Evidence map›Paper›PMID 19297618›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Inhibition of Myc-induced cell transformation by brain acid-soluble protein 1 (BASP1).

Markus Hartl, Andrea Nist, M Imran Khan, Taras Valovka, Klaus Bister

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

65 citing papers in PubMed, 93 citations in OpenAlex.

  1. Reactivation of the silencedProceedings of the National Academy of Sciences of the United States of America · 2026
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  4. Advances in RNA Labeling with Trifluoromethyl Groups.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  5. Article
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  7. Review
  8. Article
  9. Article
  10. A high-affinity cocaine binding site associated with the brain acid soluble protein 1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Cholesterol is required for transcriptional repression by BASP1.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Identification of Basp1 as a novel angiogenesis-regulating gene by multi-model system studies.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  14. MYC Analysis in Cancer and Evolution.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
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  19. Review
  20. Article

5 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

5 authors at 2 institutions in 2 countries.

Markus HartlInstitute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, A-6020 Innsbruck, Austria. markus.hartl@uibk.ac.at
Andrea Nist
M Imran Khan
Taras Valovka
Klaus Bister
Universität Innsbruck · ATScripps Research Institute · US

Funding

Austrian Science Fund FWF P 17041Austrian Science Fund FWF P 18148
6 · The paper itself

Abstract

Cell transformation by the Myc oncoprotein involves transcriptional activation or suppression of specific target genes with intrinsic oncogenic or tumor-suppressive potential, respectively. We have identified the BASP1 (CAP-23, NAP-22) gene as a novel target suppressed by Myc. The acidic 25-kDa BASP1 protein was originally isolated as a cortical cytoskeleton-associated protein from rat and chicken brain, but has also been found in other tissues and subcellular locations. BASP1 mRNA and protein expression is specifically suppressed in fibroblasts transformed by the v-myc oncogene, but not in cells transformed by other oncogenic agents. The BASP1 gene encompasses 2 exons separated by a 58-kbp intron and a Myc-responsive regulatory region at the 5' boundary of untranslated exon 1. Bicistronic expression of BASP1 and v-myc from a retroviral vector blocks v-myc-induced cell transformation. Furthermore, ectopic expression of BASP1 renders fibroblasts resistant to subsequent cell transformation by v-myc, and exogenous delivery of the BASP1 gene into v-myc-transformed cells leads to significant attenuation of the transformed phenotype. The inhibition of v-myc-induced cell transformation by BASP1 also prevents the transcriptional activation or repression of known Myc target genes. Mutational analysis showed that the basic N-terminal domain containing a myristoylation site, a calmodulin binding domain, and a putative nuclear localization signal is essential for the inhibitory function of BASP1. Our results suggest that down-regulation of the BASP1 gene is a necessary event in myc-induced oncogenesis and define the BASP1 protein as a potential tumor suppressor.

Indexed as

Cell Transformation, NeoplasticAnimalsBinding SitesCalmodulinCalmodulin-Binding ProteinsChickensGene Expression Regulation, NeoplasticMolecular Sequence DataMyristic AcidNerve Tissue ProteinsNuclear Localization SignalsProto-Oncogene Proteins c-mycQuailTumor Suppressor ProteinsCalmodulinCalmodulin-Binding ProteinsMYC protein, humanMyristic AcidNerve Tissue ProteinsNuclear Localization SignalsProto-Oncogene Proteins c-mycTumor Suppressor Proteins

Identifiers

PMID19297618
PMCPMC2667012
OpenAlexW2072631602

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.