Evidence map›Paper›PMID 37528230›Full record

ReviewNature reviews. Molecular cell biology2023

Mechanisms of substrate processing during ER-associated protein degradation.

John C Christianson, Ernst Jarosch, Thomas Sommer

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed, 1 pooled it
32.1field-weighted citation impact, top 1% 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

110 citing papers in PubMed, 1 synthesis or guideline pooled it, 154 citations in OpenAlex.

  1. Squalene Epoxidase: Its Regulations and Links with Cancers.International journal of molecular sciences · 2024
    Pooled it
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  11. Cell autonomous inflammation in VEXAS is mediated by cGAS-STING.bioRxiv : the preprint server for biology · 2026
    Article
  12. Review
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  16. CDS-localized mNature plants · 2026
    Article
  17. Article
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  20. The Effect and Molecular Mechanism ofCurrent issues in molecular biology · 2026
    Article

50 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

John C ChristiansonBotnar Research Centre, Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, University of Oxford, Oxford, UK. john.christianson@ndorms.ox.ac.uk.
Ernst JaroschMax-Delbrück-Centrer for Molecular Medicine in Helmholtz Association, Berlin-Buch, Germany.
Thomas SommerMax-Delbrück-Centrer for Molecular Medicine in Helmholtz Association, Berlin-Buch, Germany. tsommer@mdc-berlin.de.ORCID 0000-0001-9990-5202
Max Delbrück Center · DENuffield Orthopaedic Centre · GB

Funding

Cancer Research UK 29217
6 · The paper itself

Abstract

Maintaining proteome integrity is essential for long-term viability of all organisms and is overseen by intrinsic quality control mechanisms. The secretory pathway of eukaryotes poses a challenge for such quality assurance as proteins destined for secretion enter the endoplasmic reticulum (ER) and become spatially segregated from the cytosolic machinery responsible for disposal of aberrant (misfolded or otherwise damaged) or superfluous polypeptides. The elegant solution provided by evolution is ER-membrane-bound ubiquitylation machinery that recognizes misfolded or surplus proteins or by-products of protein biosynthesis in the ER and delivers them to 26S proteasomes for degradation. ER-associated protein degradation (ERAD) collectively describes this specialized arm of protein quality control via the ubiquitin-proteasome system. But, instead of providing a single strategy to remove defective or unwanted proteins, ERAD represents a collection of independent processes that exhibit distinct yet overlapping selectivity for a wide range of substrates. Not surprisingly, ER-membrane-embedded ubiquitin ligases (ER-E3s) act as central hubs for each of these separate ERAD disposal routes. In these processes, ER-E3s cooperate with a plethora of specialized factors, coordinating recognition, transport and ubiquitylation of undesirable secretory, membrane and cytoplasmic proteins. In this Review, we focus on substrate processing during ERAD, highlighting common threads as well as differences between the many routes via ERAD.

Indexed as

Endoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationUbiquitinationAnimalsHumansProteasome Endopeptidase ComplexProtein FoldingProteolysisUbiquitin-Protein LigasesProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID37528230
OpenAlexW4385463105

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.