Evidence map›Paper›PMID 32668202›Full record

ArticleCell chemical biology2020

Targeting Endogenous K-RAS for Degradation through the Affinity-Directed Protein Missile System.

Sascha Röth, Thomas J Macartney, Agnieszka Konopacka, Kwok-Ho Chan, Houjiang Zhou, Markus A Queisser, Gopal P Sapkota

Open access · hybridAbstract read
In one paragraph

Article in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.8field-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

39 citing papers in PubMed, 66 citations in OpenAlex.

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  15. RAS degraders: The new frontier for RAS-driven cancers.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Review
  16. Review
  17. Article
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  20. Delivering on the promise of protein degraders.Nature reviews. Drug discovery · 2023
    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

7 authors at 2 institutions in 1 country.

Sascha RöthMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Thomas J MacartneyMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Agnieszka KonopackaGlaxoSmithKline, Protein Degradation Group, Medicines Research Centre, Gunnels Wood Road, Stevenage, UK.
Kwok-Ho ChanGlaxoSmithKline, Protein Degradation Group, Medicines Research Centre, Gunnels Wood Road, Stevenage, UK.
Houjiang ZhouMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Markus A QueisserGlaxoSmithKline, Protein Degradation Group, Medicines Research Centre, Gunnels Wood Road, Stevenage, UK.
Gopal P SapkotaMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK. Electronic address: g.sapkota@dundee.ac.uk.
University of Dundee · GBGlaxoSmithKline (United Kingdom) · GB

Funding

Medical Research Council MC_UU_00018/6Medical Research Council MC_UU_12016/3
6 · The paper itself

Abstract

K-RAS is known as the most frequently mutated oncogene. However, the development of conventional K-RAS inhibitors has been extremely challenging, with a mutation-specific inhibitor reaching clinical trials only recently. Targeted proteolysis has emerged as a new modality in drug discovery to tackle undruggable targets. Our laboratory has developed a system for targeted proteolysis using peptidic high-affinity binders, called "AdPROM." Here, we used CRISPR/Cas9 technology to knock in a GFP tag on the native K-RAS gene in A549 adenocarcinoma (A549

Indexed as

ProteolysisA549 CellsAffinity LabelsCell LineCell ProliferationCRISPR-Cas SystemsGene Knock-In TechniquesGreen Fluorescent ProteinsHumansMicroscopy, FluorescencePeptidesProtein IsoformsProto-Oncogene Proteins p21(ras)Recombinant Fusion ProteinsAffinity LabelsGreen Fluorescent ProteinsKRAS protein, humanPeptidesProtein IsoformsProto-Oncogene Proteins p21(ras)Recombinant Fusion Proteinscancer targetsmonobodynanobodyoncogenePROTACprotein degradationRASRAS/MAPK signalingtargeted proteolysisubiquitin proteasome system

Identifiers

PMID32668202
PMCPMC7505679
OpenAlexW3043369247

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.