Evidence map›Paper›PMID 21655279›Full record

ArticlePloS one2011

The essential functions of NEDD8 are mediated via distinct surface regions, and not by polyneddylation in Schizosaccharomyces pombe.

David Girdwood, Dimitris P Xirodimas, Colin Gordon

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Protein neddylation: beyond cullin-RING ligases.Nature reviews. Molecular cell biology · 2015
    Review
  7. The NEDD8 modification pathway in plants.Frontiers in plant science · 2014
    Review
  8. Article
  9. 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

3 authors at 3 institutions in 1 country.

David GirdwoodMedical Research Council Human Genetics Unit, Western General Hospital, Edinburgh, Scotland, United Kingdom. davidgirdwood@gmail.com
Dimitris P Xirodimas
Colin Gordon
Medical Research Council · GBMRC Human Genetics UnitWellcome Trust · GB

Funding

Medical Research Council MC_U127584486
6 · The paper itself

Abstract

The ubiquitin-like protein NEDD8 is highly conserved in eukaryotes, from man to Schizosaccharomyces pombe. NEDD8 conjugation to cullin proteins is a prerequisite for cullin based E3 ubiquitin ligase activity, and essential for S. pombe viability. Here, we have performed alanine scanning mutagenesis of all conserved surface residues and show that the majority of essential residues were located around the hydrophobic patch and the C-terminus. However, we further identified essential residues not previously reported to be involved in ubiquitin ligase regulation that importantly do not prevent Ned8p conjugation. We also find that mutation of all conserved lysine residues in Ned8p, did not affect yeast viability, suggesting that mono-neddylation is sufficient for yeast viability under most conditions.

Indexed as

Cell SurvivalProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsUbiquitinsSchizosaccharomyces pombe ProteinsUbiquitins

Identifiers

PMID21655279
PMCPMC3105002
OpenAlexW2052779337

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.