Evidence map›Paper›PMID 28158422›Full record

ArticleFEMS yeast research2017

Role of phosphatidylserine synthase in shaping the phospholipidome of Candida albicans.

Chelsi D Cassilly, Abigail T Farmer, Anthony E Montedonico, Terry K Smith, Shawn R Campagna, Todd B Reynolds

Open access · bronzeAbstract read
In one paragraph

Article in FEMS yeast research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Potential role of alginate in marine bacteria-yeast interactions.Applied and environmental microbiology · 2024
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Mapping the Substrate-Binding Sites in the Phosphatidylserine Synthase inFrontiers in cellular and infection microbiology · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The Significance of Lipids to Biofilm Formation inJournal of fungi (Basel, Switzerland) · 2018
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

6 authors at 1 institution in 1 country.

Chelsi D CassillyDepartment of Microbiology, University of Tennessee, Knoxville, TN 37996, USA.
Abigail T FarmerDepartment of Chemistry, University of Tennessee, Knoxville, TN 37996, USA.
Anthony E MontedonicoDepartment of Microbiology, University of Tennessee, Knoxville, TN 37996, USA.
Terry K SmithBiomedical Sciences Research Complex, Schools of Biology and Chemistry, The North Haugh, The University St. Andrews, Fife KY16 9ST, UK.
Shawn R CampagnaDepartment of Chemistry, University of Tennessee, Knoxville, TN 37996, USA.
Todd B ReynoldsDepartment of Microbiology, University of Tennessee, Knoxville, TN 37996, USA.
University of Tennessee at Knoxville · US

Funding

Screen for phosphatidylserine synthase inhibitors: antifungals & lipid probesR01AI105690 · NIAID · UNIVERSITY OF TENNESSEE KNOXVILLE · PI REYNOLDS, TODD B · 2013 to 2015
$1.2M
NIAID NIH HHS R01 AI105690
6 · The paper itself

Abstract

Phosphatidylserine (PS) synthase (Cho1p) and the PS decarboxylase enzymes (Psd1p and Psd2p), which synthesize PS and phosphatidylethanolamine (PE), respectively, are crucial for Candida albicans virulence. Mutations that disrupt these enzymes compromise virulence. These enzymes are part of the cytidine diphosphate-diacylglycerol pathway (i.e. de novo pathway) for phospholipid synthesis. Understanding how losses of PS and/or PE synthesis pathways affect the phospholipidome of Candida is important for fully understanding how these enzymes impact virulence. The cho1Δ/Δ and psd1Δ/Δ psd2Δ/Δ mutations cause similar changes in levels of phosphatidic acid, phosphatidylglycerol, phosphatidylinositol and PS. However, only slight changes were seen in PE and phosphatidylcholine (PC). This finding suggests that the alternative mechanism for making PE and PC, the Kennedy pathway, can compensate for loss of the de novo synthesis pathway. Candida albicans Cho1p, the lipid biosynthetic enzyme with the most potential as a drug target, has been biochemically characterized, and analysis of its substrate specificity and kinetics reveal that these are similar to those previously published for Saccharomyces cerevisiae Cho1p.

Indexed as

Candida albicansCDPdiacylglycerol-Serine O-PhosphatidyltransferaseGene DeletionKineticsPhospholipidsSubstrate SpecificityCDPdiacylglycerol-Serine O-PhosphatidyltransferasePhospholipidsCandida albicanslipidomics: phosphatidylserinephosphatidylcholinephosphatidylethanolaminephosphatidylglycerolphosphatidylinositol

Identifiers

PMID28158422
PMCPMC5399917
OpenAlexW2583101813

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.