Evidence map›Paper›PMID 31530095›Full record

ReviewOpen biology2019

Cellular functions and molecular mechanisms of non-lysine ubiquitination.

Amie J McClellan, Sophie Heiden Laugesen, Lars Ellgaard

Abstract readReview
In one paragraph

Review in Open biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed, 1 pooled it
–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

99 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Squalene Epoxidase: Its Regulations and Links with Cancers.International journal of molecular sciences · 2024
    Pooled it
  2. Article
  3. Plants (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Computational Pipelines for Protein Ubiquitylation Analysis and Prediction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Article
  7. Review
  8. Proteostasis of immune checkpoint receptors.The Biochemical journal · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. CXXC5 is a ubiquitinated protein and is degraded by the ubiquitin-proteasome pathway.Protein science : a publication of the Protein Society · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Emerging roles for E3 ubiquitin ligases in neural development and disease.Frontiers in cell and developmental biology · 2025
    Review

39 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.

Amie J McClellanDivision of Science and Mathematics, Bennington College, 1 College Drive, Bennington, VT 05201, USA.
Sophie Heiden LaugesenDepartment of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen N, Denmark.
Lars EllgaardDepartment of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen N, Denmark.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein ubiquitination is of great cellular importance through its central role in processes such as degradation, DNA repair, endocytosis and inflammation. Canonical ubiquitination takes place on lysine residues, but in the past 15 years non-lysine ubiquitination on serine, threonine and cysteine has been firmly established. With the emerging importance of non-lysine ubiquitination, it is crucial to identify the responsible molecular machinery and understand the mechanistic basis for non-lysine ubiquitination. Here, we first provide an overview of the literature that has documented non-lysine ubiquitination. Informed by these examples, we then discuss the molecular mechanisms and cellular implications of non-lysine ubiquitination, and conclude by outlining open questions and future perspectives in the field.

Indexed as

UbiquitinationAnimalsEndoplasmic ReticulumHumansLysineProteasome Endopeptidase ComplexProteinsSubstrate SpecificityUbiquitinUbiquitin-Protein LigasesLysineProteasome Endopeptidase ComplexProteinsUbiquitinUbiquitin-Protein Ligasesendoplasmic reticulum-associated degradationMARCH E3 ligasesprotein degradationserine/threonine ubiquitinationubiquitin–proteasome system

Identifiers

PMID31530095
PMCPMC6769291

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.