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Phospholipase D

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

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1996
Abstract:Phospholipase D is an ubiquitous enzyme that hydrolyzes phosphatidylcholine to phosphatidic acid and choline. Its cellular actions are related to the production of phosphatidic acid and include alterations to cell growth, shape, and secretion.
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Phospholipase D in cellular senescence

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1999
Cellular senescence appears to be an important part of organismal aging. Cellular senescence is characterized by flattened enlarged morphology, inhibition of DNA replication in response to growth factors, inability to phosphorylate the pRb tumor suppressor protein, inability to produce c-fos or AP-1 and overexpression of a variety of genes, notably p21
M E, Venable, L M, Obeid
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Measurement of Phospholipase D Activity

Analytical Biochemistry, 1997
Phosphodiesteric cleavage of phosphatidylcholine by members of a growing family of phospholipases D produces choline and phosphatidic acid. These enzymes can also catalyse a transphosphatidylation reaction in which the aliphatic chain of a primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product.
A J, Morris, M A, Frohman, J, Engebrecht
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Dimerization of Phospholipase D Isozymes

Biochemical and Biophysical Research Communications, 2002
Two mammalian phospholipase D (PLD) isozymes (PLD1 and PLD2) have been reported. In this study, we differentially tagged these isozymes with enhanced green fluorescent protein (EGFP-rPLD1 and EGFP-rPLD2) or Xpress peptide epitope (Xpress-rPLD1 and Xpress-rPLD2) to examine the association between these isozymes.
Yoonseok, Kam, John H, Exton
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Plant Phospholipase D

2009
Phospholipase D (PLD) is involved in different plant processes, ranging from responses to abiotic and biotic stresses to plant development and seed quality. The PLD family consists of multiple members that have distinguishable biochemical and regulatory properties.
Wenhua Zhang   +4 more
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Phospholipase D structure and regulation

Chemistry and Physics of Lipids, 1999
The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may
M A, Frohman, A J, Morris
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Soluble Phospholipase D

1993
Publisher Summary This chapter discusses the detection and characterization of the soluble phospholipase D. Phospholipase D is an important component in cellular signal transduction mechanisms. A unique property of phospholipase D is its ability to catalyze a transphosphatidylation reaction by which the phosphatidyl moiety of the phospholipid ...
M. Motasim Billah   +2 more
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Kinetics of myocardial phospholipase D

Molecular and Cellular Biochemistry, 1996
Myocardial phospholipase D (PLD) is located in different subcellular membranes, including sarcolemma (SL) and sarcoplasmic reticulum (SR). In this study, the kinetics of PLD-dependent hydrolytic and transphosphatidylation activities were examined in SL and SR fractions isolated from rat heart by measuring the formation of phosphatidic acid and ...
J, Dai, S Y, Liu, V, Panagia
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Phospholipase D in Tetrahymena: activity and significance

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1999
Abstract We detected phospholipase D in three species of ciliates: Tetrahymena: T. thermophila, T. pyriformis and T. setosa in nutrient medium supplemented with ethanol in in vivo systems, by the appearance of phosphatidylethanol. The calcium ionophore A23187 increased the synthesis of phosphatidylethanol, as compared with untreated controls.
Rasmussen, M., Rasmussen, L.
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