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Results 1 - 5 of 5
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.14malfunction loss of GPI-phospholipase C polypeptide is associated with sustained replication of nascent procyclics 708444
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.14physiological function in monomorphic ILTat 1.3 strain, total GPI-phospholipase C polypeptide enzyme activity (per cell) remains constant for 72 h after initiation of transformation. GPI-phospholipase C polypeptide remains in AnTat 1.1 through differentiation, when variant surface glycoprotein is lost and procyclin is expressed on the cell surface 708444
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.14physiological function glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD) specifically cleaves glycosylphosphatidylinositol-anchored proteins from cell membranes. Reduction of GPI-anchored proteins on cell membranes by over expression of GPI-PLD results in significant inhibition of intracellular Ca2+ mobilization and ERK1/2 phosphorylation in response to oscillatory fluid flow 715721
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.14physiological function glycosylphosphatidylinositol phospholipase C is a virulence factor that releases variant surface glycoprotein from dying cells -, 730795
Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.14physiological function GDE3 cleaves and releases urokinase receptor from its glycosylphosphatidylinositol-anchor with consequent loss of function. GDE3 overexpression depletes urokinase receptor uPAR from distinct basolateral membrane domains in breast cancer cells, resulting in a less transformed phenotype, it slows tumor growth in a xenograft model and correlates with prolonged survival in patients 747647
Results 1 - 5 of 5