Evidence map›Paper›PMID 22820888›Full record

ReviewNature reviews. Molecular cell biology2012

Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages.

Yogesh Kulathu, David Komander

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 370 papers.

0numbers the graph read from it
0cells of the map it votes in
370citing 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

370 citing papers in PubMed.

  1. Article
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  5. Review
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  8. Review
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  10. Review
  11. Article
  12. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

310 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

2 authors.

Yogesh KulathuMedical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.
David Komander

Funding

Medical Research Council MC_U105192732
6 · The paper itself

Abstract

Ubiquitylation is one of the most abundant and versatile post-translational modifications (PTMs) in cells. Its versatility arises from the ability of ubiquitin to form eight structurally and functionally distinct polymers, in which ubiquitin moieties are linked via one of seven Lys residues or the amino terminus. Whereas the roles of Lys48- and Lys63-linked polyubiquitin in protein degradation and cellular signalling are well characterized, the functions of the remaining six 'atypical' ubiquitin chain types (linked via Lys6, Lys11, Lys27, Lys29, Lys33 and Met1) are less well defined. Recent developments provide insights into the mechanisms of ubiquitin chain assembly, recognition and hydrolysis and allow detailed analysis of the functions of atypical ubiquitin chains. The importance of Lys11 linkages and Met1 linkages in cell cycle regulation and nuclear factor-κB activation, respectively, highlight that the different ubiquitin chain types should be considered as functionally independent PTMs.

Indexed as

Cell CycleLysinePolyubiquitinUbiquitinationHumansHydrolysisNF-kappa BProteasome Endopeptidase ComplexProteolysisSignal TransductionUbiquitin-Protein LigasesLysineNF-kappa BPolyubiquitinProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID22820888

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.