PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17463333-10	2007	CONCLUSION: In contrast to vitamin C treatment, augmenting BH4 levels in the endothelium by GCH overexpression reduced the accelerated atherosclerotic lesion formation in ApoE-KO/eNOS-Tg mice, associated with a reduction of superoxide production from uncoupled eNOS.	Superoxides	224-234	GTP cyclohydrolase 1	Mus musculus	92-95	
18824773-5	2008	METHODS AND RESULTS: Endothelium-targeted overexpression of GTP cyclohydrolase 1 (GCH), the rate limiting enzyme in BH4 synthesis, increased levels of tetrahydrobiopterin (BH4), reduced endothelial superoxide, improved eNOS coupling, and reduced vein graft atherosclerosis in transgenic GCH/ApoE-KO mice compared to ApoE-KO controls.	Superoxides	198-208	GTP cyclohydrolase 1	Mus musculus	60-80	
18824773-5	2008	METHODS AND RESULTS: Endothelium-targeted overexpression of GTP cyclohydrolase 1 (GCH), the rate limiting enzyme in BH4 synthesis, increased levels of tetrahydrobiopterin (BH4), reduced endothelial superoxide, improved eNOS coupling, and reduced vein graft atherosclerosis in transgenic GCH/ApoE-KO mice compared to ApoE-KO controls.	Superoxides	198-208	GTP cyclohydrolase 1	Mus musculus	82-85	
18268143-11	2008	CONCLUSIONS: These results demonstrate that endothelium-specific GTPCH I overexpression abrogates O2(-) production and preserves eNOS phosphorylation, which results in preserved structural and functional integrity of resistance mesenteric arteries and lowered blood pressure in low-renin hypertension.	Superoxides	98-103	GTP cyclohydrolase 1	Mus musculus	65-72	
18645049-1	2008	GTP cyclohydrolase 1 (GTPCH1) is the rate-limiting enzyme in de novo synthesis of tetrahydrobiopterin (BH4), an essential cofactor for endothelial NO synthase (eNOS) dictating, at least partly, the balance of NO and superoxide produced by this enzyme.	Superoxides	216-226	GTP cyclohydrolase 1	Mus musculus	0-20	
18645049-1	2008	GTP cyclohydrolase 1 (GTPCH1) is the rate-limiting enzyme in de novo synthesis of tetrahydrobiopterin (BH4), an essential cofactor for endothelial NO synthase (eNOS) dictating, at least partly, the balance of NO and superoxide produced by this enzyme.	Superoxides	216-226	GTP cyclohydrolase 1	Mus musculus	22-28	
18645049-7	2008	BH4 reduction induced by GTPCH1 siRNA injection was associated with increased aortic levels of superoxide, 3-nitrotyrosine, and adhesion molecules (intercellular adhesion molecule 1 and vascular cell adhesion molecule 1), as well as a significantly elevated systolic, diastolic, and mean BP in C57BL6 mice.	Superoxides	95-105	GTP cyclohydrolase 1	Mus musculus	25-31	
34275335-6	2021	The GCH1 (guanosine triphosphate cyclohydrolase I)-mediated biosynthesis of tetrahydrobiopterin was enhanced, reducing intracellular superoxide.	Superoxides	133-143	GTP cyclohydrolase 1	Mus musculus	4-8	
24644242-11	2014	Our results demonstrate that the GTPCH I/BH4 pathway is critical to preserve EPC quantity, function, and regenerative capacity during wound healing in type 1 diabetic mice at least partly through the attenuation of superoxide and TSP-1 levels and augmentation of NO level.	Superoxides	215-225	GTP cyclohydrolase 1	Mus musculus	33-40	
28104455-6	2017	Knockdown of GTPCH by >90% led to marked loss of cellular BH4 and a striking induction of O2- generation in the mitochondria of murine endothelial cells.	Superoxides	93-95	GTP cyclohydrolase 1	Mus musculus	13-18	
25451639-7	2015	Incubation of Gch1(fl/fl)Tie2cre macrophages with dihydroethidium revealed significantly increased production of superoxide in the presence of iNOS expression, and an iNOS-independent, BH4-dependent increase in other ROS species.	Superoxides	113-123	GTP cyclohydrolase 1	Mus musculus	14-18	
21059996-7	2010	eNOS(-/-)/GCH(+/-) hybrid mice demonstrated that GTPCH preserved the circulating EPC number, reduced intracellular O2- in EPCs, and ameliorated EPC dysfunction independent of eNOS in DOCA-salt hypertension.	Superoxides	115-117	GTP cyclohydrolase 1	Mus musculus	49-54