Evidence map›Paper›PMID 21144725›Full record

ReviewCurrent opinion in cell biology2011

Disulfide bonds in ER protein folding and homeostasis.

Matthias J Feige, Linda M Hendershot

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing 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

101 citing papers in PubMed.

  1. Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Glutamine-dependent changes in fibroblast-derived extracellular matrix dictate cancer cell behavior.Matrix biology : journal of the International Society for Matrix Biology · 2026
    Article
  6. Article
  7. A roadmap to chemically reactive species: how diverse oxidants affectMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Molecular Determinants of TMC Protein Biogenesis and Trafficking.International journal of molecular sciences · 2025
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

41 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

2 authors.

Matthias J FeigeDepartment of Genetics and Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Linda M Hendershot

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 GM54068NIGMS NIH HHS R01 GM054068
6 · The paper itself

Abstract

Proteins that are expressed outside the cell must be synthesized, folded, and assembled in a way that ensures they can function in their designate location. Accordingly, these proteins are primarily synthesized in the endoplasmic reticulum (ER), which has developed a chemical environment more similar to that outside the cell. This organelle is equipped with a variety of molecular chaperones and folding enzymes that both assist the folding process, while at the same time exerting tight quality control measures that are largely absent outside the cell. A major post-translational modification of ER-synthesized proteins is disulfide bridge formation, which is catalyzed by the family of protein disulfide isomerases. As this covalent modification provides unique structural advantages to extracellular proteins, multiple pathways to disulfide bond formation have evolved. However, the advantages that disulfide bonds impart to these proteins come at a high cost to the cell. Very recent reports have shed light on how the cell can deal with or even exploit the side reactions of disulfide bond formation to maintain homeostasis of the ER and its folding machinery.

Indexed as

HomeostasisProtein FoldingAnimalsDisulfidesEndoplasmic ReticulumHumansProtein MultimerizationProtein Processing, Post-TranslationalDisulfides

Identifiers

PMID21144725
PMCPMC3078216

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.