PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25515270-5	2015	We report that treatment of human neutrophils with the delta-PKC inhibitor rottlerin significantly attenuates f-Met-Leu-Phe (fMLF)-induced MARCKS phosphorylation (IC50=5.709 muM), adhesion (IC50=8.4 muM), and migration (IC50=6.7 muM), while alpha-, beta-, and zeta-PKC inhibitors had no significant effect.	rottlerin	75-84	myristoylated alanine rich protein kinase C substrate	Homo sapiens	139-145	
18055557-5	2007	Rottlerin also reduced PMA- or human neutrophil elastase-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein in these cells.	rottlerin	0-9	myristoylated alanine rich protein kinase C substrate	Homo sapiens	84-129	
18055557-5	2007	Rottlerin also reduced PMA- or human neutrophil elastase-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein in these cells.	rottlerin	0-9	myristoylated alanine rich protein kinase C substrate	Homo sapiens	131-137	
15541367-6	2004	Translocation of MARCKS-GFP induced by VEGF-KDR stimulus was blocked by rottlerin, a PKCdelta specific inhibitor, or human PKCdelta siRNA.	rottlerin	72-81	myristoylated alanine rich protein kinase C substrate	Homo sapiens	17-23	
14747473-4	2004	Interestingly, PKCdelta is the most strongly phosphorylated isoform, and the preferential PKCdelta inhibitor rottlerin largely prevented EGF-induced phosphorylation of PKC substrates and MARCKS.	rottlerin	109-118	myristoylated alanine rich protein kinase C substrate	Homo sapiens	187-193