Evidence map›Paper›PMID 41388880›Full record

ReviewAngewandte Chemie (International ed. in English)2026

Unnatural Amino Acid and Emerging Chemistry Approaches to Map RNA-Protein Interactions.

Eryn Lundrigan, Parrish Evers, Elexa Scott, John Paul Pezacki

Abstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2026. 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

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

4 authors.

Eryn LundriganDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Pvt, Ottawa, ON, K1N 6N5, Canada.
Parrish EversDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Pvt, Ottawa, ON, K1N 6N5, Canada.
Elexa ScottDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Pvt, Ottawa, ON, K1N 6N5, Canada.
John Paul PezackiDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Pvt, Ottawa, ON, K1N 6N5, Canada.ORCID 0000-0002-4233-8945

Funding

NSERC JPP
6 · The paper itself

Abstract

RNA serves as both a genetic messenger and a functional non-coding molecule, with its activity relying on interactions with diverse proteins. Characterizing RNA-protein interactions remains challenging, particularly for dynamic or low-abundance complexes. Traditional crosslinking methods, such as UV-254 nm irradiation and formaldehyde fixation, suffer from low efficiency, poor specificity, and broad reactivity, limiting their utility for high-resolution interactome mapping. Recent advances in genetic code expansion (GCE) and unnatural amino acid (UAA) incorporation now enable chemoselective, site-specific crosslinking chemistries that circumvent these limitations. This review highlights classes of crosslinkable UAAs, including benzophenone-, diazirine-, and aryl azide-based moieties, which have been used for photo-induced covalent capture of RNA-protein interactions. Next-generation modalities, such as acetophenone derivatives, halogenated UAAs, bifunctional UAAs, acyl silanes, diaryl nitrones, and photoactivatable systems further expand the toolkit for photocrosslinking and bioorthogonal labelling. Beyond UV-based approaches, latent bioreactive UAAs and proximity-induced chemistries exploit electrophile-nucleophile substitution and masked acylating agents to enable covalent capture under physiological conditions. Together, these strategies provide unprecedented control over reactivity, temporal resolution and site specificity, advancing RNA-targeted proteomics. Continued innovation in UAA-based chemistry promise to transform how RNA-protein complexes are interrogated and manipulated with molecular precision.

Indexed as

Amino AcidsProteinsRNACross-Linking ReagentsHumansAmino AcidsCross-Linking ReagentsProteinsRNAGenetic code expansionRNA‐binding proteinsRNA crosslinkingUnnatural amino acids

Identifiers

PMID41388880
PMCPMC12865153

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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 Socratic graph.