Evidence map›Paper›PMID 25362358›Full record

ArticleNature chemical biology2014

Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells.

Wade Borcherds, François-Xavier Theillet, Andrea Katzer, Ana Finzel, Katie M Mishall, Anne T Powell, Hongwei Wu, Wanda Manieri, Christoph Dieterich, Philipp Selenko and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
–field-weighted citation impact
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

113 citing papers in PubMed.

  1. Article
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  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Transient helices with functional roles.Biophysical journal · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Commonly asked questions about transcriptional activation domains.Current opinion in structural biology · 2024
    Review
  20. Structural biases in disordered proteins are prevalent in the cell.Nature structural & molecular biology · 2024
    Article

53 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Wade Borcherds1] Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA. [2] Center for Drug Discovery and Innovation, University of South Florida, Tampa, Florida, USA.
François-Xavier TheilletIn-cell NMR Laboratory, Department of NMR-supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Berlin, Germany.
Andrea KatzerBerlin Institute for Medical Systems Biology, Max Delbrueck Center for Molecular Medicine, Berlin, Germany.
Ana FinzelBerlin Institute for Medical Systems Biology, Max Delbrueck Center for Molecular Medicine, Berlin, Germany.
Katie M Mishall1] Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA. [2] Center for Drug Discovery and Innovation, University of South Florida, Tampa, Florida, USA.
Anne T Powell1] Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA. [2] Center for Drug Discovery and Innovation, University of South Florida, Tampa, Florida, USA.
Hongwei Wu1] Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA. [2] Center for Drug Discovery and Innovation, University of South Florida, Tampa, Florida, USA.
Wanda ManieriDrug Discovery Department, Moffitt Cancer Center, University of South Florida, Tampa, Florida, USA.
Christoph DieterichMax Planck Institute for Biology of Ageing, Cologne, Germany.
Philipp SelenkoIn-cell NMR Laboratory, Department of NMR-supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Berlin, Germany.
Alexander LoewerBerlin Institute for Medical Systems Biology, Max Delbrueck Center for Molecular Medicine, Berlin, Germany.
Gary W Daughdrill1] Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida, USA. [2] Center for Drug Discovery and Innovation, University of South Florida, Tampa, Florida, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Levels of residual structure in disordered interaction domains determine in vitro binding affinities, but whether they exert similar roles in cells is not known. Here, we show that increasing residual p53 helicity results in stronger Mdm2 binding, altered p53 dynamics, impaired target gene expression and failure to induce cell cycle arrest upon DNA damage. These results establish that residual structure is an important determinant of signaling fidelity in cells.

Indexed as

Signal TransductionCell CycleCell Line, TumorDNA DamageEscherichia coliGamma RaysGene Expression RegulationHumansIntrinsically Disordered ProteinsModels, MolecularMutationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene Proteins c-mdm2Recombinant ProteinsIntrinsically Disordered ProteinsMDM2 protein, humanProto-Oncogene Proteins c-mdm2Recombinant ProteinsTumor Suppressor Protein p53

Identifiers

PMID25362358

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.