Evidence map›Paper›PMID 20308423›Full record

ArticleThe Journal of cell biology2010

New insights into oxidative folding.

Carolyn S Sevier

Open access · hybridAbstract readComment
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Carolyn S SevierDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. csevier@mit.edu
Massachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oxidoreductase ERO1 (endoplasmic reticulum [ER] oxidoreductin 1) is thought to be crucial for disulfide bond formation in the ER. In this issue, Zito et al. (2010. J. Cell Biol. doi:10.1083/jcb.200911086) examine the division of labor between the two mammalian isoforms of ERO1 (ERO1-alpha and -beta) in oxidative folding. Their analysis reveals a selective role for ERO1-beta in insulin production and a surprisingly minor contribution for either ERO1 isoform on immunoglobulin folding and secretion.

Indexed as

Protein FoldingAnimalsEndoplasmic ReticulumGlycoproteinsImmunoglobulinsInsulinIsoenzymesMiceMice, Inbred C57BLOxidation-ReductionOxidoreductasesEro1l protein, mouseGlycoproteinsImmunoglobulinsInsulinIsoenzymesOxidoreductases

Identifiers

PMID20308423
PMCPMC2845070
OpenAlexW2138348054

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.