Evidence map›Paper›PMID 32616332›Full record

ArticleTrends in biochemical sciences2020

ER-associated Protein Degradation at Atomic Resolution.

Mohamed A Eldeeb, Richard P Fahlman, Marek Michalak

Abstract readComment
PubMed Publisher
In one paragraph

Article in Trends in biochemical sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Mohamed A EldeebMcGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, H3A 2B4, Canada. Electronic address: mohamed.eldeeb@mcgill.ca.
Richard P FahlmanDepartment of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. Electronic address: rfahlman@ualberta.ca.
Marek MichalakDepartment of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. Electronic address: marek.michalak@ualberta.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum-associated degradation (ERAD) pathway eliminates misfolded proteins. The Hrd1 complex represents the main gate mediating retrotranslocation of ER luminal misfolded (ERAD-L) substrates to the cytosol. A recent cryo-electron microscopy (cryo-EM) study by Wu et al. unveils the structural features of active Hrd1, providing mechanistic insights into the movement of proteins directed for degradation across ER membranes.

Indexed as

Cryoelectron MicroscopyEndoplasmic Reticulum-Associated DegradationEndoplasmic ReticulumProteolysisUbiquitin-Protein LigasesUbiquitinsUbiquitin-Protein LigasesUbiquitinscryo-EMendoplasmic reticulumERADHRD1 complexproteasomeprotein degradationprotein quality controlubiquitin

Identifiers

PMID32616332

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.