Evidence map›Paper›PMID 23209158›Full record

ReviewCold Spring Harbor perspectives in biology2012

The endoplasmic reticulum-associated degradation pathways of budding yeast.

Guillaume Thibault, Davis T W Ng

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Functions ofJournal of fungi (Basel, Switzerland) · 2025
    Review
  2. Evolutionary uniqueeLife · 2025
    Article
  3. Microorganisms · 2024
    Review
  4. Article
  5. Effect ofMolecules (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Proline Homeostasis inFrontiers in genetics · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Putative Interaction Proteins of the Ubiquitin Ligase Hrd1 inEvolutionary bioinformatics online · 2018
    Article
  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

2 authors.

Guillaume ThibaultTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604.
Davis T W Ng

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding is a common cellular event that can produce intrinsically harmful products. To reduce the risk, quality control mechanisms are deployed to detect and eliminate misfolded, aggregated, and unassembled proteins. In the secretory pathway, it is mainly the endoplasmic reticulum-associated degradation (ERAD) pathways that perform this role. Here, specialized factors are organized to monitor and process the folded states of nascent polypeptides. Despite the complex structures, topologies, and posttranslational modifications of client molecules, the ER mechanisms are the best understood among all protein quality-control systems. This is the result of convergent and sometimes serendipitous discoveries by researchers from diverse fields. Although major advances in ER quality control and ERAD came from all model organisms, this review will focus on the discoveries culminating from the simple budding yeast.

Indexed as

Models, BiologicalProtein FoldingProteolysisEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationProteasome Endopeptidase ComplexSaccharomycetalesSubstrate SpecificityUbiquitinationUbiquitin-Protein LigasesProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID23209158
PMCPMC3504435

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.