Evidence map›Paper›PMID 29666374›Full record

ArticleNature communications2018

HATRIC-based identification of receptors for orphan ligands.

Nadine Sobotzki, Michael A Schafroth, Alina Rudnicka, Anika Koetemann, Florian Marty, Sandra Goetze, Yohei Yamauchi, Erick M Carreira, Bernd Wollscheid

Abstract readEvaluation Study
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
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

40 citing papers in PubMed.

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  16. Influenza A virus exploits transferrin receptor recycling to enter host cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Endogenous l- to d-amino acid residue isomerization modulates selectivity between distinct neuropeptide receptor family members.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Review
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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

9 authors.

Nadine SobotzkiDepartment of Health Sciences and Technology & Institute of Molecular Systems Biology & BioMedical Proteomics Platform (BMPP), ETH Zurich, Zurich, Switzerland.
Michael A SchafrothDepartment of Chemistry and Applied Biosciences, Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, Zürich, 8093, Switzerland.ORCID http://orcid.org/0000-0002-5864-6766
Alina RudnickaUniversity of Zurich, Institute of Molecular Life Sciences, Winterthurerstrasse 190, Zurich, CH-8057, Switzerland.
Anika KoetemannDepartment of Health Sciences and Technology & Institute of Molecular Systems Biology & BioMedical Proteomics Platform (BMPP), ETH Zurich, Zurich, Switzerland.
Florian MartyDualsystems Biotech AG, Wagistrasse 12, Schlieren, 8952, Switzerland.ORCID http://orcid.org/0000-0002-6801-6549
Sandra GoetzeDepartment of Health Sciences and Technology & Institute of Molecular Systems Biology & BioMedical Proteomics Platform (BMPP), ETH Zurich, Zurich, Switzerland.
Yohei YamauchiSchool of Cellular and Molecular Medicine, University of Bristol, Biomedical Sciences Building, University Walk, Bristol, BS8 1TD, UK.ORCID http://orcid.org/0000-0002-8233-9133
Erick M CarreiraDepartment of Chemistry and Applied Biosciences, Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, Zürich, 8093, Switzerland.
Bernd WollscheidDepartment of Health Sciences and Technology & Institute of Molecular Systems Biology & BioMedical Proteomics Platform (BMPP), ETH Zurich, Zurich, Switzerland. wbernd@ethz.ch.ORCID http://orcid.org/0000-0002-3923-1610

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular responses depend on the interactions of extracellular ligands, such as nutrients, growth factors, or drugs, with specific cell-surface receptors. The sensitivity of these interactions to non-physiological conditions, however, makes them challenging to study using in vitro assays. Here we present HATRIC-based ligand receptor capture (HATRIC-LRC), a chemoproteomic technology that successfully identifies target receptors for orphan ligands on living cells ranging from small molecules to intact viruses. HATRIC-LRC combines a click chemistry-based, protein-centric workflow with a water-soluble catalyst to capture ligand-receptor interactions at physiological pH from as few as 1 million cells. We show HATRIC-LRC utility for general antibody target validation within the native nanoscale organization of the surfaceome, as well as receptor identification for a small molecule ligand. HATRIC-LRC further enables the identification of complex extracellular interactomes, such as the host receptor panel for influenza A virus (IAV), the causative agent of the common flu.

Indexed as

LigandsAffinity LabelsAntibodiesCatalysisCell Line, TumorCell MembraneChromatography, AffinityClick ChemistryHumansInfluenza A virusProteomicsReceptors, Cell SurfaceSolubilityStaining and LabelingWaterAffinity LabelsAntibodiesLigandsReceptors, Cell SurfaceWater

Identifiers

PMID29666374
PMCPMC5904110

What OpenQuestion holds

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LicenceCC BY
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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.