Evidence map›Paper›PMID 27521373›Full record

ReviewJournal of lipid research2016

Lipid synthesis and membrane contact sites: a crossroads for cellular physiology.

J Pedro Fernández-Murray, Christopher R McMaster

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Phosphatidate-mediated regulation of lipid synthesis at the nuclear/endoplasmic reticulum membrane.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. A putativeJournal of biosciences · 2018
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  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.

J Pedro Fernández-MurrayDepartment of Pharmacology, Dalhousie University, Halifax, NS, Canada.
Christopher R McMasterDepartment of Pharmacology, Dalhousie University, Halifax, NS, Canada. Electronic address: christopher.mcmaster@dal.ca.
Dalhousie University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane contact sites (MCSs) are regions of close apposition between different organelles that contribute to the functional integration of compartmentalized cellular processes. In recent years, we have gained insight into the molecular architecture of several contact sites, as well as into the regulatory mechanisms that underlie their roles in cell physiology. We provide an overview of two selected topics where lipid metabolism intersects with MCSs and organelle dynamics. First, the role of phosphatidic acid phosphatase, Pah1, the yeast homolog of metazoan lipin, toward the synthesis of triacylglycerol is outlined in connection with the seipin complex, Fld1/Ldb16, and lipid droplet formation. Second, we recapitulate the different contact sites connecting mitochondria and the endomembrane system and emphasize their contribution to phospholipid synthesis and their coordinated regulation. A comprehensive view is emerging where the multiplicity of contact sites connecting different cellular compartments together with lipid transfer proteins functioning at more than one MCS allow for functional redundancy and cross-regulation.

Indexed as

Cell MembraneLipid DropletsMembrane LipidsMembrane ProteinsMitochondriaMitochondrial ProteinsPhosphatidate PhosphataseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFld1 protein, S cerevisiaeLDB16 protein, S cerevisiaeMembrane LipidsMembrane ProteinsMitochondrial ProteinsPAH1 protein, S cerevisiaePhosphatidate PhosphataseSaccharomyces cerevisiae Proteinsendoplasmic reticulummitochondriaorganellephosphatidic acidtriacylglycerolvacuole

Identifiers

PMID27521373
PMCPMC5036376
OpenAlexW2518010812

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.