Evidence map›Paper›PMID 26862208›Full record

ReviewBiochemical Society transactions2016

Specificity and disease in the ubiquitin system.

Viduth K Chaugule, Helen Walden

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Selective Lysine Ubiquitination Using Activated Phenol Esters.Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Expanding the inhibitor space of the WWP1 and WWP2 HECT E3 ligases.Journal of enzyme inhibition and medicinal chemistry · 2024
    Article
  10. Regulation of the Inflammasome Activation by Ubiquitination Machinery.Advances in experimental medicine and biology · 2024
    Review
  11. Review
  12. Review
  13. Article
  14. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    Review
  15. PARK2 regulates eIF4B-driven lymphomagenesis.Molecular cancer research : MCR · 2022
    Article
  16. Article
  17. The Downregulation of Both Giant HERCs,Journal of clinical medicine · 2022
    Article
  18. Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022
    Review
  19. Review
  20. Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
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.

Viduth K ChauguleMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, DD1 5EH, U.K.
Helen WaldenMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, DD1 5EH, U.K. h.walden@dundee.ac.uk.
MRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Cancer Research UK 17739Medical Research Council MC_UU_12016/12
6 · The paper itself

Abstract

Post-translational modification (PTM) of proteins by ubiquitination is an essential cellular regulatory process. Such regulation drives the cell cycle and cell division, signalling and secretory pathways, DNA replication and repair processes and protein quality control and degradation pathways. A huge range of ubiquitin signals can be generated depending on the specificity and catalytic activity of the enzymes required for attachment of ubiquitin to a given target. As a consequence of its importance to eukaryotic life, dysfunction in the ubiquitin system leads to many disease states, including cancers and neurodegeneration. This review takes a retrospective look at our progress in understanding the molecular mechanisms that govern the specificity of ubiquitin conjugation.

Indexed as

DiseaseAnimalsFanconi AnemiaHumansParkinson DiseaseSubstrate SpecificityUbiquitinUbiquitin-Protein LigasesUbiquitinUbiquitin-Protein LigasesE3 ligaseFanconi anemiaParkinRBRRINGubiquitin

Identifiers

PMID26862208
PMCPMC5264512
OpenAlexW2307933984

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.