Evidence map›Paper›PMID 35914173›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Radius measurement via super-resolution microscopy enables the development of a variable radii proximity labeling platform.

James V Oakley, Benito F Buksh, David F Fernández, Daniel G Oblinsky, Ciaran P Seath, Jacob B Geri, Gregory D Scholes, David W C MacMillan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing 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

87 citing papers in PubMed.

  1. Review
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  5. Chemical Biology 2025: Highlights From the Ch/Bi145 Course at Caltech.Chembiochem : a European journal of chemical biology · 2026
    Review
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  10. 2-Alkyl Furans Undergo Radiolytic Oxidative Protein Cross-Linking.Journal of the American Chemical Society · 2026
    Article
  11. Review
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  13. AbioRxiv : the preprint server for biology · 2026
    Article
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27 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

8 authors.

James V OakleyMerck Center for Catalysis at Princeton University, Princeton, NJ 08544.ORCID 0000-0003-4774-5205
Benito F BukshMerck Center for Catalysis at Princeton University, Princeton, NJ 08544.
David F FernándezMerck Center for Catalysis at Princeton University, Princeton, NJ 08544.ORCID 0000-0003-3482-0894
Daniel G OblinskyDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0001-7460-8260
Ciaran P SeathMerck Center for Catalysis at Princeton University, Princeton, NJ 08544.
Jacob B GeriMerck Center for Catalysis at Princeton University, Princeton, NJ 08544.
Gregory D ScholesDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0003-3336-7960
David W C MacMillanMerck Center for Catalysis at Princeton University, Princeton, NJ 08544.

Funding

Photoredox Catalysis Applications in Organometallics and Chemical BiologyR35GM134897 · NIGMS · PRINCETON UNIVERSITY · PI David W MacMillan · 2020 to 2026
$6.3M
HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM134897NIGMS NIH HHS R35 GM134897
6 · The paper itself

Abstract

The elucidation of protein interaction networks is critical to understanding fundamental biology as well as developing new therapeutics. Proximity labeling platforms (PLPs) are state-of-the-art technologies that enable the discovery and delineation of biomolecular networks through the identification of protein-protein interactions. These platforms work via catalytic generation of reactive probes at a biological region of interest; these probes then diffuse through solution and covalently "tag" proximal biomolecules. The physical distance that the probes diffuse determines the effective labeling radius of the PLP and is a critical parameter that influences the scale and resolution of interactome mapping. As such, by expanding the degrees of labeling resolution offered by PLPs, it is possible to better capture the various size scales of interactomes. At present, however, there is little quantitative understanding of the labeling radii of different PLPs. Here, we report the development of a superresolution microscopy-based assay for the direct quantification of PLP labeling radii. Using this assay, we provide direct extracellular measurements of the labeling radii of state-of-the-art antibody-targeted PLPs, including the peroxidase-based phenoxy radical platform (269 ± 41 nm) and the high-resolution iridium-catalyzed µMap technology (54 ± 12 nm). Last, we apply these insights to the development of a molecular diffusion-based approach to tuning PLP resolution and introduce a new aryl-azide-based µMap platform with an intermediate labeling radius (80 ± 28 nm).

Indexed as

MicroscopyProtein Interaction MapsAzidesCatalysisAzidesphotoredox catalysisproximity labelingSTED microscopy

Identifiers

PMID35914173
PMCPMC9371666

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Registered trials

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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.