacetylase InhibitorsHumansHydrogen BondingHydroxamic AcidsInhibitory Concentration 50MicrotubulesModels, MolecularMolecular ConformationAntineoplastic AgentsBibenzylscombretastatinHistone Deacetylase InhibitorsHydroxamic AcidsOxazolesTubulinTubulin Modulatorsanticancer agentscombretastatin A-4histone deacetylaseoxazoletubulin

Identifiers

PMID30658435
PMCPMC6359144
OpenAlexW2910337821

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.