Evidence map›Paper›PMID 32929246›Full record

ArticleNature chemistry2020

Lysine acylation using conjugating enzymes for site-specific modification and ubiquitination of recombinant proteins.

Raphael Hofmann, Gaku Akimoto, Thomas G Wucherpfennig, Cathleen Zeymer, Jeffrey W Bode

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.8field-weighted citation impact, top 5% of its field
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

36 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
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  8. Highly Efficient Transpeptidase-Catalyzed Isopeptide Ligation.Journal of the American Chemical Society · 2025
    Article
  9. Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.Chembiochem : a European journal of chemical biology · 2024
    Article
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  11. Article
  12. Article
  13. Review
  14. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 2 countries.

Raphael HofmannLaboratorium für Organische Chemie, Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-9769-6555
Gaku AkimotoLaboratorium für Organische Chemie, Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0003-0060-6793
Thomas G WucherpfennigLaboratorium für Organische Chemie, Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland.
Cathleen ZeymerLaboratorium für Organische Chemie, Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-7138-381X
Jeffrey W BodeLaboratorium für Organische Chemie, Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland. bode@org.chem.ethz.ch.ORCID http://orcid.org/0000-0001-8394-8910
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes are powerful tools for protein labelling due to their specificity and mild reaction conditions. Many protocols, however, are restricted to modifications at protein termini, rely on non-peptidic metabolites or require large recognition domains. Here we report a chemoenzymatic method, which we call lysine acylation using conjugating enzymes (LACE), to site-specifically modify folded proteins at internal lysine residues. LACE relies on a minimal genetically encoded tag (four residues) recognized by the E2 small ubiquitin-like modifier-conjugating enzyme Ubc9, and peptide or protein thioesters. Together, this approach obviates the need for E1 and E3 enzymes, enabling isopeptide formation with just Ubc9 in a programmable manner. We demonstrate the utility of LACE by the site-specific attachment of biochemical probes, one-pot dual-labelling in combination with sortase, and the conjugation of wild-type ubiquitin and ISG15 to recombinant proteins.

Indexed as

AcylationAmino Acid SequenceBinding SitesLysineLysine AcetyltransferasesModels, MolecularProtein BindingProtein EngineeringRecombinant ProteinsSubstrate SpecificityUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9LysineLysine AcetyltransferasesRecombinant ProteinsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID32929246
OpenAlexW3086598145

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.