A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS
Phospholipid antibodies -- Congresses : Antiphospholipid syndrome : insights and highlights from the 13th International Congress on Antiphospholipid Antibodies / Doruk Erkan, Silvia S. Pierangeli, editors
Phospholipids -- Analysis : Micro/nanoencapsulation of active food ingredients / Qingrong Huang, editor, Peter Given, editor, Michael Qian, editor ; sponsored by the ACS Division of Agricultural and Food Chemistry, Inc
Phospholipids -- chemistry : Micro/nanoencapsulation of active food ingredients / Qingrong Huang, editor, Peter Given, editor, Michael Qian, editor ; sponsored by the ACS Division of Agricultural and Food Chemistry, Inc
2009
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Phospholipids -- Congresses. : Phospholipids : characterization, metabolism, and novel biological applications : proceedings of the 6th International Colloquium / editors, Gregor Cevc, Fritz Paltauf
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
Nuclear phosphoprotein encoded by the p53 gene (GENES, P53) whose normal function is to control CELL PROLIFERATION and APOPTOSIS. A mutant or absent p53 protein has been found in LEUKEMIA; OSTEOSARCOMA; LUNG CANCER; and COLORECTAL CANCER
A tyrosine-specific protein kinase encoded by the v-src oncogene of ROUS SARCOMA VIRUS. The transforming activity of pp60(v-src) depends on both the lack of a critical carboxy-terminal tyrosine phosphorylation site at position 527, and the attachment of pp60(v-src) to the plasma membrane which is accomplished by myristylation of its N-terminal glycine
Phosphoproteinphosphatase : Inhibitors of protein kinases and protein phosphataes / contributors, D.R. Alexander [and others] ; editors, Lorenzo A. Pinna and Patricia T.W. Cohen
2004
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Phosphoproteins -- See Also the narrower term p53 protein