Evidence map›Paper›PMID 34008964›Full record

ReviewBiochemistry2021

Topoisomerase II Poisons: Converting Essential Enzymes into Molecular Scissors.

Kendra R Vann, Alexandria A Oviatt, Neil Osheroff

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.4field-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

50 citing papers in PubMed, 92 citations in OpenAlex.

  1. A multispecies toolkit ofProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Structural Mechanisms of Topoisomerase-Targeting Drugs.Annual review of biochemistry · 2025
    Review
  12. Article
  13. Article
  14. DNA Cleavage Mediated by Bacterial Type II Topoisomerases.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  15. DNA Supercoiling Catalyzed by Bacterial Gyrase.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  16. DNA Decatenation Catalyzed by Bacterial Topoisomerase IV.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  17. Review
  18. Article
  19. Small Molecule Inhibitors ofInternational journal of molecular sciences · 2024
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

Kendra R VannDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.
Alexandria A OviattDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.
Neil OsheroffDepartments of Biochemistry and Medicine (Hematology/Oncology), Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.ORCID 0000-0002-2550-4884
Vanderbilt University · US

Funding

Vanderbilt/Meharry Initiative for Minority Student DvptR25GM062459 · NIGMS · VANDERBILT UNIVERSITY · PI VELEZ EDWARDS, DIGNA R · 2002 to 2020
$10.4M
BIOCHEMICAL &CHEMICAL TRAINING FOR CANCER RESEARCHT32CA009582 · NCI · VANDERBILT UNIVERSITY · PI David K Cortez · 1987 to 2026
$8.8M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
FUNCTION AND BIOLOGY OF EUKARYOTIC DNA TOPOISOMERASESR01GM033944 · NIGMS · VANDERBILT UNIVERSITY · PI OSHEROFF, NEIL · 1985 to 2015
$5.5M
Mechanistic Studies of Type II Topoisomerases and Topoisomerase-Targeted AgentsR01GM126363 · NIGMS · VANDERBILT UNIVERSITY · PI OSHEROFF, NEIL · 2018 to 2025
$2.6M
Overcoming fluoroquinolone resistance in Neisseria gonorrhoeaeF31AI149863 · NIAID · VANDERBILT UNIVERSITY · PI OVIATT, ALEXANDRIA · 2020 to 2021
$58k
Mechanism of Quinolone ResistanceI01BX002198 · VA · VETERANS HEALTH ADMINISTRATION · PI OSHEROFF, NEIL · 2015 to 2023
–
BLRD VA I01 BX002198NCI NIH HHS T32 CA009582NIAID NIH HHS F31 AI149863NIGMS NIH HHS R01 GM033944NIGMS NIH HHS R01 GM126363NIGMS NIH HHS R25 GM062459NIGMS NIH HHS T32 GM008320
6 · The paper itself

Abstract

The extensive length, compaction, and interwound nature of DNA, together with its controlled and restricted movement in eukaryotic cells, create a number of topological issues that profoundly affect all of the functions of the genetic material. Topoisomerases are essential enzymes that modulate the topological structure of the double helix, including the regulation of DNA under- and overwinding and the removal of tangles and knots from the genome. Type II topoisomerases alter DNA topology by generating a transient double-stranded break in one DNA segment and allowing another segment to pass through the DNA gate. These enzymes are involved in a number of critical nuclear processes in eukaryotic cells, such as DNA replication, transcription, and recombination, and are required for proper chromosome structure and segregation. However, because type II topoisomerases generate double-stranded breaks in the genetic material, they also are intrinsically dangerous enzymes that have the capacity to fragment the genome. As a result of this dualistic nature, type II topoisomerases are the targets for a number of widely prescribed anticancer drugs. This article will describe the structure and catalytic mechanism of eukaryotic type II topoisomerases and will go on to discuss the actions of topoisomerase II poisons, which are compounds that stabilize DNA breaks generated by the type II enzyme and convert these essential enzymes into "molecular scissors." Topoisomerase II poisons represent a broad range of structural classes and include anticancer drugs, dietary components, and environmental chemicals.

Indexed as

Antineoplastic AgentsDNADNA DamageDNA Topoisomerases, Type IIEukaryotaGenomeHumansTopoisomerase II InhibitorsTranslocation, GeneticAntineoplastic AgentsDNADNA Topoisomerases, Type IITopoisomerase II Inhibitors

Identifiers

PMID34008964
PMCPMC8209676
OpenAlexW3163016702

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.