Evidence map›Paper›PMID 22004789›Full record

ArticleThe Biochemical journal2012

Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes.

Roland Hjerpe, Yann Thomas, Jesse Chen, Aleksandra Zemla, Siobhan Curran, Natalia Shpiro, Lawrence R Dick, Thimo Kurz

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

72 citing papers in PubMed, 106 citations in OpenAlex.

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  12. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  13. The Ubiquitin-like Proteins ofBiomolecules · 2023
    Review
  14. Chemical Synthesis of Non-hydrolyzable Ubiquitin(-Like) Hybrid Chains.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Article
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  20. Review

12 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

8 authors at 2 institutions in 2 countries.

Roland HjerpeScottish Institute for Cell Signalling, Protein Ubiquitylation Unit, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.
Yann Thomas
Jesse Chen
Aleksandra Zemla
Siobhan Curran
Natalia Shpiro
Lawrence R Dick
Thimo Kurz
University of Dundee · GBMillennium Engineering and Integration (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin and UBL (ubiquitin-like) modifiers are small proteins that covalently modify other proteins to alter their properties or behaviours. Ubiquitin modification (ubiquitylation) targets many substrates, often leading to their proteasomal degradation. NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8) is the UBL most closely related to ubiquitin, and its best-studied role is the activation of CRLs (cullin-RING ubiquitin ligases) by its conjugation to a conserved C-terminal lysine residue on cullin proteins. The attachment of UBLs requires three UBL-specific enzymes, termed E1, E2 and E3, which are usually well insulated from parallel UBL pathways. In the present study, we report a new mode of NEDD8 conjugation (NEDDylation) whereby the UBL NEDD8 is linked to proteins by ubiquitin enzymes in vivo. We found that this atypical NEDDylation is independent of classical NEDD8 enzymes, conserved from yeast to mammals, and triggered by an increase in the NEDD8 to ubiquitin ratio. In cells, NEDD8 overexpression leads to this type of NEDDylation by increasing the concentration of NEDD8, whereas proteasome inhibition has the same effect by depleting free ubiquitin. We show that bortezomib, a proteasome inhibitor used in cancer therapy, triggers atypical NEDDylation in tissue culture, which suggests that a similar process may occur in patients receiving this treatment.

Indexed as

AnimalsBoronic AcidsBortezomibCells, CulturedCHO CellsCricetinaeCricetulusEnzyme InhibitorsHEK293 CellsHeLa CellsHumansNEDD8 ProteinPyrazinesTransfectionUbiquitinUbiquitinationBoronic AcidsBortezomibEnzyme InhibitorsNEDD8 ProteinNEDD8 protein, humanPyrazinesUbiquitinUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID22004789
PMCPMC3280039
OpenAlexW2168588242

What OpenQuestion holds

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LicenceCC BY-NC
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.