PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17570678-1	2007	The protein kinase C (PKC) family of serine/threonine kinases has been the subject of intensive study in the field of cancer since their initial discovery as major cellular receptors for the tumor promoting phorbol esters nearly 30 years ago.	Phorbol Esters	207-221	protein kinase C iota	Homo sapiens	22-25	
1851155-1	1991	Interaction of protein kinase C (PKC) isozymes with phosphatidylinositol 4,5-bisphosphate (PIP2) was investigated by monitoring the changes in the intrinsic fluorescence of the enzyme, the kinase activity, and phorbol ester binding.	Phorbol Esters	210-223	protein kinase C iota	Homo sapiens	33-36	
2295617-1	1990	Interactions of types I, II, and III protein kinase C (PKC) with phospholipids were investigated by following the changes in protein kinase activity and phorbol ester binding.	Phorbol Esters	153-166	protein kinase C iota	Homo sapiens	55-58	
1527599-2	1992	A striking example of this differential distribution is seen in the cerebellum, where Purkinje cells express PKC-I, an isozyme that is strongly activated by both phorbol ester (PE), and low doses of cis-unsaturated fatty acid (c-UFA), while granule cells predominantly express PKC-II, an isozyme that is strongly activated by PE but not c-UFA.	Phorbol Esters	162-175	protein kinase C iota	Homo sapiens	109-114	
1527599-2	1992	A striking example of this differential distribution is seen in the cerebellum, where Purkinje cells express PKC-I, an isozyme that is strongly activated by both phorbol ester (PE), and low doses of cis-unsaturated fatty acid (c-UFA), while granule cells predominantly express PKC-II, an isozyme that is strongly activated by PE but not c-UFA.	Phorbol Esters	177-179	protein kinase C iota	Homo sapiens	109-114	
1527599-2	1992	A striking example of this differential distribution is seen in the cerebellum, where Purkinje cells express PKC-I, an isozyme that is strongly activated by both phorbol ester (PE), and low doses of cis-unsaturated fatty acid (c-UFA), while granule cells predominantly express PKC-II, an isozyme that is strongly activated by PE but not c-UFA.	Phorbol Esters	326-328	protein kinase C iota	Homo sapiens	109-114	
1851155-7	1991	Binding of PIP2 to PKC in the absence of divalent metal ion also caused a reduction of [3H]phorbol 12,13-dibutyrate binding as a result of reducing the affinity of the enzyme for phorbol ester.	Phorbol Esters	179-192	protein kinase C iota	Homo sapiens	19-22	
2295617-3	1990	The phospholipid-induced inactivation of PKC was concentration and time dependent and only affected the kinase activity without influencing phorbol ester binding.	Phorbol Esters	140-153	protein kinase C iota	Homo sapiens	41-44	
2295617-10	1990	Under the same conditions, the phorbol ester-binding activity of PKC I was also recovered, but the kinase activity was not.	Phorbol Esters	31-44	protein kinase C iota	Homo sapiens	65-70