Evidence map›Paper›PMID 22457068›Full record

ArticleNucleic acids research2012

Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding.

Cecilia Andresen, Sara Helander, Alexander Lemak, Christophe Farès, Veronika Csizmok, Jonas Carlsson, Linda Z Penn, Julie D Forman-Kay, Cheryl H Arrowsmith, Patrik Lundström and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.5field-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

71 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Bend it like BIN1: how a membrane-curving adaptor protein shapes cardiac physiology.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. MYC phase separation selectively modulates the transcriptome.Nature structural & molecular biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. mRNA interactions with disordered regions control protein activity.bioRxiv : the preprint server for biology · 2023
    Article
  18. Article
  19. Review
  20. Article

11 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

11 authors at 4 institutions in 3 countries.

Cecilia AndresenDivision of Molecular Biotechnology, Department of Physics, Chemistry and Biology, Linköping University, SE-58183 Linköping, Sweden.
Sara Helander
Alexander Lemak
Christophe Farès
Veronika Csizmok
Jonas Carlsson
Linda Z Penn
Julie D Forman-Kay
Cheryl H Arrowsmith
Patrik Lundström
Maria Sunnerhagen
Linköping University · SEUniversity of Toronto · CAHospital for Sick Children · CAOntario Institute for Cancer Research · CA

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
CIHRNIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

The crucial role of Myc as an oncoprotein and as a key regulator of cell growth makes it essential to understand the molecular basis of Myc function. The N-terminal region of c-Myc coordinates a wealth of protein interactions involved in transformation, differentiation and apoptosis. We have characterized in detail the intrinsically disordered properties of Myc-1-88, where hierarchical phosphorylation of S62 and T58 regulates activation and destruction of the Myc protein. By nuclear magnetic resonance (NMR) chemical shift analysis, relaxation measurements and NOE analysis, we show that although Myc occupies a very heterogeneous conformational space, we find transiently structured regions in residues 22-33 and in the Myc homology box I (MBI; residues 45-65); both these regions are conserved in other members of the Myc family. Binding of Bin1 to Myc-1-88 as assayed by NMR and surface plasmon resonance (SPR) revealed primary binding to the S62 region in a dynamically disordered and multivalent complex, accompanied by population shifts leading to altered intramolecular conformational dynamics. These findings expand the increasingly recognized concept of intrinsically disordered regions mediating transient interactions to Myc, a key transcriptional regulator of major medical importance, and have important implications for further understanding its multifaceted role in gene regulation.

Indexed as

Binding SitesHumansNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene Proteins c-mycsrc Homology DomainsTrans-ActivatorsTumor Suppressor ProteinsMYC protein, humanProto-Oncogene Proteins c-mycTrans-ActivatorsTumor Suppressor Proteins

Identifiers

PMID22457068
PMCPMC3401448
OpenAlexW2133721361

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.