PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19208911-2	2009	Insulin-stimulated phosphorylation (measured using the phospho-Akt substrate [PAS] antibody) of AS160 and TBC1D1 appears to occur in an Akt-dependent manner, but the kinases responsible for contraction-stimulated PAS-AS160 and PAS-TBC1D1 remain unclear.	Aminosalicylic Acid	78-81	TBC1 domain family, member 4	Mus musculus	96-101	
19208911-8	2009	CONCLUSIONS: These data suggest that 1) insulin stimulates glucose transport and phosphorylation of AS160 and TBC1D1 in a PI 3-kinase/Akt-dependent manner, 2) contraction stimulates PAS-AS160 (but not PAS-TBC1D1 or glucose transport) in a PI 3-kinase/Akt-dependent manner, and 3) contraction stimulates PAS-TBC1D1 and glucose transport (but not PAS-AS160) in an AMPK-dependent manner.	Aminosalicylic Acid	182-185	TBC1 domain family, member 4	Mus musculus	100-105	
19208911-8	2009	CONCLUSIONS: These data suggest that 1) insulin stimulates glucose transport and phosphorylation of AS160 and TBC1D1 in a PI 3-kinase/Akt-dependent manner, 2) contraction stimulates PAS-AS160 (but not PAS-TBC1D1 or glucose transport) in a PI 3-kinase/Akt-dependent manner, and 3) contraction stimulates PAS-TBC1D1 and glucose transport (but not PAS-AS160) in an AMPK-dependent manner.	Aminosalicylic Acid	182-185	TBC1 domain family, member 4	Mus musculus	186-191	
19208911-8	2009	CONCLUSIONS: These data suggest that 1) insulin stimulates glucose transport and phosphorylation of AS160 and TBC1D1 in a PI 3-kinase/Akt-dependent manner, 2) contraction stimulates PAS-AS160 (but not PAS-TBC1D1 or glucose transport) in a PI 3-kinase/Akt-dependent manner, and 3) contraction stimulates PAS-TBC1D1 and glucose transport (but not PAS-AS160) in an AMPK-dependent manner.	Aminosalicylic Acid	182-185	TBC1 domain family, member 4	Mus musculus	186-191	
19208911-2	2009	Insulin-stimulated phosphorylation (measured using the phospho-Akt substrate [PAS] antibody) of AS160 and TBC1D1 appears to occur in an Akt-dependent manner, but the kinases responsible for contraction-stimulated PAS-AS160 and PAS-TBC1D1 remain unclear.	Aminosalicylic Acid	213-216	TBC1 domain family, member 4	Mus musculus	96-101	
22318952-5	2012	Here, analysis of AS160 immunoprecipitates from muscle extracts with site-specific phospho-antibodies revealed that contraction and AICAR caused no increase but rather a slight decrease in phosphorylation of the major PAS recognition site AS160-Thr(649).	Aminosalicylic Acid	218-221	TBC1 domain family, member 4	Mus musculus	18-23	
18276596-1	2008	The Akt substrate of 160 kDa (AS160) is phosphorylated on Akt substrate (PAS) motifs in response to insulin and contraction in skeletal muscle, regulating glucose uptake.	Aminosalicylic Acid	73-76	TBC1 domain family, member 4	Mus musculus	4-28	
18276596-1	2008	The Akt substrate of 160 kDa (AS160) is phosphorylated on Akt substrate (PAS) motifs in response to insulin and contraction in skeletal muscle, regulating glucose uptake.	Aminosalicylic Acid	73-76	TBC1 domain family, member 4	Mus musculus	30-35	
18276596-2	2008	Here we discovered a dissociation between AS160 protein expression and apparent AS160 PAS phosphorylation among soleus, tibialis anterior, and extensor digitorum longus muscles.	Aminosalicylic Acid	86-89	TBC1 domain family, member 4	Mus musculus	80-85