PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10659998-5 1999 Prior treatment of VSMCs with staurosporine (1 microM), a PKC inhibitor, inhibited the ability of PMA to attenuate BK-induced responses, suggesting that the inhibitory effect of PMA is mediated through the activation of PKC. Staurosporine 30-43 protein kinase C, alpha Rattus norvegicus 58-61 11486239-4 2001 The PKC inhibitors staurosporine and calphostin C inhibited the increase in force/[Ca(2+)]i induced by phenylephrine to a much greater extent than that induced by 80 mM K+. Staurosporine 19-32 protein kinase C, alpha Rattus norvegicus 4-7 10662600-9 2000 Staurosporine, a nonselective inhibitor of protein kinase C (PKC), inhibited PCB-induced release of [(3)H]-AA. Staurosporine 0-13 protein kinase C, alpha Rattus norvegicus 61-64 10659998-5 1999 Prior treatment of VSMCs with staurosporine (1 microM), a PKC inhibitor, inhibited the ability of PMA to attenuate BK-induced responses, suggesting that the inhibitory effect of PMA is mediated through the activation of PKC. Staurosporine 30-43 protein kinase C, alpha Rattus norvegicus 220-223 10098498-9 1999 Western blots demonstrated expression of PKCalpha, betaI, epsilon, delta, and zeta in H9c2 cells; PKC inhibitors (staurosporine or Ro 31-8220) or down-regulation of PKCalpha, betaI, epsilon, and delta by long-term (24 h) TPA treatment caused a partial blockade of the AVP-induced response, whereas the A23187-induced AA release was unaffected by down-regulation of these isoforms. Staurosporine 114-127 protein kinase C, alpha Rattus norvegicus 41-82 10578141-4 1999 These increases were reduced or eliminated by pretreatment of the cells with the PKC antagonists staurosporine or GF 109203X or the NO scavenger, phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl 3-oxide (PTIO). Staurosporine 97-110 protein kinase C, alpha Rattus norvegicus 81-84 10098498-9 1999 Western blots demonstrated expression of PKCalpha, betaI, epsilon, delta, and zeta in H9c2 cells; PKC inhibitors (staurosporine or Ro 31-8220) or down-regulation of PKCalpha, betaI, epsilon, and delta by long-term (24 h) TPA treatment caused a partial blockade of the AVP-induced response, whereas the A23187-induced AA release was unaffected by down-regulation of these isoforms. Staurosporine 114-127 protein kinase C, alpha Rattus norvegicus 41-44 9633917-7 1998 The effect of myotrophin on the stimulation of PKC activity and [3H]leucine incorporation was abolished by pretreatment with either staurosporine or H-7, two selective, pharmacological PKC inhibitors. Staurosporine 132-145 protein kinase C, alpha Rattus norvegicus 47-50 9705215-8 1998 The phosphorylation of these proteins decreased in the presence of staurosporine, which also supported PKC-mediated phosphorylation. Staurosporine 67-80 protein kinase C, alpha Rattus norvegicus 103-106 9633917-7 1998 The effect of myotrophin on the stimulation of PKC activity and [3H]leucine incorporation was abolished by pretreatment with either staurosporine or H-7, two selective, pharmacological PKC inhibitors. Staurosporine 132-145 protein kinase C, alpha Rattus norvegicus 185-188 9604867-11 1998 The PKC inhibitors staurosporine, bisindolylmaleimide, and AMG-C16 blocked the stimulated translocation of PKC-alpha and -beta, but not that of PKC-zeta. Staurosporine 19-32 protein kinase C, alpha Rattus norvegicus 4-7 9604867-11 1998 The PKC inhibitors staurosporine, bisindolylmaleimide, and AMG-C16 blocked the stimulated translocation of PKC-alpha and -beta, but not that of PKC-zeta. Staurosporine 