ArticleJournal of the American Chemical Society2025
Proteome-Wide Covalent Targeting of Acidic Residues with Tunable
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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.
Who cites it
6 citing papers in PubMed.
- Unlocking the Silent Proteome: Chemoselective Asn/Gln Activation for Multidimensional Protein Diversification.Journal of the American Chemical Society · 2026Article
- Covalent modification of a glutamic acid inspired by HaloTag technology.Nature communications · 2026Article
- Tryptophan Bioconjugation through Auxiliary Boron-Accelerated, Additive-Free Friedel-Crafts Alkylation.JACS Au · 2026Article
- Targeting a Glutamic Acid in PDEδ with Fluoromethyl-Aryl Electrophiles Impairs K-Ras Signaling.Journal of medicinal chemistry · 2026Article
- Direct Aziridine Synthesis from Amines and Styrene Derivatives via a Base-Promoted Oxidative Cascade Reaction.Journal of the American Chemical Society · 2026Article
- Synthesis and Application of Bioactive N-Functionalized Aziridines.Angewandte Chemie (International ed. in English) · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Carboxylate side chains in aspartic and glutamic acids play critical roles in protein structure and function due to their polarity and negative charge. These acidic residues, which are abundant in high-value drug targets, represent attractive yet underexplored hotspots for covalent inhibitor discovery. In this study, we introduce
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.