Evidence map›Paper›PMID 33578803›Full record

ReviewBiomolecules2021

Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma.

Katharina F Witting, Monique P C Mulder

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Ubiquitin-proteasome system in the different stages of dominantly inherited Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  5. The multifaceted roles of E3 ubiquitin ligases in osteoarthritis.Frontiers in cell and developmental biology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Overexpression of UBA5 in Cells Mimics the Phenotype of Cells Lacking UBA5.International journal of molecular sciences · 2022
    Article
  18. Article
  19. Review
  20. Review
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 1 institution in 1 country.

Katharina F WittingOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center LUMC, Einthovenweg 20, 2333 ZC Leiden, The Netherlands.
Monique P C MulderOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center LUMC, Einthovenweg 20, 2333 ZC Leiden, The Netherlands.ORCID 0000-0001-5386-7132
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modification with Ubiquitin-like proteins represents a complex signaling language regulating virtually every cellular process. Among these post-translational modifiers is Ubiquitin-fold modifier (UFM1), which is covalently attached to its substrates through the orchestrated action of a dedicated enzymatic cascade. Originally identified to be involved embryonic development, its biological function remains enigmatic. Recent research reveals that UFM1 regulates a variety of cellular events ranging from DNA repair to autophagy and ER stress response implicating its involvement in a variety of diseases. Given the contribution of UFM1 to numerous pathologies, the enzymes of the UFM1 cascade represent attractive targets for pharmacological inhibition. Here we discuss the current understanding of this cryptic post-translational modification especially its contribution to disease as well as expand on the unmet needs of developing chemical and biochemical tools to dissect its role.

Indexed as

Gene Expression RegulationAnimalsAutophagyCell SurvivalCysteine EndopeptidasesDNA DamageDNA RepairEndoplasmic Reticulum StressHumansMiceProtein BindingProtein Processing, Post-TranslationalProteinsSignal TransductionSubstrate SpecificityUbiquitinCysteine EndopeptidasesProteinsUbiquitinUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUFC1 protein, humanUFL1 protein, humanUFL1 protein, mouseUFM1 protein, humanUfm1 protein, mouseUfSP1 protein, mouseUfSP2 protein, mouseactivity-based probessubstratesUbiquitin-like modifiersUFM1

Identifiers

PMID33578803
PMCPMC7916544
OpenAlexW3127862737

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.