Evidence map›Paper›PMID 31790487›Full record

ArticlePloS one2019

Formation of a structurally-stable conformation by the intrinsically disordered MYC:TRRAP complex.

Edmond J Feris, John W Hinds, Michael D Cole

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  8. Epigenetic Control of Translation Checkpoint and Tumor Progression via RUVBL1-EEF1A1 Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  9. MYC: a complex problem.Trends in cell biology · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Structure of the human SAGA coactivator complex.Nature structural & molecular biology · 2021
    Article
  14. Article
  15. Review
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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.

Edmond J FerisDepartment of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH, United States of America.ORCID 0000-0001-9649-2844
John W HindsDepartment of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH, United States of America.
Michael D ColeDepartment of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH, United States of America.ORCID 0000-0002-3421-5451
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
FUNCTION OF THE C-MYC ONCOGENER01CA055248 · NCI · PRINCETON UNIVERSITY · PI COLE, MICHAEL DAVID · 1992 to 2020
$8.6M
NCI NIH HHS P30 CA023108NCI NIH HHS R01 CA055248
6 · The paper itself

Abstract

Our primary goal is to therapeutically target the oncogenic transcription factor MYC to stop tumor growth and cancer progression. Here, we report aspects of the biophysical states of the MYC protein and its interaction with one of the best-characterized MYC cofactors, TRansactivation/tRansformation-domain Associated Protein (TRRAP). The MYC:TRRAP interaction is critical for MYC function in promoting cancer. The interaction between MYC and TRRAP occurs at a precise region in the MYC protein, called MYC Homology Box 2 (MB2), which is central to the MYC transactivation domain (TAD). Although the MYC TAD is inherently disordered, this report suggests that MB2 may acquire a defined structure when complexed with TRRAP which could be exploited for the investigation of inhibitors of MYC function by preventing this protein-protein interaction (PPI). The MYC TAD, and in particular the MB2 motif, is unique and invariant in evolution, suggesting that MB2 is an ideal site for inhibiting MYC function.

Indexed as

Adaptor Proteins, Signal TransducingEthylene GlycolHEK293 CellsHumansIntrinsically Disordered ProteinsNuclear ProteinsProtein BindingProtein ConformationProtein StabilityProton Magnetic Resonance SpectroscopyProto-Oncogene Proteins c-mycAdaptor Proteins, Signal TransducingEthylene GlycolIntrinsically Disordered ProteinsNuclear ProteinsProto-Oncogene Proteins c-myctransformation-transcription domain-associated protein

Identifiers

PMID31790487
PMCPMC6886782
OpenAlexW2991244815

What OpenQuestion holds

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LicenceCC BY
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.