PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9388190-0	1997	12-O-Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase (ERK) signaling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells.	Tetradecanoylphorbol Acetate	0-36	mitogen-activated protein kinase 1	Mus musculus	94-97	
9388190-0	1997	12-O-Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase (ERK) signaling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells.	Tetradecanoylphorbol Acetate	0-36	src homology 2 domain-containing transforming protein C1	Mus musculus	169-172	
9388190-0	1997	12-O-Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase (ERK) signaling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells.	Serine	143-149	mitogen-activated protein kinase 1	Mus musculus	94-97	
9388190-0	1997	12-O-Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase (ERK) signaling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells.	Serine	143-149	src homology 2 domain-containing transforming protein C1	Mus musculus	169-172	
9388190-1	1997	We investigated the activation of the Ras/ERK signaling pathway by 12-O-tetradecanoylphorbol-13-acetate (TPA) in NIH3T3 fibroblasts.	Tetradecanoylphorbol Acetate	67-103	mitogen-activated protein kinase 1	Mus musculus	42-45	
9388190-1	1997	We investigated the activation of the Ras/ERK signaling pathway by 12-O-tetradecanoylphorbol-13-acetate (TPA) in NIH3T3 fibroblasts.	Tetradecanoylphorbol Acetate	105-108	mitogen-activated protein kinase 1	Mus musculus	42-45	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Tetradecanoylphorbol Acetate	31-34	src homology 2 domain-containing transforming protein C1	Mus musculus	109-112	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Tetradecanoylphorbol Acetate	31-34	src homology 2 domain-containing transforming protein C1	Mus musculus	113-116	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Tetradecanoylphorbol Acetate	31-34	src homology 2 domain-containing transforming protein C1	Mus musculus	206-209	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Tetradecanoylphorbol Acetate	31-34	protein phosphatase 1 catalytic subunit gamma	Mus musculus	282-285	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Tetradecanoylphorbol Acetate	31-34	protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform	Mus musculus	294-298	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Sodium Dodecyl Sulfate	121-124	src homology 2 domain-containing transforming protein C1	Mus musculus	109-112	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Sodium Dodecyl Sulfate	121-124	src homology 2 domain-containing transforming protein C1	Mus musculus	113-116	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Sodium Dodecyl Sulfate	121-124	src homology 2 domain-containing transforming protein C1	Mus musculus	206-209	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Sodium Dodecyl Sulfate	121-124	protein phosphatase 1 catalytic subunit gamma	Mus musculus	282-285	
9388190-3	1997	Further analysis revealed that TPA treatment induced, dependently on protein kinase C, the mobility shift of p66(shc) in SDS-polyacrylamide gel electrophoresis, which could be prevented by treatment of the Shc immunoprecipitate with serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).	Sodium Dodecyl Sulfate	121-124	protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform	Mus musculus	294-298	
9388190-4	1997	Phosphoamino acid analysis of Shc showed that unlike growth factor-induced Shc phosphorylation, where Shc is mainly phosphorylated at tyrosine residues, TPA-induced phosphorylation was only at serine residues.	Phosphoamino Acids	0-17	src homology 2 domain-containing transforming protein C1	Mus musculus	30-33	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	97-100	src homology 2 domain-containing transforming protein C1	Mus musculus	82-85	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	97-100	growth factor receptor bound protein 2	Mus musculus	91-95	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	97-100	src homology 2 domain-containing transforming protein C1	Mus musculus	82-85	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	97-100	protein phosphatase 1 catalytic subunit gamma	Mus musculus	273-276	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	179-182	src homology 2 domain-containing transforming protein C1	Mus musculus	27-30	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	179-182	src homology 2 domain-containing transforming protein C1	Mus musculus	82-85	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	179-182	growth factor receptor bound protein 2	Mus musculus	91-95	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	179-182	src homology 2 domain-containing transforming protein C1	Mus musculus	82-85	
9388190-5	1997	Like growth factor-induced Shc phosphorylation, which leads to the association of Shc with Grb2, TPA also induced this association, but, correspondingly to the above results, the TPA-induced association was disrupted by in vitro treatment of the Shc immunoprecipitate with PP1.	Tetradecanoylphorbol Acetate	179-182	protein phosphatase 1 catalytic subunit gamma	Mus musculus	273-276	
9388190-6	1997	Taken together, these results suggest that the TPA signal was fed at or upstream of Shc to activate the Ras/ERK signaling pathway involving serine phosphorylation of Shc.	Tetradecanoylphorbol Acetate	47-50	src homology 2 domain-containing transforming protein C1	Mus musculus	84-87	
9388190-6	1997	Taken together, these results suggest that the TPA signal was fed at or upstream of Shc to activate the Ras/ERK signaling pathway involving serine phosphorylation of Shc.	Tetradecanoylphorbol Acetate	47-50	mitogen-activated protein kinase 1	Mus musculus	108-111	
9388190-6	1997	Taken together, these results suggest that the TPA signal was fed at or upstream of Shc to activate the Ras/ERK signaling pathway involving serine phosphorylation of Shc.	Tetradecanoylphorbol Acetate	47-50	src homology 2 domain-containing transforming protein C1	Mus musculus	166-169	
9388190-6	1997	Taken together, these results suggest that the TPA signal was fed at or upstream of Shc to activate the Ras/ERK signaling pathway involving serine phosphorylation of Shc.	Serine	140-146	src homology 2 domain-containing transforming protein C1	Mus musculus	84-87	
9388190-6	1997	Taken together, these results suggest that the TPA signal was fed at or upstream of Shc to activate the Ras/ERK signaling pathway involving serine phosphorylation of Shc.	Serine	140-146	mitogen-activated protein kinase 1	Mus musculus	108-111	
9388190-6	1997	Taken together, these results suggest that the TPA signal was fed at or upstream of Shc to activate the Ras/ERK signaling pathway involving serine phosphorylation of Shc.	Serine	140-146	src homology 2 domain-containing transforming protein C1	Mus musculus	166-169