Evidence map›Paper›PMID 12629207›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

The topoisomerase IIbeta circular clamp arrests transcription and signals a 26S proteasome pathway.

Hai Xiao, Yong Mao, Shyamal D Desai, Nai Zhou, Chun-Yuan Ting, Jaulang Hwang, Leroy F Liu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. 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
1.6field-weighted citation impact, top 17% 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, 99 citations in OpenAlex.

  1. Aclarubicin Reduces the Nuclear Mobility of Human DNA Topoisomerase IIβ.International journal of molecular sciences · 2024
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. SUMO: A Swiss Army Knife for Eukaryotic Topoisomerases.Frontiers in molecular biosciences · 2022
    Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. SCFOncogenesis · 2020
    Article
  19. 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

7 authors at 1 institution in 1 country.

Hai XiaoDepartment of Pharmacology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854-5635, USA.
Yong Mao
Shyamal D Desai
Nai Zhou
Chun-Yuan Ting
Jaulang Hwang
Leroy F Liu
Institute of Molecular Biology, Academia Sinica · TW

Funding

MECHANISMS OF ACTION IN ANTITUMOR DRUGSR01CA039662 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI LIU, LEROY F · 1985 to 2013
$3.8M
FUNCTIONAL AND MECHANISTIC STUDIES OF DNA TOPOISOMERASESR01GM027731 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI LIU, LEROY F · 1985 to 2001
$687k
NCI NIH HHS CA 39662NCI NIH HHS R01 CA039662NIGMS NIH HHS GM 27731
6 · The paper itself

Abstract

It has been proposed that the topoisomerase II (TOP2)beta-DNA covalent complex arrests transcription and triggers 26S proteasome-mediated degradation of TOP2beta. It is unclear whether the initial trigger for proteasomal degradation is due to DNA damage or transcriptional arrest. In the current study we show that the TOP2 catalytic inhibitor 4,4-(2,3-butanediyl)-bis(2,6-piperazinedione) (ICRF-193), which traps TOP2 into a circular clamp rather than the TOP2-DNA covalent complex, can also arrest transcription. Arrest of transcription, which is TOP2beta-dependent, is accompanied by proteasomal degradation of TOP2beta. Different from TOP2 poisons and other DNA-damaging agents, ICRF-193 did not induce proteasomal degradation of the large subunit of RNA polymerase II. These results suggest that proteasomal degradation of TOP2beta induced by the TOP2-DNA covalent complex or the TOP2 circular clamp is due to transcriptional arrest but not DNA damage. By contrast, degradation of the large subunit of RNA polymerase II is due to a DNA-damage signal.

Indexed as

Proteasome Endopeptidase ComplexTopoisomerase II InhibitorsAnimalsApoptosisCell LineDiketopiperazinesDNA-Binding ProteinsDNA DamageDNA RepairDNA Topoisomerases, Type IIDown-RegulationEnzyme InhibitorsHeLa CellsHL-60 CellsHumansMice4,4'-(1,2-dimethyl-1,2-ethanediyl)bis-2,6-piperazinedioneATP dependent 26S proteaseDiketopiperazinesDNA-Binding ProteinsDNA Topoisomerases, Type IIEnzyme InhibitorsPeptide HydrolasesPiperazinesProteasome Endopeptidase ComplexTeniposideTopoisomerase II InhibitorsTumor Suppressor Protein p53

Identifiers

PMID12629207
PMCPMC152276
OpenAlexW2119861722

What OpenQuestion holds

Textmetadata
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.