Evidence map›Paper›PMID 23085588›Full record

ReviewJournal of molecular and cellular cardiology2013

New concepts of endoplasmic reticulum function in the heart: programmed to conserve.

Shirin Doroudgar, Christopher C Glembotski

Abstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Acute endoplasmic reticulum stress-induced mitochondria respiratory chain damage: The role of activated calpains.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  9. Loss of Sec-1 Family Domain-Containing 1 (Journal of cardiovascular development and disease · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Nucleosome proteostasis and histone turnover.Frontiers in molecular biosciences · 2022
    Review
  18. Article
  19. Review
  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.

Shirin DoroudgarSan Diego State University Heart Institute and The Department of Biology, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
Christopher C Glembotski

Funding

Surgery, Physiology and ImmunohistopathologyP01HL085577 · NHLBI · SAN DIEGO STATE UNIVERSITY · PI GUSTAFSSON, ASA B. · 2006 to 2017
$18.4M
Role of Unfolded Protein Response in Cardiac ProtectionR01HL075573 · NHLBI · SAN DIEGO STATE UNIVERSITY · PI GLEMBOTSKI, CHRIS · 2004 to 2011
$3.0M
Roles for ER Stress Inducible Cardiomyokines in the heartR01HL104535 · NHLBI · SAN DIEGO STATE UNIVERSITY · PI GLEMBOTSKI, CHRIS · 2010 to 2013
$1.5M
NHLBI NIH HHS HL-075573NHLBI NIH HHS HL-085577NHLBI NIH HHS HL104535NHLBI NIH HHS P01 HL085577NHLBI NIH HHS R01 HL075573NHLBI NIH HHS R01 HL104535
6 · The paper itself

Abstract

Secreted and membrane proteins play critical roles in myocardial health and disease. Studies in non-myocytes have shown that the peri-nuclear ER is the site for synthesis, folding, and quality control of most secreted and membrane proteins, as well as a nexus of a signal transduction system, called the ER stress response, which informs the cell about the status of ER protein folding. Moreover, the dynamic physical and functional association of the ER with mitochondria is a key site responsible for integrating ER function and mitochondrial metabolism, but is only just beginning to be understood in the myocardium. Although a great deal is known about roles played by the sarcoplasmic reticulum (SR) in contractile calcium handling in the heart, little is known about the relative locations and functions of the peri-nuclear ER and the SR in terms of secreted and membrane protein synthesis and folding. In this review we will explore the current state of knowledge of the location of secreted and membrane protein synthesis, folding, and quality control machinery in cardiac myocytes, as well as our understanding of the functional consequences of ER stress and the unfolded protein response in the heart in terms of protein synthesis, cell growth, and metabolic regulation. This article is part of a Special Issue entitled "Focus on Cardiac Metabolism".

Indexed as

AnimalsEndoplasmic ReticulumEndoplasmic Reticulum StressHeartHumansMyocardiumProtein BiosynthesisSarcoplasmic ReticulumSignal Transduction

Identifiers

PMID23085588
PMCPMC3557761

What OpenQuestion holds

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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.