Evidence map›Paper›PMID 23563141›Full record

ArticleNature structural & molecular biology2013

Assembly, analysis and architecture of atypical ubiquitin chains.

Manuela K Hospenthal, Stefan M V Freund, David Komander

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

84 citing papers in PubMed, 151 citations in OpenAlex.

  1. AmideBiomolecular NMR assignments · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. The Ubiquitin Tale: Current Strategies and Future Challenges.ACS pharmacology & translational science · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Bacterial mimicry of eukaryotic HECT ubiquitin ligation.bioRxiv : the preprint server for biology · 2023
    Article
  13. Proteomic approaches to study ubiquitinomics.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Review
  14. An expanded lexicon for the ubiquitin code.Nature reviews. Molecular cell biology · 2023
    Review
  15. Article
  16. Article
  17. Assembly and disassembly of branched ubiquitin chains.Frontiers in molecular biosciences · 2023
    Review
  18. Review
  19. Review
  20. Review

24 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Manuela K HospenthalMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Stefan M V Freund
David Komander
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

European Research Council 309756Medical Research Council MC_U105192732Medical Research Council U.1051.03.019.00001.01(92732)Medical Research Council U105192732
6 · The paper itself

Abstract

Ubiquitin (Ub) chains regulate many cellular processes, but several chain types including Lys6 linkages have remained unstudied. Here we analyze the bacterial effector E3 ligase NleL (non-Lee-encoded effector ligase) from enterohemorrhagic Escherichia coli (EHEC) O157:H7, which assembles Lys6- and Lys48-linked Ub polymers. Using linkage-specific human deubiquitinases (DUBs) we show that NleL generates heterotypic Ub chains, and branched chains are efficiently hydrolyzed by DUBs. USP family DUBs cleave Lys6-linked polymers exclusively from the distal end, whereas a DUB with preference for Lys6 can cleave Lys6-linked polymers at any position in the chain. We used NleL to generate large quantities of Lys6-linked polyUb. Crystallographic and NMR spectroscopy analyses revealed that an asymmetric interface between Ile44 and Ile36 hydrophobic patches of neighboring Ub moieties is propagated in longer Lys6-linked Ub chains. Interactions via the Ile36 patch can displace Leu8 from the Ile44 patch, leading to marked structural perturbations of Ub.

Indexed as

Crystallography, X-RayEndopeptidasesEscherichia coli O157Escherichia coli ProteinsHumansMagnetic Resonance SpectroscopyModels, MolecularProtein ConformationUbiquitin-Protein LigasesEndopeptidasesEscherichia coli ProteinsNleL protein, E coliUbiquitin-Protein Ligases

Identifiers

PMID23563141
PMCPMC4176834
OpenAlexW2147363233

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.