Evidence map›Paper›PMID 34764289›Full record

ArticleNature communications2021

A modular toolbox to generate complex polymeric ubiquitin architectures using orthogonal sortase enzymes.

Maximilian Fottner, Maria Weyh, Stefan Gaussmann, Dominic Schwarz, Michael Sattler, Kathrin Lang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.1field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Chemical Biology 2025: Highlights From the Ch/Bi145 Course at Caltech.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Photocatalytic Diselenide Contraction as a Tool for Site-Selective Isosteric Ubiquitylation.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Reading and Writing the Ubiquitin Code Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
  18. Article
  19. Review
  20. 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

6 authors at 3 institutions in 2 countries.

Maximilian FottnerDepartment of Chemistry, Lab for Synthetic Biochemistry, Technical University of Munich, Institute for Advanced Study, TUM-IAS, Lichtenberg Str. 4, 85748, Garching, Germany.
Maria WeyhDepartment of Chemistry, Lab for Synthetic Biochemistry, Technical University of Munich, Institute for Advanced Study, TUM-IAS, Lichtenberg Str. 4, 85748, Garching, Germany.ORCID http://orcid.org/0000-0002-5792-2298
Stefan GaussmannBavarian NMR Center, Department of Chemistry, Technical University of Munich, Lichtenberg Str. 4, 85748, Garching, Germany.ORCID http://orcid.org/0000-0003-0225-5165
Dominic SchwarzDepartment of Chemistry, Lab for Synthetic Biochemistry, Technical University of Munich, Institute for Advanced Study, TUM-IAS, Lichtenberg Str. 4, 85748, Garching, Germany.
Michael SattlerBavarian NMR Center, Department of Chemistry, Technical University of Munich, Lichtenberg Str. 4, 85748, Garching, Germany.
Kathrin LangLaboratory of Organic Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 3, 8093, Zurich, Switzerland. kathrin.lang@org.chem.ethz.ch.ORCID http://orcid.org/0000-0002-1318-6567
ETH Zurich · CHHelmholtz Zentrum München · DEInstitute for Advanced Study · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The post-translational modification of proteins with ubiquitin (Ub) and Ub-like modifiers (Ubls) represents one of the most important regulators in eukaryotic biology. Polymeric Ub/Ubl chains of distinct topologies control the activity, stability, interaction and localization of almost all cellular proteins and elicit a variety of biological outputs. Our ability to characterize the roles of distinct Ub/Ubl topologies and to identify enzymes and receptors that create, recognize and remove these modifications is however hampered by the difficulty to prepare them. Here we introduce a modular toolbox (Ubl-tools) that allows the stepwise assembly of Ub/Ubl chains in a flexible and user-defined manner facilitated by orthogonal sortase enzymes. We demonstrate the universality and applicability of Ubl-tools by generating distinctly linked Ub/Ubl hybrid chains, and investigate their role in DNA damage repair. Importantly, Ubl-tools guarantees straightforward access to target proteins, site-specifically modified with distinct homo- and heterotypic (including branched) Ub chains, providing a powerful approach for studying the functional impact of these complex modifications on cellular processes.

Indexed as

DNA DamageHumansPolymersProtein BindingProtein Processing, Post-TranslationalUbiquitinUbiquitinationPolymersUbiquitin

Identifiers

PMID34764289
PMCPMC8585875
OpenAlexW3213562584

What OpenQuestion 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 OpenQuestion graph.