Evidence map›Paper›PMID 20144991›Full record

ArticleJournal of cell science2010

Regulated increase in folding capacity prevents unfolded protein stress in the ER.

Chantal Christis, Asier Fullaondo, Danny Schildknegt, Souren Mkrtchian, Albert J R Heck, Ineke Braakman

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Type I interferons and endoplasmic reticulum stress in health and disease.International review of cell and molecular biology · 2020
    Review
  6. Characterization of CNPY5 and its family members.Protein science : a publication of the Protein Society · 2019
    Article
  7. Article
  8. Endoplasmic Reticulum (ER) Stress and Endocrine Disorders.International journal of molecular sciences · 2017
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Stressed out about obesity: IRE1α-XBP1 in metabolic disorders.Trends in endocrinology and metabolism: TEM · 2011
    Review
  18. Review
  19. Article
  20. 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

6 authors at 2 institutions in 3 countries.

Chantal ChristisCellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands.
Asier Fullaondo
Danny Schildknegt
Souren Mkrtchian
Albert J R Heck
Ineke Braakman
Utrecht University · NLKarolinska Institutet · SE

Funding

Medical Research Council
6 · The paper itself

Abstract

Stimulation of thyrocytes with thyroid stimulating hormone (TSH) leads to a morphological change and a massive increase in thyroglobulin (Tg) production. Although Tg is a demanding client of the endoplasmic reticulum (ER), its increase did not result in significant accumulation of unfolded protein in the ER. Instead, ER chaperones and folding enzymes reached maximum synthesis rates immediately after TSH stimulation, before significant upregulation of Tg synthesis. The resulting increase in folding capacity before client protein production prevented cellular unfolded-protein stress, confirmed by the silence of the most conserved branch of the unfolded protein response. Thyrocytes set an example of physiological adaptation of cells to a future potentially stress-causing situation, which suggests a general strategy for both non-secretory and specialized secretory cells.

Indexed as

AnimalsBlotting, WesternCell LineElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumMolecular ChaperonesProtein FoldingRatsReverse Transcriptase Polymerase Chain ReactionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationThyroglobulinThyrotropinUnfolded Protein ResponseMolecular ChaperonesThyroglobulinThyrotropin

Identifiers

PMID20144991
PMCPMC2823579
OpenAlexW2139570905

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.