Evidence map›Paper›PMID 28446710›Full record

ReviewOpen biology2017

Linear ubiquitin chains: enzymes, mechanisms and biology.

Katrin Rittinger, Fumiyo Ikeda

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. E2 variants for probing E3 ubiquitin ligase activities.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Repressive Control of Keratinocyte Cytoplasmic Inflammatory Signaling.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Atypical Ubiquitination and Parkinson's Disease.International journal of molecular sciences · 2022
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022
    Review

3 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 at 2 institutions in 2 countries.

Katrin RittingerMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK katrin.rittinger@crick.ac.uk.ORCID 0000-0002-7698-4435
Fumiyo IkedaInstitute of Molecular Biotechnology (IMBA), Dr Bohr-gasse 3, 1030 Vienna, Austria fumiyo.ikeda@imba.oeaw.ac.at.ORCID 0000-0003-0407-2768
Institute of Molecular Biotechnology · ATThe Francis Crick Institute · GB

Funding

European Research Council 614711Medical Research Council MC_U117565398Wellcome Trust FC001142
6 · The paper itself

Abstract

Ubiquitination is a versatile post-translational modification that regulates a multitude of cellular processes. Its versatility is based on the ability of ubiquitin to form multiple types of polyubiquitin chains, which are recognized by specific ubiquitin receptors to induce the required cellular response. Linear ubiquitin chains are linked through Met 1 and have been established as important players of inflammatory signalling and apoptotic cell death. These chains are generated by a ubiquitin E3 ligase complex called the linear ubiquitin chain assembly complex (LUBAC) that is thus far the only E3 ligase capable of forming linear ubiquitin chains. The complex consists of three subunits, HOIP, HOIL-1L and SHARPIN, each of which have specific roles in the observed biological functions of LUBAC. Furthermore, LUBAC has been found to be associated with OTULIN and CYLD, deubiquitinases that disassemble linear chains and counterbalance the E3 ligase activity of LUBAC. Gene mutations in HOIP, HOIL-1L and OTULIN are found in human patients who suffer from autoimmune diseases, and HOIL-1L mutations are also found in myopathy patients. In this paper, we discuss the mechanisms of linear ubiquitin chain generation and disassembly by their respective enzymes and review our current understanding of their biological functions and association with human diseases.

Indexed as

AnimalsAutoimmune DiseasesHumansPolymorphism, GeneticProtein DomainsProtein SubunitsSignal TransductionThermotoleranceTumor Necrosis FactorsUbiquitinUbiquitinationUbiquitin-Protein LigasesProtein SubunitsTumor Necrosis FactorsUbiquitinUbiquitin-Protein Ligasesimmune responsesinflammatory signallingLUBACOTULINRBR E3 ligasesubiquitin

Identifiers

PMID28446710
PMCPMC5413910
OpenAlexW2609298734

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.