19-32 protein kinase C, alpha Rattus norvegicus 107-116 8780012-4 1996 Moreover, pretreatment of PC12 cells with the protein kinase inhibitor staurosporine or with calphostin C, a specific inhibitor of PKC, also blocks the increase of AA release induced by NGF. Staurosporine 71-84 protein kinase C, alpha Rattus norvegicus 131-134 9374197-7 1997 Using a more specific PKC substrate, N-terminal acetylated peptide (4-14) from myelin basic protein, we then demonstrated that A beta indeed increased PKC activity and that this activity could be blocked by the PKC inhibitor, staurosporine. Staurosporine 226-239 protein kinase C, alpha Rattus norvegicus 22-25 9374197-7 1997 Using a more specific PKC substrate, N-terminal acetylated peptide (4-14) from myelin basic protein, we then demonstrated that A beta indeed increased PKC activity and that this activity could be blocked by the PKC inhibitor, staurosporine. Staurosporine 226-239 protein kinase C, alpha Rattus norvegicus 151-154 9374197-7 1997 Using a more specific PKC substrate, N-terminal acetylated peptide (4-14) from myelin basic protein, we then demonstrated that A beta indeed increased PKC activity and that this activity could be blocked by the PKC inhibitor, staurosporine. Staurosporine 226-239 protein kinase C, alpha Rattus norvegicus 151-154 9035611-10 1996 Inhibition of PKC activity by PKC inhibitors (H-7 or staurosporine) or downregulation induced by prolonged treatment with phorbol 12-myristate 13-acetate (PMA) or thyleametoxin (TX) significantly blocked the NE-induced AA release, which indicates PKC is involved in mediating NE-induced AA release. Staurosporine 53-66 protein kinase C, alpha Rattus norvegicus 14-17 8224525-12 1993 In contrast, the Ca(2+)-dependent PKC activity in anterior pituitary was inhibited by H7, staurosporine and Ro-31-8220 with high potency as in all other preparations. Staurosporine 90-103 protein kinase C, alpha Rattus norvegicus 34-37 8146021-6 1994 A dose-dependent inhibition of EPO mRNA formation, independent of effects on total RNA synthesis, as determined by [3H]uridine incorporation, was also found in the presence of the kinase inhibitor staurosporine (ED50 approximately 2 x 10(-8) M) and three structurally related derivatives with increased selectivity for PKC (RO 317549, ED50 approximately 1 x 10(-6) M; RO 318220, ED50 approximately 1 x 10(-6) M and CGP 41251, ED50 approximately 4 x 10(-6) M). Staurosporine 197-210 protein kinase C, alpha Rattus norvegicus 319-322 8452537-5 1993 Confirming this, 4 beta-phorbol 12-monoacetate and 4 alpha-phorbol had no effect on cellular eicosanoid formation, while the PMA-induced response was fully abolished both in the presence of the PKC inhibitors staurosporine and CGP 41251 and in PKC-down-regulated cells. Staurosporine 209-222 protein kinase C, alpha Rattus norvegicus 194-197 1538715-5 1992 Previous studies indicated that staurosporine inhibits PKC by binding its catalytic domain. Staurosporine 32-45 protein kinase C, alpha Rattus norvegicus 55-58 1538715-7 1992 Our kinetic results provide evidence that staurosporine inhibits PKC by binding to a site of the catalytic domain other than the ATP substrate and protein substrate binding sites. Staurosporine 42-55 protein kinase C, alpha Rattus norvegicus 65-68 1538715-8 1992 Staurosporine inhibition appears to entail binding at a conserved site in the catalytic domain of PKC, because staurosporine inhibited rat brain PKC-alpha, PKC-beta, and PKC-gamma, as well as the catalytic fragments of PKC-beta and PKC-gamma, with similar