Evidence map›Paper›PMID 30869179›Full record

ReviewAngewandte Chemie (International ed. in English)2020

Targeting the Small GTPase Superfamily through Their Regulatory Proteins.

Janine L Gray, Frank von Delft, Paul E Brennan

Open access · hybridAbstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Activation of Lysosomal Retrograde Transport Triggers TPC1-IP3R1 CaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  10. Article
  11. Methods for Controlling Small GTPase Activity.Chembiochem : a European journal of chemical biology · 2025
    Review
  12. Review
  13. Dual Role for Pld1 inJournal of proteome research · 2025
    Article
  14. Article
  15. Article
  16. Review
  17. Heterogeneous folding landscapes and predetermined breaking points within a protein family.Protein science : a publication of the Protein Society · 2024
    Article
  18. A Comparative Genomic Study of Conventional and Undifferentiated Melanoma.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2024
    Article
  19. Article
  20. Article

25 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

3 authors at 2 institutions in 2 countries.

Janine L GrayStructural Genomics Consortium, University of Oxford, NDMRB, Old Road Campus, Oxford, OX3 7DQ, UK.ORCID 0000-0001-8679-2499
Frank von DelftStructural Genomics Consortium, University of Oxford, NDMRB, Old Road Campus, Oxford, OX3 7DQ, UK.ORCID 0000-0003-0378-0017
Paul E BrennanStructural Genomics Consortium, University of Oxford, NDMRB, Old Road Campus, Oxford, OX3 7DQ, UK.ORCID 0000-0002-8950-7646
Nuffield Orthopaedic Centre · GBUniversity of Johannesburg · ZA

Funding

Wellcome TrustWellcome Trust 106169/ZZ14/Z
6 · The paper itself

Abstract

The Ras superfamily of small GTPases are guanine-nucleotide-dependent switches essential for numerous cellular processes. Mutations or dysregulation of these proteins are associated with many diseases, but unsuccessful attempts to target the small GTPases directly have resulted in them being classed as "undruggable". The GTP-dependent signaling of these proteins is controlled by their regulators; guanine nucleotide exchange factors (GEFs), GTPase activating proteins (GAPs), and in the Rho and Rab subfamilies, guanine nucleotide dissociation inhibitors (GDIs). This review covers the recent small molecule and biologics strategies to target the small GTPases through their regulators. It seeks to critically re-evaluate recent chemical biology practice, such as the presence of PAINs motifs and the cell-based readout using compounds that are weakly potent or of unknown specificity. It highlights the vast scope of potential approaches for targeting the small GTPases in the future through their regulatory proteins.

Indexed as

Binding SitesDrug Evaluation, PreclinicalHumansMolecular Dynamics SimulationMonomeric GTP-Binding ProteinsPeptidesPhylogenyProtein BindingSmall Molecule LibrariesStructure-Activity RelationshipMonomeric GTP-Binding ProteinsPeptidesSmall Molecule Librariesdrug discoverypeptidesprotein-protein interactionssmall GTPasessmall molecules

Identifiers

PMID30869179
PMCPMC7204875
OpenAlexW2920815711

What OpenQuestion holds

Textmetadata
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.