Evidence map›Paper›PMID 25935873›Full record

ReviewCurrent opinion in biotechnology2015

Alternative modulation of protein-protein interactions by small molecules.

Gerhard Fischer, Maxim Rossmann, Marko Hyvönen

Abstract readReview
In one paragraph

Review in Current opinion in biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. AI-Enforced Ultra-Large Virtual Screening Discovers Potent CD28 Binders.Journal of chemical information and modeling · 2026
    Article
  2. In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Review
  5. A Valuable Target for Therapy: The Metalloproteinase ADAM10.Current protein & peptide science · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Identification of anti-Acta pharmaceutica Sinica. B · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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.

Gerhard FischerDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
Maxim RossmannDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
Marko HyvönenDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK. Electronic address: mh256@cam.ac.uk.

Funding

Wellcome Trust 090340/Z/09/Z
6 · The paper itself

Abstract

Protein-protein interactions (PPI) have become increasingly popular drug targets, with a number of promising compounds currently in clinical trials. Recent research shows, that PPIs can be modulated in more ways than direct inhibition, where novel non-competitive modes of action promise a solution for the difficult nature of PPI drug discovery. Here, we review recently discovered PPI modulators in light of their mode of action and categorise them as disrupting versus stabilising, orthosteric versus allosteric and by their ability to affect the proteins' dynamics. We also give recent examples of compounds successful in the clinic, analyse their physicochemical properties and discuss how to overcome the hurdles in discovering alternative modes of modulation.

Indexed as

Drug DiscoveryAllosteric RegulationAnimalsDrug Delivery SystemsHumansProtein BindingSmall Molecule LibrariesSmall Molecule Libraries

Identifiers

PMID25935873
PMCPMC4728186

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.