Evidence map›Paper›PMID 30978004›Full record

ArticleACS chemical biology2019

Rapid and Reversible Knockdown of Endogenously Tagged Endosomal Proteins via an Optimized HaloPROTAC Degrader.

Hannah Tovell, Andrea Testa, Chiara Maniaci, Houjiang Zhou, Alan R Prescott, Thomas Macartney, Alessio Ciulli, Dario R Alessi

Open access · hybridAbstract read
In one paragraph

Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 142 citations in OpenAlex.

  1. Post-Translational Regulation Using Degrons in Ewing Sarcoma.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. TDP-43 dysfunction induces cryptic circular RNAs in ALS/FTD.bioRxiv : the preprint server for biology · 2026
    Article
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14 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

8 authors at 2 institutions in 1 country.

Hannah TovellMedical Research Council (MRC) Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences , University of Dundee , Dow Street , Dundee DD1 5EH , U.K.ORCID 0000-0002-2473-7256
Andrea TestaDivision of Biological Chemistry and Drug Discovery, School of Life Sciences , University of Dundee , Dow Street , Dundee , DD1 5EH , U.K.ORCID 0000-0002-8973-9711
Chiara ManiaciDivision of Biological Chemistry and Drug Discovery, School of Life Sciences , University of Dundee , Dow Street , Dundee , DD1 5EH , U.K.ORCID 0000-0001-7887-7388
Houjiang ZhouMedical Research Council (MRC) Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences , University of Dundee , Dow Street , Dundee DD1 5EH , U.K.
Alan R PrescottDundee Imaging Facility, School of Life Sciences , University of Dundee , Dundee DD1 5EH , U.K.
Thomas MacartneyMedical Research Council (MRC) Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences , University of Dundee , Dow Street , Dundee DD1 5EH , U.K.
Alessio CiulliDivision of Biological Chemistry and Drug Discovery, School of Life Sciences , University of Dundee , Dow Street , Dundee , DD1 5EH , U.K.ORCID 0000-0002-8654-1670
Dario R AlessiMedical Research Council (MRC) Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences , University of Dundee , Dow Street , Dundee DD1 5EH , U.K.ORCID 0000-0002-2140-9185
MRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_U127015387Medical Research Council MC_UU_00018/1Medical Research Council MC_UU_12016/2
6 · The paper itself

Abstract

Inducing post-translational protein knockdown is an important approach to probe biology and validate drug targets. An efficient strategy to achieve this involves expression of a protein of interest fused to an exogenous tag, allowing tag-directed chemical degraders to mediate protein ubiquitylation and proteasomal degradation. Here, we combine improved HaloPROTAC degrader probes with CRISPR/Cas9 genome editing technology to trigger rapid degradation of endogenous target proteins. Our optimized probe, HaloPROTAC-E, a chloroalkane conjugate of high-affinity VHL binder VH298, induced reversible degradation of two endosomally localized proteins, SGK3 and VPS34, with a DC

Indexed as

Class III Phosphatidylinositol 3-KinasesCRISPR-Cas SystemsEndosomesGene EditingGene Knock-In TechniquesHEK293 CellsHumansProteinsProtein Serine-Threonine KinasesClass III Phosphatidylinositol 3-KinasesProteinsProtein Serine-Threonine Kinases

Identifiers

PMID30978004
PMCPMC6528276
OpenAlexW2938455624

What OpenQuestion holds

Textmetadata
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.