Evidence map›Paper›PMID 32588820›Full record

ArticleeLife2020

Doa10 is a membrane protein retrotranslocase in ER-associated protein degradation.

Claudia C Schmidt, Vedran Vasic, Alexander Stein

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

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  17. Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023
    Review
  18. Article
  19. The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023
    Review
  20. 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 1 institution in 2 countries.

Claudia C SchmidtResearch Group Membrane Protein Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-7642-7081
Vedran VasicResearch Group Membrane Protein Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-2575-1006
Alexander SteinResearch Group Membrane Protein Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-2696-0611
MRC Laboratory of Molecular Biology · GB

Funding

Deutsche Forschungsgemeinschaft SFB1190, TP15H2020 European Research Council 677770
6 · The paper itself

Abstract

In endoplasmic reticulum-associated protein degradation (ERAD), membrane proteins are ubiquitinated, extracted from the membrane, and degraded by the proteasome. The cytosolic ATPase Cdc48 drives extraction by pulling on polyubiquitinated substrates. How hydrophobic transmembrane (TM) segments are moved from the phospholipid bilayer into cytosol, often together with hydrophilic and folded ER luminal protein parts, is not known. Using a reconstituted system with purified proteins from

Indexed as

Endoplasmic Reticulum-Associated DegradationMembrane ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesMembrane ProteinsSaccharomyces cerevisiae ProteinsSSM4 protein, S cerevisiaeUbiquitin-Protein Ligasesbiochemistrycell biologychemical biologyERADin vitro reconstitutionmembrane proteinsprotein quality controlprotein translocationS. cerevisiaeubiquitin proteasome system

Identifiers

PMID32588820
PMCPMC7319771
OpenAlexW3037410272

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.