Evidence map›Paper›PMID 26085216›Full record

ReviewImmunological reviews2015

Linear ubiquitination in immunity.

Yutaka Shimizu, Lucia Taraborrelli, Henning Walczak

Open access · hybridAbstract readReview
In one paragraph

Review in Immunological reviews, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. LUBAC is required for RIG-I sensing of RNA viruses.Cell death and differentiation · 2024
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. HOIP modulates the stability of GPx4 by linear ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Article

27 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 1 institution in 1 country.

Yutaka ShimizuCentre for Cell Death, Cancer, and Inflammation (CCCI), UCL Cancer Institute, University College London, London, UK.
Lucia TaraborrelliCentre for Cell Death, Cancer, and Inflammation (CCCI), UCL Cancer Institute, University College London, London, UK.
Henning WalczakCentre for Cell Death, Cancer, and Inflammation (CCCI), UCL Cancer Institute, University College London, London, UK.
University College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Linear ubiquitination is a post-translational protein modification recently discovered to be crucial for innate and adaptive immune signaling. The function of linear ubiquitin chains is regulated at multiple levels: generation, recognition, and removal. These chains are generated by the linear ubiquitin chain assembly complex (LUBAC), the only known ubiquitin E3 capable of forming the linear ubiquitin linkage de novo. LUBAC is not only relevant for activation of nuclear factor-κB (NF-κB) and mitogen-activated protein kinases (MAPKs) in various signaling pathways, but importantly, it also regulates cell death downstream of immune receptors capable of inducing this response. Recognition of the linear ubiquitin linkage is specifically mediated by certain ubiquitin receptors, which is crucial for translation into the intended signaling outputs. LUBAC deficiency results in attenuated gene activation and increased cell death, causing pathologic conditions in both, mice, and humans. Removal of ubiquitin chains is mediated by deubiquitinases (DUBs). Two of them, OTULIN and CYLD, are constitutively associated with LUBAC. Here, we review the current knowledge on linear ubiquitination in immune signaling pathways and the biochemical mechanisms as to how linear polyubiquitin exerts its functions distinctly from those of other ubiquitin linkage types.

Indexed as

AnimalsCell DeathDeubiquitinating Enzyme CYLDEndopeptidasesHumansImmunityMiceMitogen-Activated Protein Kinase KinasesMultiprotein ComplexesNF-kappa BProtein Processing, Post-TranslationalSignal TransductionTumor Suppressor ProteinsUbiquitinationCYLD protein, humanDeubiquitinating Enzyme CYLDEndopeptidasesMitogen-Activated Protein Kinase KinasesMultiprotein ComplexesNF-kappa BOTULIN protein, humanTumor Suppressor Proteinscell deathdeubiquitinasesinflammationlinear ubiquitinationsignaling pathways

Identifiers

PMID26085216
PMCPMC4737190
OpenAlexW1523475366

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.