Evidence map›Paper›PMID 42855951›Full record

ReviewChembiochem : a European journal of chemical biology2026

Functionalization of Peptides via Radical Arylation.

Daniel R Troeger, Markus R Heinrich

Abstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Daniel R TroegerDepartment of Chemistry and Pharmacy, Pharmaceutical Chemistry, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.ORCID https://orcid.org/0009-0001-4678-1549
Markus R HeinrichDepartment of Chemistry and Pharmacy, Pharmaceutical Chemistry, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.ORCID https://orcid.org/0000-0001-7113-2025

Funding

Deutsche Forschungsgemeinschaft DFG-HE5413/10-1
6 · The paper itself

Abstract

Among the manifold methods for the functionalization of peptides known today, radical chemistry has so far only rarely been exploited to introduce structural modifications on this challenging type of substrate. In this short review, we give an overview showing that, especially, radical arylation reactions can represent attractive and powerful tools to access functionalized peptides under mild and biocompatible conditions where no protecting group strategy is required. Besides offering new opportunities to directly synthesize functionalized peptides for diverse biological applications, including drug development, it is also our intention to give deeper insight into aryl radical generation and aryl radical reactivity, which can, in a wider sense, be highly useful for future developments in the field of the selective radical functionalization of biomacromolecules.

Indexed as

PeptidesFree RadicalsFree RadicalsPeptidesarylationcysteinepeptidesradical reactionsselenocysteinetryptophantyrosine

Identifiers

PMID42855951
PMCPMC13653118

What OpenQuestion holds

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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.