Evidence map›Paper›PMID 9601083›Full record

ArticleThe Biochemical journal1998

Characterization of sphingosine kinase (SK) activity in Saccharomyces cerevisiae and isolation of SK-deficient mutants.

M M Lanterman, J D Saba

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1998. 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
2.5field-weighted citation impact, top 10% 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, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Sphingolipids as cell fate regulators in lung development and disease.Apoptosis : an international journal on programmed cell death · 2015
    Review
  5. Autophagy in the light of sphingolipid metabolism.Apoptosis : an international journal on programmed cell death · 2015
    Review
  6. Article
  7. Review
  8. Extracellular and intracellular actions of sphingosine-1-phosphate.Advances in experimental medicine and biology · 2010
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Signal transduction of stress via ceramide.The Biochemical journal · 1998
    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

2 authors at 1 institution in 1 country.

M M LantermanChildren's Hospital Oakland Research Institute, 747 Fifty Second St., Oakland, CA 94609-1809, USA.
J D Saba
Children’s Institute · US

Funding

PHS HHS 1R01/77528-01
6 · The paper itself

Abstract

Sphingosine kinase (SK) catalyses the phosphorylation of sphingosine to generate sphingosine 1-phosphate, which is a second messenger involved in the proliferative responses of mammalian cells. Although the yeast Saccharomyces cerevisiae has similar phosphorylated sphingoid bases which appear to be involved in growth regulation and the response to stress, SK activity had not been previously demonstrated in yeast. In this study, an in vitro system was set up to characterize yeast SK activity. Activity was detected in the cytosol at neutral pH and 37 degreesC. Yeast SK phosphorylated the sphingoid bases sphingosine, dihydrosphingosine and phytosphingosine. (d,l)-threo-dihydrosphingosine, an inhibitor of mammalian SK, did not inhibit the yeast enzyme. Unique properties of yeast SK were an optimal temperature of 43 degreesC, and in vivo activation during nutrient deprivation. Spontaneous mutants with diminished SK activity were isolated utilizing a screen for resistance to sphingosine in a sphingosine-phosphate-lyase deletion background. Abnormal growth and heat sensitivity were observed in these mutants. These findings suggest that SK may function as a stress-response protein in yeast.

Indexed as

LysophospholipidsCell DivisionCell SurvivalEnzyme ActivationEnzyme InhibitorsHeat-Shock ProteinsHydrogen-Ion ConcentrationKineticsMutationPhenotypePhosphorylationPhosphotransferases (Alcohol Group Acceptor)Saccharomyces cerevisiaeSphingosineSphingosine KinaseSporesEnzyme InhibitorsHeat-Shock ProteinsLysophospholipidsPhosphotransferases (Alcohol Group Acceptor)phytosphingosinesafingolSphingosinesphingosine 1-phosphateSphingosine Kinase

Identifiers

PMID9601083
PMCPMC1219509
OpenAlexW1767680774

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.