Evidence map›Paper›PMID 36732563›Full record

ArticleScientific reports2023

Characterisation of a cyclic peptide that binds to the RAS binding domain of phosphoinositide 3-kinase p110α.

Mohamed Ismail, Stephen R Martin, Roger George, Francesca Houghton, Geoff Kelly, Raphaël A G Chaleil, Panayiotis Anastasiou, Xinyue Wang, Nicola O'Reilly, Stefania Federico and 8 more

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. A renaissance in targeting the PI3K/AKT/mTOR pathway.Nature reviews. Drug discovery · 2026
    Review
  5. Review
  6. Article
  7. Review
  8. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 2 institutions in 1 country.

Mohamed IsmailOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Stephen R MartinStructural Biology, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Roger GeorgeStructural Biology, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Francesca HoughtonOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Geoff KellyStructural Biology, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Raphaël A G ChaleilBiomolecular Modelling Lab, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Panayiotis AnastasiouOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Xinyue WangOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Nicola O'ReillyPeptide Chemistry, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Stefania FedericoPeptide Chemistry, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Dhira JoshiPeptide Chemistry, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Hemavathi NagarajPeptide Chemistry, Science Technology Platforms, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Rachel CooleyOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Ning Sze HuiOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Miriam Molina-ArcasOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
David C HancockOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Ali TavassoliSchool of Chemistry, University of Southampton, Southampton, SO17 1BJ, UK.
Julian DownwardOncogene Biology Laboratory, Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. julian.downward@crick.ac.uk.
The Francis Crick Institute · GBUniversity of Southampton · GB

Funding

Cancer Research UK 15680Cancer Research UK 20185Medical Research Council MC_PC_17179Medical Research Council MR/W004054/1Wellcome Trust FC001070
6 · The paper itself

Abstract

P110α is a member of the phosphoinositide 3-kinase (PI3K) enzyme family that functions downstream of RAS. RAS proteins contribute to the activation of p110α by interacting directly with its RAS binding domain (RBD), resulting in the promotion of many cellular functions such as cell growth, proliferation and survival. Previous work from our lab has highlighted the importance of the p110α/RAS interaction in tumour initiation and growth. Here we report the discovery and characterisation of a cyclic peptide inhibitor (cyclo-CRVLIR) that interacts with the p110α-RBD and blocks its interaction with KRAS. cyclo-CRVLIR was discovered by screening a "split-intein cyclisation of peptides and proteins" (SICLOPPS) cyclic peptide library. The primary cyclic peptide hit from the screen initially showed a weak affinity for the p110α-RBD (K

Indexed as

Phosphatidylinositol 3-KinaseSignal TransductionPeptides, CyclicPhosphatidylinositol 3-KinasesProto-Oncogene Proteins p21(ras)Peptides, CyclicPhosphatidylinositol 3-KinasePhosphatidylinositol 3-KinasesProto-Oncogene Proteins p21(ras)

Identifiers

PMID36732563
PMCPMC9894841
OpenAlexW4319001254

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.