Evidence map›Paper›PMID 29536114›Full record

ReviewCellular and molecular life sciences : CMLS2018

Bridging the molecular and biological functions of the oxysterol-binding protein family.

Antonietta Pietrangelo, Neale D Ridgway

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
12.1field-weighted citation impact, top 1% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Role of Oxysterol-Binding Protein Family in Cholesterol Metabolism and Cancer Progression: A Review.Medical science monitor : international medical journal of experimental and clinical research · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. All roads lead to OSBP.Nature chemical biology · 2025
    Article
  13. Article
  14. Article
  15. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  16. Mechanisms for assembly of the nucleoplasmic reticulum.Cellular and molecular life sciences : CMLS · 2024
    Review
  17. The Endoplasmic Reticulum and Its Contacts: Emerging Roles in Axon Development, Neurotransmission, and Degeneration.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  18. Review
  19. Article
  20. Article

1 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 at 1 institution in 1 country.

Antonietta PietrangeloAtlantic Research Center, C306 CRC Bldg, Department of Pediatrics, and Biochemistry and Molecular Biology, Dalhousie University, 5849 University Av., Halifax, NS, B3H4R2, Canada.
Neale D RidgwayAtlantic Research Center, C306 CRC Bldg, Department of Pediatrics, and Biochemistry and Molecular Biology, Dalhousie University, 5849 University Av., Halifax, NS, B3H4R2, Canada. nridgway@dal.ca.ORCID http://orcid.org/0000-0002-0441-6228
Dalhousie University · CA

Funding

Institute of Nutrition, Metabolism and Diabetes MOP-15284
6 · The paper itself

Abstract

Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) constitute a large eukaryotic gene family that transports and regulates the metabolism of sterols and phospholipids. The original classification of the family based on oxysterol-binding activity belies the complex dual lipid-binding specificity of the conserved OSBP homology domain (OHD). Additional protein- and membrane-interacting modules mediate the targeting of select OSBP/ORPs to membrane contact sites between organelles, thus positioning the OHD between opposing membranes for lipid transfer and metabolic regulation. This unique subcellular location, coupled with diverse ligand preferences and tissue distribution, has identified OSBP/ORPs as key arbiters of membrane composition and function. Here, we will review how molecular models of OSBP/ORP-mediated intracellular lipid transport and regulation at membrane contact sites relate to their emerging roles in cellular and organismal functions.

Indexed as

Multigene FamilyBiological TransportDyslipidemiasEndoplasmic ReticulumGolgi ApparatusHumansNeoplasmsOxysterol Binding ProteinsPhospholipidsReceptors, SteroidSterolsOxysterol Binding ProteinsPhospholipidsReceptors, SteroidSterolsCancerDyslipidemiaIntracellular lipid transportMembrane contact sitesMetabolismOxysterol-binding proteinsViral replication

Identifiers

PMID29536114
PMCPMC11105248
OpenAlexW2791859663

What OpenQuestion 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 OpenQuestion graph.