Evidence map›Paper›PMID 37438365›Full record

ArticleNature communications2023

Deciphering intercellular signaling complexes by interaction-guided chemical proteomics.

Jiangnan Zheng, Zhendong Zheng, Changying Fu, Yicheng Weng, An He, Xueting Ye, Weina Gao, Ruijun Tian

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. 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
5.1field-weighted citation impact, top 4% 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, 22 citations in OpenAlex.

  1. Article
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  9. Foundation models in molecular biology.Biophysics reports · 2024
    Article
  10. Proximitomics by Reactive Species.ACS central science · 2024
    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

8 authors at 2 institutions in 1 country.

Jiangnan Zheng *Department of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China. zhengjn@sustech.edu.cn.ORCID 0000-0001-7268-2934
Zhendong Zheng *Department of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China.ORCID 0000-0003-1124-082X
Changying Fu *Department of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China.
Yicheng WengDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China.
An HeDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China.
Xueting YeDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China.
Weina GaoDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China.
Ruijun TianDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China. tianrj@sustech.edu.cn.ORCID 0000-0001-9521-5124
Southern University of Science and Technology · CNHarbin Institute of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Indirect cell-cell interactions mediated by secreted proteins and their plasma membrane receptors play essential roles for regulating intercellular signaling. However, systematic profiling of the interactions between living cell surface receptors and secretome from neighboring cells remains challenging. Here we develop a chemical proteomics approach, termed interaction-guided crosslinking (IGC), to identify ligand-receptor interactions in situ. By introducing glycan-based ligation and click chemistry, the IGC approach via glycan-to-glycan crosslinking successfully captures receptors from as few as 0.1 million living cells using only 10 ng of secreted ligand. The unparalleled sensitivity and selectivity allow systematic crosslinking and identification of ligand-receptor complexes formed between cell secretome and surfaceome in an unbiased and all-to-all manner, leading to the discovery of a ligand-receptor interaction between pancreatic cancer cell-secreted urokinase (PLAU) and neuropilin 1 (NRP1) on pancreatic cancer-associated fibroblasts. This approach is thus useful for systematic exploring new ligand-receptor pairs and discovering critical intercellular signaling events.

Indexed as

ProteomicsSignal TransductionBiological TransportCell CommunicationLigandsLigands

Identifiers

PMID37438365
PMCPMC10338493
OpenAlexW4384023567

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.