Evidence map›Paper›PMID 29363591›Full record

ReviewThe Biochemical journal2018

Topoisomerases as anticancer targets.

Justine L Delgado, Chao-Ming Hsieh, Nei-Li Chan, Hiroshi Hiasa

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 224 papers.

0numbers the graph read from it
0cells of the map it votes in
224citing papers in PubMed
16.8field-weighted citation impact, top 1% 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

224 citing papers in PubMed, 459 citations in OpenAlex.

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164 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

4 authors at 1 institution in 1 country.

Justine L DelgadoDivision of Medicinal and Natural Products Chemistry, Department of Pharmaceutical Sciences and Experimental Therapeutics, College of Pharmacy, University of Iowa, 115 S Grand Ave., S321 Pharmacy Building, Iowa City, IA 52242, U.S.A.
Chao-Ming HsiehInstitute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei City 100, Taiwan.
Nei-Li ChanInstitute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei City 100, Taiwan.
Hiroshi HiasaDepartment of Pharmacology, University of Minnesota Medical School, 6-120 Jackson Hall, 321 Church Street SE, Minneapolis, MN 55455, U.S.A. hiasa001@umn.edu.
National Taiwan University · TW

Funding

PREDOCTORAL TRAINING PROGRAM IN BIOTECHNOLOGYT32GM008365 · NIGMS · UNIVERSITY OF IOWA · PI KERNS, ROBERT JOHN · 1990 to 2021
$3.8M
Antibacterial Agents that Restrict the Emergence of ResistanceR01AI087671 · NIAID · UNIVERSITY OF IOWA · PI KERNS, ROBERT JOHN · 2010 to 2014
$1.9M
NIAID NIH HHS R01 AI087671NIGMS NIH HHS T32 GM008365
6 · The paper itself

Abstract

Many cancer type-specific anticancer agents have been developed and significant advances have been made toward precision medicine in cancer treatment. However, traditional or nonspecific anticancer drugs are still important for the treatment of many cancer patients whose cancers either do not respond to or have developed resistance to cancer-specific anticancer agents. DNA topoisomerases, especially type IIA topoisomerases, are proved therapeutic targets of anticancer and antibacterial drugs. Clinically successful topoisomerase-targeting anticancer drugs act through topoisomerase poisoning, which leads to replication fork arrest and double-strand break formation. Unfortunately, this unique mode of action is associated with the development of secondary cancers and cardiotoxicity. Structures of topoisomerase-drug-DNA ternary complexes have revealed the exact binding sites and mechanisms of topoisomerase poisons. Recent advances in the field have suggested a possibility of designing isoform-specific human topoisomerase II poisons, which may be developed as safer anticancer drugs. It may also be possible to design catalytic inhibitors of topoisomerases by targeting certain inactive conformations of these enzymes. Furthermore, identification of various new bacterial topoisomerase inhibitors and regulatory proteins may inspire the discovery of novel human topoisomerase inhibitors. Thus, topoisomerases remain as important therapeutic targets of anticancer agents.

Indexed as

Anti-Bacterial AgentsAntineoplastic AgentsCatalytic DomainDNADNA Breaks, Double-StrandedDNA, NeoplasmDNA Topoisomerases, Type IIDrug DesignGene ExpressionHumansMolecular Docking SimulationMolecular Targeted TherapyNeoplasmsProtein Structure, SecondaryStructure-Activity RelationshipTopoisomerase InhibitorsAnti-Bacterial AgentsAntineoplastic AgentsDNADNA, NeoplasmDNA Topoisomerases, Type IITopoisomerase Inhibitorsanticancer agentschemotherapytopoisomerase Itopoisomerase IItopoisomerase inhibitorstopoisomerase poisoning

Identifiers

PMID29363591
PMCPMC6110615
OpenAlexW2784709079

What OpenQuestion holds

Textmetadata
LicenceTDM
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.