PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27043409-5	2016	Mechanistically, inhibition of Arg1 enzymatic activity disrupted multiple components of ILC2 metabolic programming by altering arginine catabolism, impairing polyamine biosynthesis and reducing aerobic glycolysis.	Polyamines	158-167	arginase, liver	Mus musculus	31-35	
22865229-2	2012	IL-4-induced activation of macrophages produced arginase-1, which converts arginine into ornithine, a precursor of polyamines and proline.	Polyamines	115-125	arginase, liver	Mus musculus	48-58	
21585399-3	2011	AAMs exert their activity in part via the enzyme arginase-1 (Arg1), which hydrolyses L-arginine into urea and ornithine, and can supply precursor substrate for proline and polyamine production.	Polyamines	172-181	arginase, liver	Mus musculus	61-65	
19360123-1	2009	Macrophage-specific expression of Arginase-1 is commonly believed to promote inflammation, fibrosis, and wound healing by enhancing L-proline, polyamine, and Th2 cytokine production.	Polyamines	143-152	arginase, liver	Mus musculus	34-44	
16845475-6	2006	Second, dramatic increases in transcripts for arginase 1 (ARG1), the enzymes of polyamine biosynthesis, and protein inhibitor of nitric oxide synthase (NOS) activity indicate that NO production may be regulated, in part, by inhibition of NOS and coordinate depletion of the NOS substrate, L: -arginine.	Polyamines	80-89	arginase, liver	Mus musculus	46-56	
16845475-6	2006	Second, dramatic increases in transcripts for arginase 1 (ARG1), the enzymes of polyamine biosynthesis, and protein inhibitor of nitric oxide synthase (NOS) activity indicate that NO production may be regulated, in part, by inhibition of NOS and coordinate depletion of the NOS substrate, L: -arginine.	Polyamines	80-89	arginase, liver	Mus musculus	58-62	
11080091-0	2000	Arginase I: a limiting factor for nitric oxide and polyamine synthesis by activated macrophages?	Polyamines	51-60	arginase, liver	Mus musculus	0-10	
11080091-2	2000	We tested whether expression of the cytosolic isoform of arginase (arginase I) was limiting for NO or polyamine production by activated RAW 264.7 macrophage cells.	Polyamines	102-111	arginase, liver	Mus musculus	67-77	
23999450-10	2014	Finally, ArgI promoted aortic vascular smooth muscle cell proliferation, which was associated with increased production of intracellular polyamines.	Polyamines	137-147	arginase, liver	Mus musculus	9-13	
23179835-9	2013	M2 macrophages constitutively produce the enzyme arginase I (argI), which sequesters L-arginine from iNOS and results in the production of ornithine and downstream polyamines and L-proline.	Polyamines	164-174	arginase, liver	Mus musculus	49-59	
12923240-11	2003	The main roles of AI are regulation of arginine concentration by degrading arginine and production of ornithine for polyamine biosynthesis, but AI may not be the principal enzyme for regulating glutamate biosynthesis in tissues and cells.	Polyamines	116-125	arginase, liver	Mus musculus	18-20	
11080091-7	2000	Thus endogenous levels of arginase I are limiting for polyamine synthesis, but not for NO synthesis, by activated macrophage cells.	Polyamines	54-63	arginase, liver	Mus musculus	26-36	
11080091-8	2000	This study also demonstrates that it is possible to alter arginase I levels sufficiently to affect polyamine synthesis without affecting induced NO synthesis.	Polyamines	99-108	arginase, liver	Mus musculus	58-68	
32553276-5	2020	Accumulation of arginase-1 in Pp6-deficient keratinocytes drove polyamine production from the urea cycle.	Polyamines	64-73	arginase, liver	Mus musculus	16-26	
26538654-5	2015	Arginase 1 (Arg1) and nitric oxide synthases compete for l-arginine to produce either polyamines or nitric oxide, respectively.	Polyamines	86-96	arginase, liver	Mus musculus	12-16	
26538654-5	2015	Arginase 1 (Arg1) and nitric oxide synthases compete for l-arginine to produce either polyamines or nitric oxide, respectively.	Polyamines	86-96	arginase, liver	Mus musculus	0-10