PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14564711-3	1967	Pyruvate carboxylase was found to be active in both the mitochondria and cytoplasm of epididymal adipose tissue cells; it was dependent on both ATP and biotin.	Biotin	152-158	pyruvate carboxylase	Rattus norvegicus	0-20	
9973543-2	1999	We studied the effect of biotin on the genetic expression of rat liver mitochondrial carboxylases: pyruvate carboxylase (PC), propionyl-CoA carboxylase (PCC), and 3-methylcrotonyl-CoA carboxylase (MCC).	Biotin	25-31	pyruvate carboxylase	Rattus norvegicus	99-119	
17720579-1	2007	Pyruvate carboxylase (PC) is a biotin-dependent enzyme that plays a crucial role in gluconeogenesis, lipogenesis, Krebs cycle anaplerosis and amino acid catabolism.	Biotin	31-37	pyruvate carboxylase	Rattus norvegicus	0-20	
9973543-10	1999	These results suggest that biotin regulates the expression of the catabolic carboxylases (PCC and MCC), that this regulation occurs after the posttranscriptional level, and that pyruvate carboxylase, a key enzyme for gluconeogenesis, Krebs cycle anaplerosis, and fatty acid synthesis, is spared of this control.	Biotin	27-33	pyruvate carboxylase	Rattus norvegicus	178-198	
9252365-2	1997	Pyruvate carboxylase (EC 6.4.1.1) is a biotin-containing enzyme that plays an important role in gluconeogenesis and lipogenesis.	Biotin	39-45	pyruvate carboxylase	Rattus norvegicus	0-20	
9278559-13	1997	This study provides evidence consistent with the hypothesis that chronic administration of lipoic acid lowers the activities of pyruvate carboxylase and beta-methylcrotonyl-CoA carboxylase in vivo by competing with biotin.	Biotin	215-221	pyruvate carboxylase	Rattus norvegicus	128-148	
8866570-8	1996	The amounts of mGPD protein, as judged from Western analysis, and of PC protein, as judged from probing transblots with streptavidin that binds to biotin-containing enzymes, roughly correlated with the enzyme activities.	Biotin	147-153	pyruvate carboxylase	Rattus norvegicus	69-71	
7201583-0	1982	Brain pyruvate carboxylase and the pathophysiology of biotin-dependent diseases.	Biotin	54-60	pyruvate carboxylase	Rattus norvegicus	6-26	
7201583-1	1982	Given the cerebellar symptomatology of biotin-dependent diseases and other lactic acidoses, we hypothesized that cerebellar pyruvate carboxylase activity might be differentially low or especially sensitive to cofactor deprivation.	Biotin	39-45	pyruvate carboxylase	Rattus norvegicus	124-144	
7201583-2	1982	Accordingly, pyruvate carboxylase activity was measured in selected areas of normal and biotin-deficient rat brain.	Biotin	88-94	pyruvate carboxylase	Rattus norvegicus	13-33	
7201583-4	1982	In biotin-deficient rats, hepatic pyruvate carboxylase activity was 3% of control, whereas pyruvate carboxylase activities of all brain sections were 53 to 71% of control.	Biotin	3-9	pyruvate carboxylase	Rattus norvegicus	34-54	
106342-4	1979	The highest PC activity is found in the brain stem of control and biotin-deficient rats.	Biotin	66-72	pyruvate carboxylase	Rattus norvegicus	12-14	
106342-5	1979	Normally fed rats show, shortly after birth, a maximum in liver PC activity, which is absent in biotin-deficient animals.	Biotin	96-102	pyruvate carboxylase	Rattus norvegicus	64-66	
4827253-0	1974	Activities of pyruvate carboxylase and propionyl CoA carboxylase in rat tissues during biotin deficiency and restoration of the activities after biotin administration.	Biotin	87-93	pyruvate carboxylase	Rattus norvegicus	14-34	
4827253-0	1974	Activities of pyruvate carboxylase and propionyl CoA carboxylase in rat tissues during biotin deficiency and restoration of the activities after biotin administration.	Biotin	145-151	pyruvate carboxylase	Rattus norvegicus	14-34	
2930495-3	1989	A biotin deficiency resulting in a 90% decrease in myocardial pyruvate carboxylase left the pyruvate carboxylation rate unchanged.	Biotin	2-8	pyruvate carboxylase	Rattus norvegicus	62-82