Evidence map›Paper›PMID 38505698›Full record

ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2022

Expressed Protein Selenoester Ligation.

Sameer S Kulkarni, Emma E Watson, Joshua W C Maxwell, Gerhard Niederacher, Jason Johansen-Leete, Susanne Huhmann, Somnath Mukherjee, Alexander R Norman, Julia Kriegesmann, Christian F W Becker and 1 more

Abstract read
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In one paragraph

Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

11 authors.

Sameer S KulkarniSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Sydney Sydney NSW 2006 Australia.ORCID 0000-0001-5896-9568
Emma E WatsonSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Sydney Sydney NSW 2006 Australia.ORCID 0000-0001-5946-473X
Joshua W C MaxwellSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Sydney Sydney NSW 2006 Australia.ORCID 0000-0003-1481-370X
Gerhard NiederacherFaculty of Chemistry, Institute of Biological Chemistry University of Vienna Vienna Austria.
Jason Johansen-LeeteSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Sydney Sydney NSW 2006 Australia.
Susanne HuhmannFaculty of Chemistry, Institute of Biological Chemistry University of Vienna Vienna Austria.ORCID 0000-0001-5519-3426
Somnath MukherjeeFaculty of Chemistry, Institute of Biological Chemistry University of Vienna Vienna Austria.
Alexander R NormanSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Sydney Sydney NSW 2006 Australia.ORCID 0000-0001-7908-0135
Julia KriegesmannFaculty of Chemistry, Institute of Biological Chemistry University of Vienna Vienna Austria.ORCID 0000-0003-3852-5147
Christian F W BeckerFaculty of Chemistry, Institute of Biological Chemistry University of Vienna Vienna Austria.ORCID 0000-0002-8890-7082
Richard J PayneSchool of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science The University of Sydney Sydney NSW 2006 Australia.ORCID 0000-0002-3618-9226

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herein, we describe the development and application of a novel expressed protein selenoester ligation (EPSL) methodology for the one-pot semi-synthesis of modified proteins. EPSL harnesses the rapid kinetics of ligation reactions between modified synthetic selenopeptides and protein aryl selenoesters (generated from expressed intein fusion precursors) followed by in situ chemoselective deselenization to afford target proteins at concentrations that preclude the use of traditional ligation methods. The utility of the EPSL technology is showcased through the efficient semi-synthesis of ubiquitinated polypeptides, lipidated analogues of the membrane-associated GTPase YPT6, and site-specifically phosphorylated variants of the oligomeric chaperone protein Hsp27 at high dilution.

Indexed as

Expressed Protein SelenoestersPeptidesProtein ModificationsProteinsProtein Semi-Synthesis

Identifiers

PMID38505698
PMCPMC10947028

What OpenQuestion holds

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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 OpenQuestion graph.