Evidence map›Paper›PMID 34439852›Full record

ReviewBiomolecules2021

The Targeting of Native Proteins to the Endoplasmic Reticulum-Associated Degradation (ERAD) Pathway: An Expanding Repertoire of Regulated Substrates.

Deepa Kumari, Jeffrey L Brodsky

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. FAM134B controls collagen I dynamics in hepatic stellate cell-driven fibrosis.American journal of physiology. Gastrointestinal and liver physiology · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. ER exit in physiology and disease.Frontiers in molecular biosciences · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. A second chance for protein targeting/folding: Ubiquitination and deubiquitination of nascent proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Review
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 at 1 institution in 1 country.

Deepa KumariDepartment of Biological Sciences, University of Pittsburgh, A320 Langley Hall, Fifth & Ruskin Ave, Pittsburgh, PA 15260, USA.
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, A320 Langley Hall, Fifth & Ruskin Ave, Pittsburgh, PA 15260, USA.
University of Pittsburgh · US

Funding

Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CARATTINO, MARCELO DANIEL · 2008 to 2022
$13.4M
Modulating Hsp70-dependent proteostasis in Alzheimer's DiseaseR35GM131732 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JEFFREY L. BRODSKY · 2019 to 2026
$3.4M
NIDDK NIH HHS P30 DK079307NIGMS NIH HHS R35 GM131732NIH HHS DK079307NIH HHS GM131732
6 · The paper itself

Abstract

All proteins are subject to quality control processes during or soon after their synthesis, and these cellular quality control pathways play critical roles in maintaining homeostasis in the cell and in organism health. Protein quality control is particularly vital for those polypeptides that enter the endoplasmic reticulum (ER). Approximately one-quarter to one-third of all proteins synthesized in eukaryotic cells access the ER because they are destined for transport to the extracellular space, because they represent integral membrane proteins, or because they reside within one of the many compartments of the secretory pathway. However, proteins that mature inefficiently are subject to ER-associated degradation (ERAD), a multi-step pathway involving the chaperone-mediated selection, ubiquitination, and extraction (or "retrotranslocation") of protein substrates from the ER. Ultimately, these substrates are degraded by the cytosolic proteasome. Interestingly, there is an increasing number of native enzymes and metabolite and solute transporters that are also targeted for ERAD. While some of these proteins may transiently misfold, the ERAD pathway also provides a route to rapidly and quantitatively downregulate the levels and thus the activities of a variety of proteins that mature or reside in the ER.

Indexed as

Endoplasmic Reticulum-Associated DegradationAnimalsEndoplasmic ReticulumMammalsMolecular ChaperonesProtein FoldingProtein TransportProteolysisUbiquitinUbiquitinationYeastsMolecular ChaperonesUbiquitinERADmolecular chaperonesproteasomeprotein quality controlubiquitin

Identifiers

PMID34439852
PMCPMC8393694
OpenAlexW3187121684

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.