protencies. Staurosporine 0-13 protein kinase C, alpha Rattus norvegicus 98-101 1538715-8 1992 Staurosporine inhibition appears to entail binding at a conserved site in the catalytic domain of PKC, because staurosporine inhibited rat brain PKC-alpha, PKC-beta, and PKC-gamma, as well as the catalytic fragments of PKC-beta and PKC-gamma, with similar protencies. Staurosporine 0-13 protein kinase C, alpha Rattus norvegicus 145-154 1538715-8 1992 Staurosporine inhibition appears to entail binding at a conserved site in the catalytic domain of PKC, because staurosporine inhibited rat brain PKC-alpha, PKC-beta, and PKC-gamma, as well as the catalytic fragments of PKC-beta and PKC-gamma, with similar protencies. Staurosporine 111-124 protein kinase C, alpha Rattus norvegicus 98-101 1538715-8 1992 Staurosporine inhibition appears to entail binding at a conserved site in the catalytic domain of PKC, because staurosporine inhibited rat brain PKC-alpha, PKC-beta, and PKC-gamma, as well as the catalytic fragments of PKC-beta and PKC-gamma, with similar protencies. Staurosporine 111-124 protein kinase C, alpha Rattus norvegicus 145-154 1538715-10 1992 Taken in the context of previous mechanistic studies of PKC-catalyzed histone III-S phosphorylation, these results provide evidence that staurosporine binds to a complex of PKC, MgATP, and histone III-S, thereby forming a complex that cannot break down to products. Staurosporine 137-150 protein kinase C, alpha Rattus norvegicus 56-59 1538715-12 1992 Thus, the kinetics of inhibition of the catalytic fragment of PKC-gamma by staurosporine provide evidence that staurosporine inhibits PKC by a mixed mechanism. Staurosporine 75-88 protein kinase C, alpha Rattus norvegicus 62-65 1538715-12 1992 Thus, the kinetics of inhibition of the catalytic fragment of PKC-gamma by staurosporine provide evidence that staurosporine inhibits PKC by a mixed mechanism. Staurosporine 111-124 protein kinase C, alpha Rattus norvegicus 62-65 24404591-3 2013 After 1 h, these processes were suppressed by PKC inhibitors staurosporine, GF 109203X and chelerythrine, but increased by PKC activator PMA. Staurosporine 61-74 protein kinase C, alpha Rattus norvegicus 46-49 15709112-4 2005 This redistribution was inhibited by staurosporine, a pan PKC inhibitor, or by 12-(2-cyanoethyl)-6,7,12,13-tetrahydro-13-methyl-5-oxo-5H-indolo(2,3-a)pyrrolo(3,4-c)-carbazole (Go6976) at a concentration that selectively inhibits conventional PKC isozymes (PKC alpha, -beta, and -gamma). Staurosporine 37-50 protein kinase C, alpha Rattus norvegicus 58-61 15709112-4 2005 This redistribution was inhibited by staurosporine, a pan PKC inhibitor, or by 12-(2-cyanoethyl)-6,7,12,13-tetrahydro-13-methyl-5-oxo-5H-indolo(2,3-a)pyrrolo(3,4-c)-carbazole (Go6976) at a concentration that selectively inhibits conventional PKC isozymes (PKC alpha, -beta, and -gamma). Staurosporine 37-50 protein kinase C, alpha Rattus norvegicus 242-245 15709112-4 2005 This redistribution was inhibited by staurosporine, a pan PKC inhibitor, or by 12-(2-cyanoethyl)-6,7,12,13-tetrahydro-13-methyl-5-oxo-5H-indolo(2,3-a)pyrrolo(3,4-c)-carbazole (Go6976) at a concentration that selectively inhibits conventional PKC isozymes (PKC alpha, -beta, and -gamma). Staurosporine 37-50 protein kinase C, alpha Rattus norvegicus 256-284 12456804-6 2002 Multiple nonselective PKC inhibitors, including staurosporine, bisindolylmaleimide I, and Calphostin C, inhibited both EGF and TRH induced rat PRL promoter activity. Staurosporine 48-61 protein kinase C, alpha Rattus norvegicus 22-25