ArticleThe Biochemical journal1996
Phorbol ester-sensitive phospholipase D is mainly localized in the endoplasmic reticulum of BHK cells.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- Generation of choline for acetylcholine synthesis by phospholipase D isoforms.BMC neuroscience · 2001Article
- Involvement of PL-D in the alternate signal tranduction pathway of macrophages induced by an external stimulus.Molecular and cellular biochemistry · 2000Article
- Intracellular cleavage of glycosylphosphatidylinositol by phospholipase D induces activation of protein kinase Calpha.The Biochemical journal · 1999Article
- Utilization of phosphatidylcholine and production of diradylglycerol as a consequence of sphingomyelin synthesis.The Biochemical journal · 1998Article
- Cloning and expression analysis of murine phospholipase D1.The Biochemical journal · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The localization of phorbol ester-sensitive phospholipase D (PLD) in baby hamster kidney cells has been investigated by determining the subcellular distribution of the phosphatidylbutanol produced when the cells are incubated with phorbol 12-myristate 13-acetate and n-butanol. Results derived by isolation of plasma membrane vesicles from intact cells or by subcellular fractionation on a sucrose density gradient suggest the PLD is specific for phosphatidylcholine and its primary site of action is not the plasma membrane but the endoplasmic reticulum.
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Registered trials
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