PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8280066-0 1993 Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: possible role of protein kinase M. Human erythrocytes contain cytosolic protein kinase C (PKC) which, when activated by phorbol 12-myristate 13-acetate (PMA), induces the phosphorylation of the membrane skeletal proteins band 4.1, band 4.9 and adducin. Tetradecanoylphorbol Acetate 0-31 erythrocyte membrane protein band 4.1 Homo sapiens 356-364 2830906-1 1988 Activation of protein kinase C in erythrocytes by 4-beta-phorbol 12-myristate 13-acetate (PMA) resulted in a parallel stimulation (time course and dose response) of the phosphorylation of both membrane proteins (heterodimers of 107 kDa and 97 kDa, protein 4.1 and 4.9, respectively) and of phosphatidylinositol 4-phosphate (PIP) and, to a lesser extent, of phosphatidylinositol 4,5-bisphosphate (PIP2). Tetradecanoylphorbol Acetate 50-88 erythrocyte membrane protein band 4.1 Homo sapiens 248-267 2830906-1 1988 Activation of protein kinase C in erythrocytes by 4-beta-phorbol 12-myristate 13-acetate (PMA) resulted in a parallel stimulation (time course and dose response) of the phosphorylation of both membrane proteins (heterodimers of 107 kDa and 97 kDa, protein 4.1 and 4.9, respectively) and of phosphatidylinositol 4-phosphate (PIP) and, to a lesser extent, of phosphatidylinositol 4,5-bisphosphate (PIP2). Tetradecanoylphorbol Acetate 90-93 erythrocyte membrane protein band 4.1 Homo sapiens 248-267 3711103-1 1986 The addition of the tumor promoting phorbol ester 12-O-tetradecanoyl phorbol 13-acetate to intact human red blood cells activates protein kinase C and stimulates the phosphorylation of the membrane skeletal proteins band 4.1 and band 4.9 as well as two proteins of molecular mass 115 and 110 kDa. Tetradecanoylphorbol Acetate 50-87 erythrocyte membrane protein band 4.1 Homo sapiens 216-224 2991234-1 1985 The phosphorylation of the membrane skeleton components protein 4.1 and protein 4.9 in intact erythrocytes is shown to increase in the presence of either 1 microM 12-O-tetradecanoyl phorbol 13-acetate or 2 mM dibutyryl cAMP. Tetradecanoylphorbol Acetate 163-200 erythrocyte membrane protein band 4.1 Homo sapiens 56-67