Evidence map›Paper›PMID 37036999›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

A genetically encoded photoproximity labeling approach for mapping protein territories.

Nir Hananya, Xuanjia Ye, Shany Koren, Tom W Muir

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
14.4field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Evolving faster proximity chemistry.Nature chemical biology · 2026
    Article
  5. Article
  6. 2-Alkyl Furans Undergo Radiolytic Oxidative Protein Cross-Linking.Journal of the American Chemical Society · 2026
    Article
  7. Review
  8. Article
  9. HNature chemical biology · 2026
    Article
  10. Article
  11. A unified photosensitizer platform forbioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Nir HananyaDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0002-9480-3183
Xuanjia YeDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0002-6277-6045
Shany KorenDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0002-3695-4194
Tom W MuirDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0001-9635-0344
Princeton University · US

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Structure, Function and Applications of InteinsR01GM086868 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2008 to 2025
$4.4M
NCI NIH HHS P01 CA196539NIGMS NIH HHS R01 GM086868
6 · The paper itself

Abstract

Studying dynamic biological processes requires approaches compatible with the lifetimes of the biochemical transactions under investigation, which can be very short. We describe a genetically encoded system that allows protein neighborhoods to be mapped using visible light. Our approach involves fusing an engineered flavoprotein to a protein of interest. Brief excitation of the fusion protein leads to the labeling of nearby proteins with cell-permeable probes. Mechanistic studies reveal different labeling pathways are operational depending on the nature of the exogenous probe that is employed. When combined with quantitative proteomics, this photoproximity labeling system generates "snapshots" of protein territories with high temporal and spatial resolution. The intrinsic fluorescence of the fusion domain permits correlated imaging and proteomics analyses, a capability that is exploited in several contexts, including defining the protein clients of the major vault protein. The technology should be broadly useful in the biomedical area.

Indexed as

LightProteinsHumansProteinsLOV domainoptogeneticsphotoproximity labelingprotein–protein interactions

Identifiers

PMID37036999
PMCPMC10120045
OpenAlexW4363676473

What OpenQuestion 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 OpenQuestion graph.