Evidence map›Paper›PMID 36794017›Full record

ArticleRSC chemical biology2023

The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy.

Yeke Ni, Yu Wang, Alethea B Tabor, John M Ward, Helen C Hailes

Abstract read
In one paragraph

Article in RSC chemical biology, 2023. 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.

Yeke NiDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.
Yu WangDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.
Alethea B TaborDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0001-8216-0347
John M WardDepartment of Biochemical Engineering, University College London Bernard Katz Building, Gower Street London WC1E 6BT UK.ORCID https://orcid.org/0000-0002-4415-5544
Helen C HailesDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0001-5574-4742

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptides play many key roles in biological systems and numerous methods have been developed to generate both natural and unnatural peptides. However, straightforward, reliable coupling methods that can be achieved under mild reactions conditions are still sought after. In this work, a new N-terminal tyrosine-containing peptide ligation method with aldehydes, utilising a Pictet-Spengler reaction is described. In a key step, tyrosinase enzymes have been used to convert l-tyrosine to l-3,4-dihydroxyphenyl alanine (l-DOPA) residues, generating suitable functionality for the Pictet-Spengler coupling. This new chemoenzymatic coupling strategy can be used for fluorescent-tagging and peptide ligation purposes.

Identifiers

PMID36794017
PMCPMC9906322

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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.