Evidence map›Paper›PMID 24440759›Full record

ReviewThe international journal of biochemistry & cell biology2014

The StarD4 subfamily of steroidogenic acute regulatory-related lipid transfer (START) domain proteins: new players in cholesterol metabolism.

Maria Calderon-Dominguez, Gregorio Gil, Miguel Angel Medina, William M Pandak, Daniel Rodríguez-Agudo

Abstract readReview
In one paragraph

Review in The international journal of biochemistry & cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. StarD5 levels of expression correlate with onset and progression of steatosis and liver fibrosis.American journal of physiology. Gastrointestinal and liver physiology · 2024
    Article
  5. Article
  6. Article
  7. [Steroidogenic acute regulatory protein-related lipid transfer 4 (StarD4) promotes breast cancer cell proliferation and its mechanism].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
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

5 authors.

Maria Calderon-DominguezDepartment of Biochemistry and Molecular Biology, Faculty of Pharmacy, Universidad de Barcelona, Spain.
Gregorio GilDepartment of Biochemistry, Virginia Commonwealth University, Richmond, VA, United States.
Miguel Angel MedinaDepartment of Molecular Biology and Biochemistry, Universidad de Malaga, Spain.
William M PandakDepartment of Medicine, Veterans Affairs Medical Center and Virginia Commonwealth University, Richmond, VA, United States.
Daniel Rodríguez-AgudoDepartment of Medicine, Veterans Affairs Medical Center and Virginia Commonwealth University, Richmond, VA, United States. Electronic address: drodriguezag@vcu.edu.

Funding

Role of Star Proteins in Bile Acid and Cholesterol MetabolismR01DK082464 · NIDDK · VIRGINIA COMMONWEALTH UNIVERSITY · PI GIL, GREGORIO, PANDAK, WILLIAM M · 2009 to 2012
$1.4M
Role of Cholesterol in Non Alcoholic Fatty LiverI01BX000197 · VA · VA VETERANS ADMINISTRATION HOSPITAL · PI PANDAK, WILLIAM M · 2009 to 2021
–
BLRD VA I01 BX000197NIDDK NIH HHS DK082464NIDDK NIH HHS R01 DK082464
6 · The paper itself

Abstract

Cholesterol levels in the body are maintained through the coordinated regulation of its uptake, synthesis, distribution, storage and efflux. However, the way cholesterol is sorted within cells remains poorly defined. The discovery of the newly described StarD4 subfamily, part of the steroidogenic acute regulatory lipid transfer (START) domain family of proteins, affords an opportunity for the study of intracellular cholesterol movement, metabolism and its disorders. The three members of this intracellular subfamily of proteins (StarD4, StarD5 and StarD6) have a similar lipid binding pocket specific for sterols (cholesterol in particular), but differing regulation and localization. The ability to bind and transport cholesterol through a non-vesicular mean suggests that they play a previously unappreciated role in cholesterol homeostasis.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsBiological TransportCarrier ProteinsCholesterolHumansMembrane Transport ProteinsModels, BiologicalAdaptor Proteins, Vesicular TransportCarrier ProteinsCholesterolMembrane Transport ProteinsSTARD4 protein, humanSTARD5 protein, humanSTARD6 protein, humanCholesterolCholesterol transportStarD4 subfamilySteroidogenic acute regulatory lipid transfer domainSterols

Identifiers

PMID24440759
PMCPMC3951587

What OpenQuestion holds

Textmetadata
LicenceTDM
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.