Evidence map›Paper›PMID 41076584›Full record

ArticleACS chemical biology2025

Development of Second-Generation Acyl Silane Photoaffinity Probes for Cellular Chemoproteomic Profiling.

Annika C S Page, Lauren M Orr, Margot L Meyers, Bridget P Belcher, Theodore G Coffey, Spencer O Scholz, Sabine Cismoski, Daniel K Nomura, F Dean Toste

Abstract read
In one paragraph

Article in ACS chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Annika C S PageDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Lauren M OrrDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Margot L MeyersDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Bridget P BelcherDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Theodore G CoffeyDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Spencer O ScholzDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.ORCID 0000-0002-5082-7204
Sabine CismoskiDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Daniel K NomuraDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.ORCID 0000-0003-1614-8360
F Dean TosteDepartment of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.ORCID 0000-0001-8018-2198

Funding

Chemical Approaches to Modulate PAX3-FOXO1 in Fusion-Positive Alveolar RhabdomyosarcomaUM1CA294108 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALEX B BURGIN, Alexandra E Gould · 2024 to 2026
$6.9M
Tackling Undruggable Cancer Targets using Chemoproteomic PlatformsR35CA263814 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI Daniel Nomura · 2022 to 2026
$4.6M
Harnessing E3 Ligases for Cancer TherapyR01CA240981 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI Daniel Nomura · 2019 to 2026
$4.3M
Acquisition of a Cryoprobe and Related Accessories for a 600 MHz NMR Spectrometer to Support Health Research Activities at the University of California, BerkeleyS10OD024998 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI HARTWIG, JOHN F · 2018 to 2018
$265k
National Science Foundation 2127788NCI NIH HHS R01 CA240981NCI NIH HHS R35 CA263814NCI NIH HHS UM1 CA294108NIH HHS S10 OD024998
6 · The paper itself

Abstract

Deconvolution of the protein targets of hit compounds from phenotypic screens, often conducted in live cells, is critical for understanding mechanism of action and identifying potentially hazardous off-target interactions. While photoaffinity labeling and chemoproteomics are long-established approaches for discovering small-molecule-protein interactions in live cells, there are a relatively small number of photoaffinity labeling strategies that can be applied for chemoproteomic target identification studies. Recently, we reported a novel chemical framework for photoaffinity labeling based on the photo-Brook rearrangement of acyl silanes and demonstrated its ability, when appended to protein-targeting ligands, to label recombinant proteins. Here, we report the application of these probes to live cell photoaffinity workflows, demonstrate their complementarity to current state-of-the-art minimalist diazirine-based photoaffinity probes, and introduce a modular synthetic route to access acyl silane scaffolds with improved labeling properties.

Indexed as

Photoaffinity LabelsProteomicsSilanesDiazomethaneHumansDiazomethanePhotoaffinity LabelsSilanes

Identifiers

PMID41076584
PMCPMC13157324

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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.