Evidence map›Paper›PMID 8289795›Full record

ArticleMolecular and cellular biology1994

Intracellular association of the protein product of the c-myc oncogene with the TATA-binding protein.

S Maheswaran, H Lee, G E Sonenshein

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.9field-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

31 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Review
  3. Multiple direct interactions of TBP with the MYC oncoprotein.Nature structural & molecular biology · 2019
    Article
  4. TRRAP and GCN5 are used by c-Myc to activate RNA polymerase III transcription.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  5. Article
  6. Article
  7. A global transcriptional regulatory role for c-Myc in Burkitt's lymphoma cells.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Identification of a large Myc-binding protein that contains RCC1-like repeats.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  16. Article
  17. Article
  18. Article
  19. YY1 and c-Myc associate in vivo in a manner that depends on c-Myc levels.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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.

S MaheswaranDepartment of Biochemistry, Boston University School of Medicine, Massachusetts 02118.
H Lee
G E Sonenshein
Boston University · US

Funding

EXPRESSION OF ONCOGENES &IGA GENES IN TRANSFORMED CELLSR01CA036355 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SONENSHEIN, GAIL E · 1985 to 2007
$2.1M
NCI NIH HHS CA36355
6 · The paper itself

Abstract

The c-myc proto-oncogene encodes nuclear phosphoproteins that bind DNA in a sequence-specific fashion and appear to function as transcriptional activators. Here we demonstrate that a 40-kDa nuclear protein coimmunoprecipitated with c-Myc specifically when nuclear proteins, extracted from nuclei of exponentially growing murine B-lymphoma WEHI 231 cells by using procedures for preparation of trans-acting factors, were reacted with anti-c-Myc antibodies made against different regions of the c-Myc protein. In contrast, preparation of nuclear lysates under denaturing conditions significantly reduced this coprecipitation. Upon incubation of WEHI 231 cells with the reversible chemical cross-linking agent dithiobis(succinimidyl propionate), the 40-kDa protein could be cross-linked to c-Myc protein intracellularly. Identification of the 40-kDa protein as the TATA-binding protein (TBP) of the TFIID transcription initiation complex was made by comigration and V-8 protease mapping, which yielded identical peptide fragments upon digestion of the 40-kDa protein and material immunoprecipitated with an anti-TBP specific antibody. Furthermore, in vitro-translated TBP bound to the amino-terminal portion of c-Myc. Column chromatography of cross-linked nuclear proteins showed TBP to be in a large-molecular-weight complex with c-Myc, consistent with a transcription initiation complex. These results indicate that intracellularly, c-Myc interacts with TBP, suggesting a mechanism of interaction of this oncoprotein with the basal transcription machinery.

Indexed as

Genes, mycAnimalsCell LineCell NucleusCross-Linking ReagentsDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelLymphoma, B-CellMiceMolecular WeightNuclear ProteinsProto-Oncogene Proteins c-mycTATA BoxTATA-Box Binding ProteinTranscription FactorsTumor Cells, CulturedCross-Linking ReagentsDNA-Binding ProteinsNuclear ProteinsProto-Oncogene Proteins c-mycTATA-Box Binding ProteinTranscription Factors

Identifiers

PMID8289795
PMCPMC358470
OpenAlexW2158619898

What OpenQuestion holds

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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.