PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11951087-6	2002	RESULTS: Co-immunoprecipitation of Cx43 with PKCgamma was observed only in cells over expressing PKCgamma and in cells activated with phorbol ester.	Phorbol Esters	134-147	gap junction alpha-1 protein	Oryctolagus cuniculus	35-39	
11951087-16	2002	The presence of PKCgamma and loss of surface Cx43 from two retinal cell lines, WERI and Y79, upon phorbol ester activation further suggests that activation of PKCgamma may be a common mechanism for control of cell surface Cx43.	Phorbol Esters	98-111	gap junction alpha-1 protein	Oryctolagus cuniculus	45-49	
11951087-16	2002	The presence of PKCgamma and loss of surface Cx43 from two retinal cell lines, WERI and Y79, upon phorbol ester activation further suggests that activation of PKCgamma may be a common mechanism for control of cell surface Cx43.	Phorbol Esters	98-111	gap junction alpha-1 protein	Oryctolagus cuniculus	222-226	
11951087-7	2002	Both overexpression and phorbol ester produced a rapid phosphorylation of Cx43 on serine.	Phorbol Esters	24-37	gap junction alpha-1 protein	Oryctolagus cuniculus	74-78	
11951087-8	2002	Cx43 cell surface gap junction plaques decreased in cells over expressing PKCgamma and in cells treated with phorbol ester.	Phorbol Esters	109-122	gap junction alpha-1 protein	Oryctolagus cuniculus	0-4	
11951087-12	2002	CONCLUSIONS: PKCgamma can be co-immunoprecipitated with Cx43 from lens epithelial cells using phorbol ester activation.	Phorbol Esters	94-107	gap junction alpha-1 protein	Oryctolagus cuniculus	56-60