Results 251 to 260 of about 275,439 (289)
Relationship Between Virulence Factor Activities, Cytotoxicity of <i>Candida albicans</i> Strains Isolated from Oral Cavity, and Cytokine Production by Oral Keratinocytes Exposed to Those Strains. [PDF]
Dent J (Basel)Yano K +10 more
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Lipid landscaping of the bacterial cell surface. [PDF]
Proc Natl Acad Sci U S AGrabowicz M, May KL.
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The PLA2R Paradox: Seropositive Membranous Nephropathy With Negative Staining. [PDF]
Kidney Int RepTang X +6 more
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Selective Inhibition of <i>Yersinia enterocolitica</i> Type III Secretion by <i>Lindera obtusiloba</i> Extract and Cinnamtannin B1. [PDF]
PharmaceuticsYoo JH, Kim TJ.
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Journal of Biochemistry, 2002
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
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Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
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Seminars in Cell & Developmental Biology, 1997
Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
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Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
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Seminars in Cell & Developmental Biology, 1997
Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Biochemistry and Cell Biology, 2004
Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
openaire +2 more sources