Evidence map›Paper›PMID 21880767›Full record

ArticleJournal of virology2011

Mechanism of glycyrrhizic acid inhibition of Kaposi's sarcoma-associated herpesvirus: disruption of CTCF-cohesin-mediated RNA polymerase II pausing and sister chromatid cohesion.

Hyojeung Kang, Paul M Lieberman

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
6.4field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Review
  8. Article
  9. Regulation ofiScience · 2022
    Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Cohesin Mutations in Cancer: Emerging Therapeutic Targets.International journal of molecular sciences · 2021
    Review
  15. Article
  16. Review
  17. Review
  18. 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

2 authors at 2 institutions in 2 countries.

Hyojeung KangThe Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104-4268, USA.
Paul M Lieberman
Kyungpook National University · KRThe Wistar Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
Regulation of KSHV LatencyR01CA117830 · NCI · WISTAR INSTITUTE · PI PAUL M. LIEBERMAN · 2006 to 2026
$6.4M
NCI NIH HHS P30 CA010815NCI NIH HHS P30 CA10815NCI NIH HHS R01 CA117830NCI NIH HHS T32 CA009171NCI NIH HHS T32: CA09171-31
6 · The paper itself

Abstract

Glycyrrhizic acid (GA), a derivative of licorice, selectively inhibits the growth of lymphocytes latently infected with Kaposi's sarcoma-associated herpesvirus. The mechanism involves the deregulation of the multicistronic latency transcript, including the failure to generate the mature forms of viral mRNA encoding LANA. We show here that GA disrupts an RNA polymerase II (RNAPII) complex that accumulates at the CTCF-cohesin binding site within the first intron of the latency transcript. GA altered the enrichment of the RNAPII pausing complex, along with pausing factors SPT5 and NELF-A, at the intragenic CTCF-cohesin binding sites. GA blocked the interaction of cohesin subunit SMC3 with another cohesin subunit, RAD21, and reduced SPT5 interaction with RNAPII. Covalent coupling of GA to a solid support revealed that GA interacts with several cellular proteins, including SMC3 and SPT5, but not their respective interaction partners RAD21 and RNAPII. GA treatment also inhibited the transcription of some cellular genes, like c-myc, which contain a similar CTCF-cohesin binding site within the first intron. We also found that GA leads to a more general loss of sister chromatid cohesion for cellular chromosomes. These findings suggest that RNAPII pauses at intragenic CTCF-cohesin binding sites and that abrogation of this pausing by GA leads to loss of proper mRNA production and defects in sister chromatid cohesion, a process important for both viral and cellular chromosome stability.

Indexed as

Antiviral AgentsCCCTC-Binding FactorCell Cycle ProteinsCell LineChromatidsChromosomal Proteins, Non-HistoneCohesinsGlycyrrhizic AcidHerpesvirus 8, HumanHumansNuclear ProteinsProtein BindingRepressor ProteinsRNA Polymerase IITranscriptional Elongation FactorsTranscription FactorsAntiviral AgentsCCCTC-Binding FactorCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsCTCF protein, humanGlycyrrhizic AcidNSMF protein, humanNuclear ProteinsRepressor ProteinsRNA Polymerase IISUPT5H protein, humanTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID21880767
PMCPMC3194953
OpenAlexW2058811737

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.