Evidence map›Paper›PMID 31669350›Full record

ReviewMolecular and cellular endocrinology2020

Disposing of misfolded ER proteins: A troubled substrate's way out of the ER.

Christina Oikonomou, Linda M Hendershot

Open access · greenAbstract readReview
In one paragraph

Review in Molecular and cellular endocrinology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Christina OikonomouSt. Jude Children's Research Hospital, Memphis, TN, 38104, USA; The University of Tennessee Health Science Center, Memphis, TN, USA.
Linda M HendershotSt. Jude Children's Research Hospital, Memphis, TN, 38104, USA; The University of Tennessee Health Science Center, Memphis, TN, USA. Electronic address: linda.hendershot@stjude.org.
St. Jude Children's Research Hospital · US

Funding

Role of Molecular Chaperones in Ig Biosynthesis 11-2008R01GM054068 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI HENDERSHOT, LINDA M · 1996 to 2018
$5.7M
NIGMS NIH HHS R01 GM054068
6 · The paper itself

Abstract

Secreted, plasma membrane, and resident proteins of the secretory pathway are synthesized in the endoplasmic reticulum (ER) where they undergo post-translational modifications, oxidative folding, and subunit assembly in tightly monitored processes. An ER quality control (ERQC) system oversees protein maturation and ensures that only those reaching their native state will continue trafficking into the secretory pathway to reach their final destinations. Those that fail must be recognized and eliminated to maintain ER homeostasis. Two cellular mechanisms have been identified to rid the ER of terminally unfolded, misfolded, and aggregated proteins. ER-associated degradation (ERAD) was discovered nearly 30 years ago and entails the identification of improperly matured secretory pathway proteins and their retrotranslocation to the cytosol for degradation by the ubiquitin-proteasome system. ER-phagy has been more recently described and caters to larger, more complex proteins and protein aggregates that are not readily handled by ERAD. This pathway has unique upstream components and relies on the same downstream effectors of autophagy used in other cellular processes to deliver clients to lysosomes for degradation. In this review, we describe the main elements of ERQC, ERAD, and ER-phagy and focus on recent advances in these fields.

Indexed as

AnimalsEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationHumansProtein FoldingProteinsProtein TransportSecretory PathwayProteinsERADER-Associated degradationER chaperonesER-PhagyERQCER quality controlUbiquitin proteasome systemUnfolded protein responseUPRUPS

Identifiers

PMID31669350
PMCPMC6911830
OpenAlexW2981544598

What OpenQuestion holds

Textmetadata
LicenceTDM
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.