Evidence map›Paper›PMID 24929527›Full record

ReviewNature chemical biology2014

Small-molecule modulation of Ras signaling.

Jochen Spiegel, Philipp M Cromm, Gunther Zimmermann, Tom N Grossmann, Herbert Waldmann

Abstract readReview
PubMed Publisher
In one paragraph

Review 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 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing 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

112 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Peptide-based covalent inhibitors of protein-protein interactions.Journal of peptide science : an official publication of the European Peptide Society · 2023
    Review
  20. Article

52 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.

Jochen Spiegel1] Max Planck Institute of Molecular Physiology, Dortmund, Germany. [2] Department of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Philipp M Cromm1] Max Planck Institute of Molecular Physiology, Dortmund, Germany. [2] Department of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Gunther Zimmermann1] Max Planck Institute of Molecular Physiology, Dortmund, Germany. [2] Department of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.
Tom N Grossmann1] Department of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany. [2] Chemical Genomics Centre of the Max Planck Society, Dortmund, Germany.
Herbert Waldmann1] Max Planck Institute of Molecular Physiology, Dortmund, Germany. [2] Department of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite intense efforts in pharmaceutical industry and academia, a therapeutic grip on oncogenic Ras proteins has remained elusive. Mutated Ras is associated with ~20-30% of all human cancers often not responsive to established therapies. In particular, K-Ras, the most frequently mutated Ras isoform, is considered one of the most important but 'undruggable' targets in cancer research. Recently, new cavities on Ras for small-molecule ligands were identified, and selective direct targeting of mutated K-Ras(G12C) has become possible for what is to our knowledge the first time. In addition, impairment of Ras spatial organization, in particular via targeting the prenyl-binding Ras chaperone PDEδ, has opened a fresh perspective in anticancer research. These recent advances fuel hopes for the development of new drugs targeting Ras.

Indexed as

Signal TransductionAmino Acid SequenceGuanosine DiphosphateGuanosine TriphosphateHumansMolecular Sequence DataMolecular Targeted TherapyMutationProtein ConformationProtein Kinasesras ProteinsSmall Molecule LibrariescAMP phosphodiesterase kinaseGuanosine DiphosphateGuanosine TriphosphateProtein Kinasesras ProteinsSmall Molecule Libraries

Identifiers

PMID24929527

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.