Evidence map›Paper›PMID 27044894›Full record

ArticleThe Journal of cell biology2016

Doa1 is a MAD adaptor for Cdc48.

Ting Zhang, Yihong Ye

Open access · bronzeAbstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 42% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
  3. Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion.International journal of molecular sciences · 2020
    Review
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Ting ZhangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Yihong YeLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 yihongy@mail.nih.gov.
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Mechanism of protein retro-translocation from the endoplasmic reticulumZIADK033008 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2010 to 2025
$9.3M
6 · The paper itself

Abstract

Dislocation of polypeptides from the mitochondrial outer membrane by the p97/Cdc48-Ufd1-Npl4 adenosine triphosphatase complex is essential for mitochondria-associated degradation and Parkin-mediated mitophagy. In this issue, Wu et al. (2016.J. Cell Biol.http://dx.doi.org/10.1083/jcb.201510098) identify Doa1 as a pivotal adaptor that recruits substrates to Cdc48 for processing.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsHumansPeptidesSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCell Cycle ProteinsPeptidesSaccharomyces cerevisiae Proteins

Identifiers

PMID27044894
PMCPMC4828697
OpenAlexW2328840809

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.