Evidence map›Paper›PMID 38233583›Full record

ArticleNature chemical biology2024

Profiling the interactome of oligonucleotide drugs by proximity biotinylation.

Alfred Hanswillemenke, Daniel Tobias Hofacker, Michèle Sorgenfrei, Carolin Fruhner, Mirita Franz-Wachtel, Dirk Schwarzer, Boris Maček, Thorsten Stafforst

Open access · hybridAbstract read
In one paragraph

Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
6.5field-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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  11. Article
  12. Article
  13. Measuring Ligand-bound Protein Complexes with Proximity Labeling: A Practical Guide.Chembiochem : a European journal of chemical biology · 2024
    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

8 authors at 1 institution in 1 country.

Alfred Hanswillemenke *Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0009-0004-1651-7132
Daniel Tobias Hofacker *Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0001-5880-0690
Michèle SorgenfreiInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0001-8480-197X
Carolin FruhnerInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Mirita Franz-WachtelInterfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Dirk SchwarzerInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-7477-3319
Boris MačekInterfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-1206-2458
Thorsten StafforstInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany. thorsten.stafforst@uni-tuebingen.de.ORCID 0000-0001-9359-3439
University of Tübingen · DE

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 430214260Deutsche Forschungsgemeinschaft (German Research Foundation) 455100081
6 · The paper itself

Abstract

Drug-ID is a novel method applying proximity biotinylation to identify drug-protein interactions inside living cells. The covalent conjugation of a drug with a biotin ligase enables targeted biotinylation and identification of the drug-bound proteome. We established Drug-ID for two small-molecule drugs, JQ1 and SAHA, and applied it for RNaseH-recruiting antisense oligonucleotides (ASOs). Drug-ID profiles the drug-protein interactome de novo under native conditions, directly inside living cells and at pharmacologically effective drug concentrations. It requires minimal amounts of cell material and might even become applicable in vivo. We studied the dose-dependent aggregation of ASOs and the effect of different wing chemistries (locked nucleic acid, 2'-methoxyethyl and 2'-Fluoro) and ASO lengths on the interactome. Finally, we demonstrate the detection of stress-induced, intracellular interactome changes (actinomycin D treatment) with an in situ variant of the approach, which uses a recombinant biotin ligase and does not require genetic manipulation of the target cell.

Indexed as

BiotinylationBiotinCarbon-Nitrogen LigasesHumansOligonucleotides, AntisenseProtein BindingRibonuclease HBiotinCarbon-Nitrogen LigasesOligonucleotides, AntisenseRibonuclease H

Identifiers

PMID38233583
PMCPMC11062921
OpenAlexW4390954524

What OpenQuestion holds

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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.