Evidence map›Paper›PMID 17434796›Full record

ReviewBiochimica et biophysica acta2007

Sterol transport in yeast and the oxysterol binding protein homologue (OSH) family.

Timothy A Schulz, William A Prinz

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Osh2 mediatesAntimicrobial agents and chemotherapy · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. CHARMM-GUIJournal of chemical theory and computation · 2023
    Review
  8. Article
  9. Article
  10. Outline of the biosynthesis and regulation of ergosterol in yeast.World journal of microbiology & biotechnology · 2019
    Review
  11. Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2019
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Non-vesicular Lipid Transport Machinery inFrontiers in cellular and infection microbiology · 2018
    Review
  17. Review
  18. Review
  19. Article
  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 at 1 institution in 1 country.

Timothy A SchulzLaboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA.
William A Prinz
National Institutes of Health · US

Funding

Intracellular Lipid Trafficking and Organelle BiogenesisZ01DK060004 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI PRINZ, WILLIAM · 2002 to 2008
$532k
Intramural NIH HHS Z01 DK060004
6 · The paper itself

Abstract

Sterols such as cholesterol are a significant component of eukaryotic cellular membranes, and their unique physical properties influence a wide variety of membrane processes. It is known that the concentration of sterol within the membrane varies widely between organelles, and that the cell actively maintains this distribution through various transport processes. Vesicular pathways such as secretion or endocytosis may account for this traffic, but increasing evidence highlights the importance of nonvesicular routes as well. The structure of an oxysterol-binding protein homologue (OSH) in yeast (Osh4p/Kes1p) has recently been solved, identifying it as a sterol binding protein, and there is evidence consistent with the role of a cytoplasmic, nonvesicular sterol transporter. Yeast have seven such proteins, which appear to have distinct but overlapping functions with regard to maintaining intracellular sterol distribution and homeostasis. Control of sterol distribution can have far-reaching effects on membrane-related functions, and Osh proteins have been implicated in a variety of processes such as secretory vesicle budding from the Golgi and establishment of cell polarity. This review summarizes the current body of knowledge regarding this family and its potential functions, placing it in the context of known and hypothesized pathways of sterol transport in yeast.

Indexed as

Biological Transport, ActiveCarrier ProteinsCell MembraneEndoplasmic ReticulumErgosterolGolgi ApparatusIntracellular MembranesOxysterol Binding ProteinsProtein TransportSaccharomyces cerevisiae ProteinsSterolsVesicular Transport ProteinsCarrier ProteinsErgosterolHES1 protein, S cerevisiaeOSH2 protein, S cerevisiaeOSH3 protein, S cerevisiaeOsh6p protein, S cerevisiaeOxysterol Binding ProteinsSaccharomyces cerevisiae ProteinsSterolsVesicular Transport Proteins

Identifiers

PMID17434796
PMCPMC2034499
OpenAlexW2029127632

What Socratic holds

Textmetadata
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 Socratic graph.