Evidence map›Paper›PMID 32094691›Full record

ArticleNature cell biology2020

Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins.

Vedran Vasic, Niels Denkert, Claudia C Schmidt, Dietmar Riedel, Alexander Stein, Michael Meinecke

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  6. Competition between Der1 and ERAD-M substrates controls Hrd1 complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  8. Article
  9. Article
  10. Review
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  12. Article
  13. ER-associated degradation ligase HRD1 links ER stress to DNA damage repair by modulating the activity of DNA-PKcs.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  14. Review
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Vedran Vasic *Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Niels Denkert *Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0002-2551-0360
Claudia C SchmidtMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Dietmar RiedelDepartment of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Alexander SteinMax Planck Institute for Biophysical Chemistry, Göttingen, Germany. alexander.stein@mpibpc.mpg.de.ORCID http://orcid.org/0000-0002-2696-0611
Michael MeineckeDepartment of Cellular Biochemistry, University Medical Centre Göttingen, Göttingen, Germany. michael.meinecke@med.uni-goettingen.de.ORCID http://orcid.org/0000-0003-1414-6951
Max Planck Institute for Biophysical Chemistry · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During endoplasmic-reticulum-associated protein degradation (ERAD), misfolded proteins are polyubiquitinated, extracted from the ER membrane and degraded by the proteasome

Indexed as

Endoplasmic Reticulum-Associated DegradationProtein FoldingUbiquitinationBinding SitesCarboxypeptidasesCell MembraneElectrophysiological PhenomenaProtein DomainsProtein TransportSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesCarboxypeptidasesCPY protein, S cerevisiaeHRD1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID32094691
OpenAlexW3008769615

What OpenQuestion holds

Textmetadata
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.