Evidence map›Paper›PMID 40089463›Full record

ArticleNature communications2025

Spatiotemporally resolved mapping of extracellular proteomes via in vivo-compatible TyroID.

Zijuan Zhang, Yankun Wang, Wenjie Lu, Xiaofei Wang, Hongyang Guo, Xuanzhen Pan, Zeyu Liu, Zhaofa Wu, Wei Qin

Abstract read
In one paragraph

Article in Nature communications, 2025. 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
–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

13 citing papers in PubMed.

  1. Review
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  10. Precise andACS central science · 2025
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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.

Zijuan Zhang *School of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Yankun Wang *School of Pharmaceutical Sciences, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0003-1645-5985
Wenjie LuSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Xiaofei WangState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Hongyang GuoSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Xuanzhen PanSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Zeyu LiuSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Zhaofa WuState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-2027-5194
Wei QinSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China. weiqin@tsinghua.edu.cn.ORCID http://orcid.org/0009-0007-4061-2326

Funding

National Natural Science Foundation of China (National Science Foundation of China) 2240070422National Natural Science Foundation of China (National Science Foundation of China) 22477066; 92478128National Natural Science Foundation of China (National Science Foundation of China) 32300614
6 · The paper itself

Abstract

Extracellular proteins play pivotal roles in both intracellular signaling and intercellular communications in health and disease. While recent advancements in proximity labeling (PL) methods, such as peroxidase- and photocatalyst-based approaches, have facilitated the resolution of extracellular proteomes, their in vivo compatibility remains limited. Here, we report TyroID, an in vivo-compatible PL method for the unbiased mapping of extracellular proteins with high spatiotemporal resolution. TyroID employs plant- and bacteria-derived tyrosinases to produce reactive o-quinone intermediates, enabling the labeling of multiple residues on endogenous proteins with bioorthogonal handles, thereby allowing for their identification via chemical proteomics. We validate TyroID's specificity by mapping extracellular proteomes and HER2-neighboring proteins using affibody-directed recombinant tyrosinases. Demonstrating its superiority over other PL methods, TyroID enables in vivo mapping of extracellular proteomes, including mapping HER2-proximal proteins in tumor xenografts, quantifying the turnover of plasma proteins and labeling hippocampal-specific proteomes in live mouse brains. TyroID emerges as a potent tool for investigating protein localization and molecular interactions within living organisms.

Indexed as

Extracellular SpaceProteomeProteomicsAnimalsCell Line, TumorErb-b2 Receptor Tyrosine KinasesFemaleHippocampusHumansMiceERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesProteome

Identifiers

PMID40089463
PMCPMC11910615

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.