PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27071416-1	2016	Interferon-gamma inducible human guanylate binding protein-1 (hGBP1) shows a unique characteristic that hydrolyses GTP to a mixture of GDP and GMP through successive cleavages, with GMP being the major product.	Guanosine Diphosphate	135-138	guanylate binding protein 1	Homo sapiens	33-60	
32352209-1	2021	Human Guanylate-Binding Protein 1 (hGBP-1) shows a dimer-induced acceleration of the GTPase activity yielding GDP as well as GMP.	Guanosine Diphosphate	110-113	guanylate binding protein 1	Homo sapiens	6-33	
32352209-1	2021	Human Guanylate-Binding Protein 1 (hGBP-1) shows a dimer-induced acceleration of the GTPase activity yielding GDP as well as GMP.	Guanosine Diphosphate	110-113	guanylate binding protein 1	Homo sapiens	35-41	
10493878-3	1999	The unique position of hGBP1 amongst known GTPases is further demonstrated by the hydrolysis of GTP to GDP and GMP.	Guanosine Diphosphate	103-106	guanylate binding protein 1	Homo sapiens	23-28	
10493878-10	1999	By means of fluorescence and NMR spectroscopy it is demonstrated that aluminium fluoride forms a complex with hGBP1 only in the GDP state, presumably mimicking the transition state of GTP hydrolysis.	Guanosine Diphosphate	128-131	guanylate binding protein 1	Homo sapiens	110-115	
7512561-1	1994	hGBP1 is an interferon-induced 67-kDa protein of human cells that readily binds to agarose-immobilized GTP, GDP, and GMP but not to other nucleotides.	Guanosine Diphosphate	108-111	guanylate binding protein 1	Homo sapiens	0-5	
33113220-2	2021	The distinctive feature of a large GTPase, human guanylate binding protein-1 (hGBP1), is the sequential hydrolysis of GTP into GMP via GDP.	Guanosine Diphosphate	135-138	guanylate binding protein 1	Homo sapiens	49-76	
33113220-2	2021	The distinctive feature of a large GTPase, human guanylate binding protein-1 (hGBP1), is the sequential hydrolysis of GTP into GMP via GDP.	Guanosine Diphosphate	135-138	guanylate binding protein 1	Homo sapiens	78-83	
28451182-7	2017	The subsequent GDP hydrolysis in hGBP1 was also found to follow a water-mediated proton shuttle mechanism.	Guanosine Diphosphate	15-18	guanylate binding protein 1	Homo sapiens	33-38	
27071416-1	2016	Interferon-gamma inducible human guanylate binding protein-1 (hGBP1) shows a unique characteristic that hydrolyses GTP to a mixture of GDP and GMP through successive cleavages, with GMP being the major product.	Guanosine Diphosphate	135-138	guanylate binding protein 1	Homo sapiens	62-67	
20923658-2	2010	Human guanylate binding proteins (hGBP-1 and 2) belonging to large GTPases have the unique feature of hydrolyzing GTP to a mixture of GDP and GMP with unequal ratios.	Guanosine Diphosphate	134-137	guanylate binding protein 1	Homo sapiens	34-46	
25081641-3	2015	Since GBP1 is a large GTPase which undergoes conformational changes in a nucleotide-dependent manner, we investigated the effect of GTP/GDP binding on GBP1:PIM1 interaction by using computational and biological studies.	Guanosine Diphosphate	136-139	guanylate binding protein 1	Homo sapiens	6-10	
25081641-3	2015	Since GBP1 is a large GTPase which undergoes conformational changes in a nucleotide-dependent manner, we investigated the effect of GTP/GDP binding on GBP1:PIM1 interaction by using computational and biological studies.	Guanosine Diphosphate	136-139	guanylate binding protein 1	Homo sapiens	151-155	
21142871-2	2011	Structural and biochemical analyses of human GBP-1 subsequently demonstrated that the GBPs are a unique subfamily of guanosine triphosphatase (GTPases) that hydrolyze guanosine triphosphate (GTP) to both guanosine diphosphate (GDP) and GMP.	Guanosine Diphosphate	204-225	guanylate binding protein 1	Homo sapiens	45-50	
21142871-2	2011	Structural and biochemical analyses of human GBP-1 subsequently demonstrated that the GBPs are a unique subfamily of guanosine triphosphatase (GTPases) that hydrolyze guanosine triphosphate (GTP) to both guanosine diphosphate (GDP) and GMP.	Guanosine Diphosphate	227-230	guanylate binding protein 1	Homo sapiens	45-50	
22859948-2	2012	Unlike all other GTPases, hGBP1 hydrolyzes GTP to a mixture of GDP and GMP with GMP being the major product at 37 C but GDP became significant when the hydrolysis reaction was carried out at 15 C. The hydrolysis reaction in hGBP1 is believed to involve with a number of catalytic steps.	Guanosine Diphosphate	63-66	guanylate binding protein 1	Homo sapiens	26-31	
22859948-2	2012	Unlike all other GTPases, hGBP1 hydrolyzes GTP to a mixture of GDP and GMP with GMP being the major product at 37 C but GDP became significant when the hydrolysis reaction was carried out at 15 C. The hydrolysis reaction in hGBP1 is believed to involve with a number of catalytic steps.	Guanosine Diphosphate	120-123	guanylate binding protein 1	Homo sapiens	26-31	
22859948-6	2012	Denaturation studies of different catalytic complexes show that unlike other complexes the free energy of GDP-bound hGBP1 decreases significantly at lower temperature.	Guanosine Diphosphate	106-109	guanylate binding protein 1	Homo sapiens	116-121	
16873363-4	2006	The unique result of GTP hydrolysis catalyzed by hGBP1 is GDP and GMP.	Guanosine Diphosphate	58-61	guanylate binding protein 1	Homo sapiens	49-54	
19150356-1	2009	Unlike other GTPases, interferon-gamma-induced human guanylate binding protein-1 has the ability to hydrolyze GTP to both GDP and GMP, with GMP being the major product of the reaction.	Guanosine Diphosphate	122-125	guanylate binding protein 1	Homo sapiens	53-80	
16873363-13	2006	The assembled forms of the GDP- and GMP-bound states of hGBP1 are accessible only through GTP binding and hydrolysis and achieve a lifetime of a few seconds.	Guanosine Diphosphate	27-30	guanylate binding protein 1	Homo sapiens	56-61	
16511497-4	2006	Here we show that the isolated amino-terminal G domain of hGBP1 retains the main enzymatic properties of the full-length protein and can cleave GDP directly.	Guanosine Diphosphate	144-147	guanylate binding protein 1	Homo sapiens	58-63