PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20203631-1	2010	Modulation of the expression of the protein phosphatase-1 (PP1) glycogen-targeting subunit PTG exerts profound effects on cellular glycogen metabolism in vitro and in vivo.	Teniposide	91-94	inorganic pyrophosphatase 1	Homo sapiens	36-57	
20203631-1	2010	Modulation of the expression of the protein phosphatase-1 (PP1) glycogen-targeting subunit PTG exerts profound effects on cellular glycogen metabolism in vitro and in vivo.	Teniposide	91-94	inorganic pyrophosphatase 1	Homo sapiens	59-62	
20203631-4	2010	A full-length PTG mutant was generated as an adenoviral construct in which the valine and phenylalanine residues in the conserved PP1-binding domain were mutated to alanine (PTG-VF).	Teniposide	14-17	inorganic pyrophosphatase 1	Homo sapiens	130-133	
20203631-9	2010	These results indicate that the mutation of the PP1-binding domain on PTG resulted in the generation of a dominant-negative molecule that impeded endogenous PTG action and reduced cellular glycogen levels, through enhancement of glycogenolysis rather than impairment of glycogen synthesis.	Teniposide	70-73	inorganic pyrophosphatase 1	Homo sapiens	48-51