Evidence map›Paper›PMID 19337321›Full record

ArticleNature cell biology2009

Targeting protein ubiquitylation: DDB1 takes its RING off.

Sarah Jackson, Yue Xiong

Abstract readNewsComment
In one paragraph

Article in Nature cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. CRL4Science advances · 2020
    Article
  5. Article
  6. Article
  7. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Sarah Jackson
Yue Xiong

Funding

The Physiological Function and Regulation of INK4 GenesR01CA068377 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MARZLUFF, WILLIAM F. · 1995 to 2021
$6.5M
The ROC-Cullin Family of E3 Ubiquitin LigasesR01GM067113 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI XIONG, YUE · 2003 to 2019
$5.4M
NCI NIH HHS R01 CA068377NIGMS NIH HHS R01 GM067113
6 · The paper itself

Abstract

Ubiquitin E3 ligases of the RING and HECT families are distinct not only in their catalytic mechanisms but also in targeting substrates. Now it seems that one heterodimeric complex can target substrates to both types of E3 ligase.

Indexed as

UbiquitinationAnimalsDNA-Binding ProteinsDyrk KinasesHumansModels, BiologicalProtein Serine-Threonine KinasesProtein-Tyrosine KinasesUbiquitin-Protein LigasesDNA-Binding ProteinsDyrk KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesUbiquitin-Protein Ligases

Identifiers

PMID19337321
PMCPMC4869686

What OpenQuestion holds

Textmetadata
LicenceTDM
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.