ReviewChemistry (Weinheim an der Bergstrasse, Germany)2026
Precision Chemistry for Protein Lysine Modification.
Review in Chemistry (Weinheim an der Bergstrasse, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Stereoselective Covalent Targeting of BTK(C481S) and Kinases with β-Lactone Electrophiles.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Lysine post-translational modifications (PTMs) play crucial roles in regulating protein structures, interactions, and cellular signaling. Precise study of PTM functions requires homogeneous proteins with modifications at defined sites; however, selective chemical modification is challenging because multiple lysines undergo similar chemistry yet exhibit variable reactivity depending on their local environments. Early chemical strategies exploited intrinsic reactivity differences, which are effective for exposed lysines but limited for low-reactivity or sterically hindered sites. In contrast, enzymes achieve high selectivity through substrate recognition and spatial organization. Inspired by this enzymatic principle, chemical approaches have been developed, including ligand-directed chemistry, proximity-enabled modification, and on-demand generation of highly reactive electrophiles. Recent advances in ligand-guided catalysis now enable regioselective and catalytic installation of biorelevant, authentic PTMs, providing a platform for programmable lysine modification and synthetic epigenetics.
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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.