Evidence map›Paper›PMID 22162132›Full record

ArticleThe Journal of cell biology2011

Lipid traffic: Osh4p makes an unexpected exchange.

Tim P Levine

Abstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Nonvesicular lipid transfer from the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012
    Review
  3. Phosphoinositides and vesicular membrane traffic.Biochimica et biophysica acta · 2012
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Tim P LevineInstitute of Ophthalmology, University College London, London EC1V 9EL, England, UK. tim.levine@ucl.ac.uk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new study in this issue (De Saint-Jean et al. 2011. J. Cell Biol. http://dx.doi.org/jcb.201104062) reveals that the sterol transfer protein Osh4p can also transport the signaling phospholipid phosphatidylinositol 4-phosphate (PI(4)P), which binds to the same site in Osh4p as sterol. This finding helps explain some previously published studies and also indicates that lipid/sterol exchange could contribute to establishing a sterol gradient in cells.

Indexed as

ErgosterolLipid BilayersMembrane ProteinsOxysterol Binding ProteinsPhosphatidylinositol PhosphatesReceptors, SteroidSaccharomyces cerevisiae ProteinsdehydroergosterolErgosterolKES1 protein, S cerevisiaeLipid BilayersMembrane ProteinsOxysterol Binding Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesReceptors, SteroidSaccharomyces cerevisiae Proteins

Identifiers

PMID22162132
PMCPMC3241729

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.