Evidence map›Paper›PMID 42266596›Full record

ReviewBeilstein journal of organic chemistry2026

Site-specific labelling of native peptides and proteins: chemical and enzymatic strategies.

Antonio Angelastro, Jonathan Bargh, Subhajit Guria, Victor Laserna, Louis Luk

Abstract readReview
In one paragraph

Review in Beilstein journal of organic chemistry, 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

5 authors.

Antonio AngelastroBiologics Engineering, Oncology R&D, Cambridge Biomedical Campus, AstraZeneca, 1 Francis Crick Ave, Trumpington, Cambridge, CB2 0AA, UK.ORCID https://orcid.org/0000-0002-4023-7411
Jonathan BarghHit Discovery, Discovery Sciences, R&D, AstraZeneca, Pepparedsleden 1, Mölndal, Gothenburg, 43183, Sweden.ORCID https://orcid.org/0000-0003-3023-2569
Subhajit GuriaInterdisciplinary Research Center, Division of Interdisciplinary Science, Institute for Radiation Sciences, The University of Osaka, 1-2 Machikaneyama-cho, Toyonaka 560-0043, Osaka, Japan.ORCID https://orcid.org/0000-0002-5754-6157
Victor LasernaBiologics Engineering, Oncology R&D, Cambridge Biomedical Campus, AstraZeneca, 1 Francis Crick Ave, Trumpington, Cambridge, CB2 0AA, UK.ORCID https://orcid.org/0000-0003-2951-9327
Louis LukSchool of Chemistry and Cardiff Catalysis Institute, Cardiff University Main Building, Park Pl, Cardiff, CF10 3AT, UK.ORCID https://orcid.org/0000-0002-7864-6261

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Site-specific modifications of native-sequence proteins are technologies that underpin progresses in chemical biology, diagnostics and next-generation biotherapeutics. However, the pursuit of site-specificity has often come at the expense of scalability and usability, ultimately limiting translational potential of a modification tool. This review critically compares current key strategies, including terminal, disulfide-rebridging, small-molecule, glycan and enzyme-based modifications. Finally, we present a decision tree for method selection and highlight opportunities for innovation in next-generation native-sequence protein modification technologies.

Indexed as

affinity-guided chemistrydisulfide-rebridgingenzyme catalysisglycan modificationsnative-sequenceprotein labellingsmall-molecule modificationsterminal

Identifiers

PMID42266596
PMCPMC13245474

What Socratic holds

Textmetadata
LicenceCC BY
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.