Evidence map›Paper›PMID 29153511›Full record

ReviewTrends in biochemical sciences2018

How Are Proteins Reduced in the Endoplasmic Reticulum?

Lars Ellgaard, Carolyn S Sevier, Neil J Bulleid

Open access · hybridAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
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  7. Review
  8. Hypercapnia Effects on Lung Function.Comprehensive Physiology · 2026
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  12. Thiamine Deficiency and Neuroinflammation Are Important Contributors to Alcohol Use Disorder.Pathophysiology : the official journal of the International Society for Pathophysiology · 2025
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

7 more citing papers are in PubMed but not listed here.

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

3 authors at 3 institutions in 3 countries.

Lars EllgaardDepartment of Biology, University of Copenhagen, 2200 Copenhagen, Denmark. Electronic address: lellgaard@bio.ku.dk.
Carolyn S SevierDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853-2703, USA. Electronic address: carolyn.sevier@cornell.edu.
Neil J BulleidInstitute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK. Electronic address: neil.bulleid@glasgow.ac.uk.
Cornell University · USUniversity of Copenhagen · DKUniversity of Glasgow · GB

Funding

Molecular mechanisms to maintain ER redox balanceR01GM105958 · NIGMS · CORNELL UNIVERSITY · PI SEVIER, CAROLYN S · 2014 to 2022
$2.9M
Biotechnology and Biological Sciences Research Council BB/F016735Biotechnology and Biological Sciences Research Council BB/L00593Medical Research Council MC_PC_15076NIGMS NIH HHS R01 GM105958Wellcome TrustWellcome Trust 103720
6 · The paper itself

Abstract

The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER stress response. Our understanding of this process is generally poor but progress has been made. Enzymes performing the initial reduction of client proteins, as well as the ultimate electron donor in the pathway, have been identified. Most recently, a role for the cytosol in ER protein reduction has been revealed. Nevertheless, how reducing equivalents are transferred from the cytosol to the ER lumen remains an open question. We review here why proteins are reduced in the ER, discuss recent data on catalysis of steps in the pathway, and consider the implications for redox homeostasis within the early secretory pathway.

Indexed as

Endoplasmic ReticulumHumansOxidation-ReductionProtein FoldingProteinsProteinsdisulfidesendoplasmic reticulumER-associated degradationER chaperonesprotein foldingthiol reduction

Identifiers

PMID29153511
PMCPMC5751730
OpenAlexW2770116234

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.