Evidence map›Paper›PMID 36216892›Full record

ArticleNature chemistry2023

Targeted activation in localized protein environments via deep red photoredox catalysis.

Nicholas Eng Soon Tay, Keun Ah Ryu, John L Weber, Aleksandra K Olow, David C Cabanero, David R Reichman, Rob C Oslund, Olugbeminiyi O Fadeyi, Tomislav Rovis

Abstract read
In one paragraph

Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Article
  2. Review
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  5. Article
  6. Article
  7. Article
  8. Article
  9. 2-Alkyl Furans Undergo Radiolytic Oxidative Protein Cross-Linking.Journal of the American Chemical Society · 2026
    Article
  10. Review
  11. Review
  12. AbioRxiv : the preprint server for biology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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.

Nicholas Eng Soon Tay *Department of Chemistry, Columbia University, New York, NY, USA.
Keun Ah Ryu *Exploratory Science Center, Merck & Co., Inc., Cambridge, MA, USA.
John L WeberDepartment of Chemistry, Columbia University, New York, NY, USA.
Aleksandra K OlowGenetics and Pharmacogenomics, Merck & Co., Inc., San Francisco, CA, USA.
David C CabaneroDepartment of Chemistry, Columbia University, New York, NY, USA.
David R ReichmanDepartment of Chemistry, Columbia University, New York, NY, USA.
Rob C OslundExploratory Science Center, Merck & Co., Inc., Cambridge, MA, USA. rob@induprolabs.com.ORCID 0000-0002-2920-9532
Olugbeminiyi O FadeyiExploratory Science Center, Merck & Co., Inc., Cambridge, MA, USA. niyi@induprolabs.com.ORCID 0000-0002-5525-1304
Tomislav RovisDepartment of Chemistry, Columbia University, New York, NY, USA. tr2504@columbia.edu.ORCID 0000-0001-6287-8669

Funding

Selective Functionalization of Aliphatic Amines - Supplement to Support Mariah RamosR01GM125206 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ROVIS, TOMISLAV · 2017 to 2024
$2.6M
NIGMS NIH HHS R01 GM125206
6 · The paper itself

Abstract

State-of-the-art photoactivation strategies in chemical biology provide spatiotemporal control and visualization of biological processes. However, using high-energy light (λ < 500 nm) for substrate or photocatalyst sensitization can lead to background activation of photoactive small-molecule probes and reduce its efficacy in complex biological environments. Here we describe the development of targeted aryl azide activation via deep red-light (λ = 660 nm) photoredox catalysis and its use in photocatalysed proximity labelling. We demonstrate that aryl azides are converted to triplet nitrenes via a redox-centric mechanism and show that its spatially localized formation requires both red light and a photocatalyst-targeting modality. This technology was applied in different colon cancer cell systems for targeted protein environment labelling of epithelial cell adhesion molecule (EpCAM). We identified a small subset of proteins with previously known and unknown association to EpCAM, including CDH3, a clinically relevant protein that shares high tumour-selective expression with EpCAM.

Indexed as

Colonic NeoplasmsLightCatalysisEpithelial Cell Adhesion MoleculeHumansEpithelial Cell Adhesion Molecule

Identifiers

PMID36216892
PMCPMC9840673

What OpenQuestion holds

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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.