ReviewMethods in molecular biology (Clifton, N.J.)2027
Phospholipases D: An Update on Structure-Function Relationships.
Review in Methods in molecular biology (Clifton, N.J.), 2027. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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0 citing papers in PubMed.
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phospholipases D (PLD) are lipolytic and interfacial enzymes that hydrolyze the distal phosphodiester bond of phospholipid substrates. PLD are widespread in prokaryotes and eukaryotes and have various functions in bacteria, yeast, plants, and mammals. The PLD reaction frees phosphatidic acid (PA), which is an intermediate in the lipid pathway but also a signaling molecule involved in metabolic, cellular, and physiological processes. Depending on their primary structure, PLD belong to two different groups: the HKD family, characterized by an HXKX
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Registered trials
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