Evidence map›Paper›PMID 31636382›Full record

ReviewOncogene2020

Precision medicine by designer interference peptides: applications in oncology and molecular therapeutics.

Anabel Sorolla, Edina Wang, Emily Golden, Ciara Duffy, Sónia T Henriques, Andrew D Redfern, Pilar Blancafort

Open access · hybridAbstract readReview
In one paragraph

Review in Oncogene, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Defining peptides in ChEBI.Journal of cheminformatics · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Elucidating the Role ofCurrent issues in molecular biology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. ACS omega · 2024
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
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

7 authors at 3 institutions in 1 country.

Anabel SorollaHarry Perkins Institute of Medical Research, QEII Medical Centre and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia. anabel.sorollabardaji@perkins.uwa.edu.au.
Edina WangHarry Perkins Institute of Medical Research, QEII Medical Centre and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia.
Emily GoldenHarry Perkins Institute of Medical Research, QEII Medical Centre and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia.
Ciara DuffyHarry Perkins Institute of Medical Research, QEII Medical Centre and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia.
Sónia T HenriquesSchool of Biomedical Sciences, Faculty of Health, Institute of Health & Biomedical Innovation, Queensland University of Technology, Translational Research Institute, Brisbane, QLD, 4102, Australia.
Andrew D RedfernSchool of Medicine, The University of Western Australia, Crawley, WA, 6009, Australia.
Pilar BlancafortHarry Perkins Institute of Medical Research, QEII Medical Centre and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia. pilar.blancafort@uwa.edu.au.
University of Western Australia · AUHarry Perkins Institute of Medical Research · AUQueensland University of Technology · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In molecular cancer therapeutics only 10% of known cancer gene products are targetable with current pharmacological agents. Major oncogenic drivers, such as MYC and KRAS proteins are frequently highly overexpressed or mutated in multiple human malignancies. However, despite their key role in oncogenesis, these proteins are hard to target with traditional small molecule drugs due to their large, featureless protein interfaces and lack of deep pockets. In addition, they are inaccessible to large biologicals, which are unable to cross cell membranes. Designer interference peptides (iPeps) represent emerging pharmacological agents created to block selective interactions between protein partners that are difficult to target with conventional small molecule chemicals or with large biologicals. iPeps have demonstrated successful inhibition of multiple oncogenic drivers with some now entering clinical settings. However, the clinical translation of iPeps has been hampered by certain intrinsic limitations including intracellular localization, targeting tissue specificity and pharmacological potency. Herein, we outline recent advances for the selective inhibition of major cancer oncoproteins via iPep approaches and discuss the development of multimodal peptides to overcome limitations of the first generations of iPeps. Since many protein-protein interfaces are cell-type specific, this approach opens the door to novel programmable, precision medicine tools in cancer research and treatment for selective manipulation and reprogramming of the cancer cell oncoproteome.

Indexed as

Precision MedicineAntineoplastic AgentsHumansNeoplasmsOncogenesPeptide FragmentsAntineoplastic AgentsPeptide Fragments

Identifiers

PMID31636382
PMCPMC7002299
OpenAlexW2980759136

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.