Evidence map›Paper›PMID 20362353›Full record

ArticleEuropean journal of cell biology2010

The arylstibonic acid compound NSC13746 disrupts B-ZIP binding to DNA in living cells.

Sarah L Heyerdahl, Julian Rozenberg, Louis Jamtgaard, Vikas Rishi, Lyuba Varticovski, Kelly Akah, Dominic Scudiero, Robert H Shoemaker, Tatiana S Karpova, Richard N Day and 2 more

Open access · greenAbstract read
In one paragraph

Article in European journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Ubiquitin tagged dominant negative induces degradation of B-ZIP proteins.Biochemical and biophysical research communications · 2012
    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

12 authors at 5 institutions in 1 country.

Sarah L HeyerdahlLaboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Julian Rozenberg
Louis Jamtgaard
Vikas Rishi
Lyuba Varticovski
Kelly Akah
Dominic Scudiero
Robert H Shoemaker
Tatiana S Karpova
Richard N Day
James G McNally
Charles Vinson
National Institutes of Health · USNational Cancer Institute · USScience Applications International Corporation (United States) · USUnited States Department of Health and Human Services · USUniversity of Virginia · US

Funding

Gene Regulation and Function: The B-ZIP ProteinsZIABC005271 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI VINSON, CHARLES · 2009 to 2019
$11.2M
Transcription factor mobilityZIABC010561 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MCNALLY, JAMES G · 2009 to 2013
$3.9M
GENE REGULATION AND FUNCTION: THE B-ZIP PROTEINSZ01BC005271 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI VINSON, CHARLES · 1996 to 2008
$2.0M
Fluorescence Imaging FacilityZICBC010571 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MCNALLY, JAMES G · 2009 to 2013
$1.3M
Intramural NIH HHS Z01 BC005271NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

The inhibition of DNA binding of basic leucine zipper (B-ZIP) transcription factors is a clinically relevant molecular target. Our laboratory has previously reported two methods of inhibiting B-ZIP DNA binding in solution: 1) an arylstibonic acid compound that binds to the basic region, stabilizes the B-ZIP dimer, and prevents B-ZIP DNA binding and 2) dominant negative proteins, termed A-ZIPs, that heterodimerize with B-ZIP domains in a leucine zipper-dependent manner. To determine if these two agents also inhibit DNA binding in live cells, GFP-tagged B-ZIP domains and mCherry-tagged A-ZIP domains were transfected into NIH3T3 cells to assess protein localization and Fluorescence Recovery After nuclear Photobleaching (FRAP). FRAP, showed that all six GFP-B-ZIP domains examined recovered faster in the nucleus in the presence of drug that we interpret represents an inhibition of DNA binding. Faster recovery in the presence of the A-ZIP was leucine zipper dependent. The arylstibonic also induced a cytoplasmic localization of all B-ZIP domains while the A-ZIPs induced a leucine zipper-dependent cytoplasmic localization. Thus, the change in cellular localization of B-ZIP domains could be used as a high-throughput assay for inhibitors of B-ZIP DNA binding. Additionally, the arylstibonic acid compound was cytostatic in clear cell sarcoma cells, which express a chimera between the B-ZIP domain of ATF-1 and N-terminal activation domain of EWS but not in K562 cells that express a non-B-ZIP containing chimeric protein BCR-ABL. These studies suggest that arylstibonic acid compounds or other small molecules capable of inhibiting B-ZIP DNA binding could be valuable anticancer agents.

Indexed as

AnimalsAntineoplastic AgentsBenzenesulfonatesCell Line, TumorChromatin ImmunoprecipitationDNAFluorescence Recovery After PhotobleachingFluorescence Resonance Energy TransferHumansLeucine ZippersMiceNIH 3T3 CellsOrganometallic CompoundsProtein BindingProtein MultimerizationTranscription FactorsAntineoplastic AgentsBenzenesulfonatesDNANSC 13746Organometallic CompoundsTranscription Factors

Identifiers

PMID20362353
PMCPMC7316388
OpenAlexW1983287135

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.