PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
8694760-2	1996	produced during the catalytic activity of nitric oxide synthase (NOS) and cytochrome P-450 has been implicated in the oxidative denitrification of hydroxyguanidines ( > C = NOH).	hydroxyguanidine	147-164	nitric oxide synthase 2	Homo sapiens	42-63
10937746-0	2000	Metalloporphyrin catalyzed oxidation of N-hydroxyguanidines: a biomimetic model for the H2O2-dependent activity of nitric oxide synthase.	hydroxyguanidine	40-59	nitric oxide synthase 2	Homo sapiens	115-136
10424762-7	1999	While the N-hydroxylation of the guanidine involves the usual monooxygenase activity of cytochrome P-450 (Clement et al., Biochem Pharmacol 46: 2249-2267, 1993), the resultant N-hydroxyguanidine decoupled the monooxygenase.	hydroxyguanidine	176-194	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	88-104
10424762-13	1999	In conclusion, similarities (formation of a urea derivative) and differences (formation of a cyanamide derivative) between the physiological oxidation of N-hydroxy-L-arginine by nitric oxide synthases and non-physiological N-hydroxyguanidines by cytochrome P-450 were observed.	hydroxyguanidine	223-242	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	246-262
8694760-2	1996	produced during the catalytic activity of nitric oxide synthase (NOS) and cytochrome P-450 has been implicated in the oxidative denitrification of hydroxyguanidines ( > C = NOH).	hydroxyguanidine	147-164	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	74-90
8274159-0	1993	Cytochrome P450 dependent N-hydroxylation of a guanidine (debrisoquine), microsomal catalysed reduction and further oxidation of the N-hydroxy-guanidine metabolite to the urea derivative.	hydroxyguanidine	133-152	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	11-15
8274159-8	1993	Whereas the N-hydroxylation of the guanidine involves the usual monooxygenase activity of cytochrome P450 the resultant N-hydroxyguanidine decouples monooxygenases (cytochrome P450, FMO) and the H2O2 and, above all, O2- thus formed transform the N-hydroxyguanidine further to the corresponding urea derivative.	hydroxyguanidine	120-138	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	101-105
8274159-8	1993	Whereas the N-hydroxylation of the guanidine involves the usual monooxygenase activity of cytochrome P450 the resultant N-hydroxyguanidine decouples monooxygenases (cytochrome P450, FMO) and the H2O2 and, above all, O2- thus formed transform the N-hydroxyguanidine further to the corresponding urea derivative.	hydroxyguanidine	120-138	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	176-180
24649802-3	2014	Potential advantages of including the N-hydroxyguanidine moiety in neuraminidase inhibitors are also discussed.	hydroxyguanidine	38-56	neuraminidase 1	Homo sapiens	67-80
31841335-4	2020	Together with its developed N-hydroxyguanidine prodrug 11, 8a will serve as a most widely applicable, currently available pharmacological tool to target DDAH-1-associated diseases.	hydroxyguanidine	28-46	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	153-159
19178946-0	2009	N-Hydroxyguanidines oxidation by a N3S copper-complex mimicking the reactivity of Dopamine beta-Hydroxylase.	hydroxyguanidine	0-19	dopamine beta-hydroxylase	Homo sapiens	82-107
23782349-3	2013	Here, we developed N-hydroxyguanidine NO donor drugs that were protected against spontaneous NO release by linkage to glutamyl adducts that could be cleaved by gamma-glutamyl transpeptidase (gamma-GT), found predominantly in renal tissue.	hydroxyguanidine	19-37	inactive glutathione hydrolase 2	Homo sapiens	160-189
23782349-3	2013	Here, we developed N-hydroxyguanidine NO donor drugs that were protected against spontaneous NO release by linkage to glutamyl adducts that could be cleaved by gamma-glutamyl transpeptidase (gamma-GT), found predominantly in renal tissue.	hydroxyguanidine	19-37	inactive glutathione hydrolase 2	Homo sapiens	191-199
23322269-1	2013	This communication describes the synthesis of a new class of N-hydroxyguanidine (NHG) pro-drugs which release nitric oxide (NO), triggered by the action of gamma-glutamyl transpeptidase (gamma-GT), and have potential for the treatment of acute renal injury/failure (ARI/ARF).	hydroxyguanidine	61-79	inactive glutathione hydrolase 2	Homo sapiens	156-185
23322269-1	2013	This communication describes the synthesis of a new class of N-hydroxyguanidine (NHG) pro-drugs which release nitric oxide (NO), triggered by the action of gamma-glutamyl transpeptidase (gamma-GT), and have potential for the treatment of acute renal injury/failure (ARI/ARF).	hydroxyguanidine	61-79	inactive glutathione hydrolase 2	Homo sapiens	187-195
23322269-1	2013	This communication describes the synthesis of a new class of N-hydroxyguanidine (NHG) pro-drugs which release nitric oxide (NO), triggered by the action of gamma-glutamyl transpeptidase (gamma-GT), and have potential for the treatment of acute renal injury/failure (ARI/ARF).	hydroxyguanidine	81-84	inactive glutathione hydrolase 2	Homo sapiens	156-185
23322269-1	2013	This communication describes the synthesis of a new class of N-hydroxyguanidine (NHG) pro-drugs which release nitric oxide (NO), triggered by the action of gamma-glutamyl transpeptidase (gamma-GT), and have potential for the treatment of acute renal injury/failure (ARI/ARF).	hydroxyguanidine	81-84	inactive glutathione hydrolase 2	Homo sapiens	187-195
20630600-6	2010	Tyr588Phe mutant binds L-Arg and NOHA with much weaker affinities than WT nNOS but both proteins bind non alpha-amino acid guanidines and N-hydroxyguanidines with close affinities.	hydroxyguanidine	138-157	nitric oxide synthase 1	Rattus norvegicus	74-78
19693765-0	2009	The peptidylglycine alpha-amidating monooxygenase (PAM): a novel prodrug strategy for amidoximes and N-hydroxyguanidines?	hydroxyguanidine	101-120	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	4-49
19693765-0	2009	The peptidylglycine alpha-amidating monooxygenase (PAM): a novel prodrug strategy for amidoximes and N-hydroxyguanidines?	hydroxyguanidine	101-120	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	51-54
20630600-7	2010	WT nNOS and mutant do not form NO from the tested guanidines but oxidize several N-hydroxyguanidines with formation of NO in almost identical rates.	hydroxyguanidine	81-100	nitric oxide synthase 1	Rattus norvegicus	3-7
15955074-8	2005	The k(cat) values of NO production from the oxidation by iNOS of the studied N-hydroxyguanidines were found to vary independently of their affinity for the protein.	hydroxyguanidine	77-96	nitric oxide synthase 2	Homo sapiens	57-61
15955074-11	2005	These data indicate that a key factor for efficient oxidation of a guanidine by iNOS to NO is the ability of the corresponding N-hydroxyguanidine to bind to the active site without being too rapidly released before its further oxidation.	hydroxyguanidine	127-145	nitric oxide synthase 2	Homo sapiens	80-84
15955074-12	2005	This explains why 4,4,4-trifluorobutylguanidine is so far the best non-alpha-amino acid guanidine substrate of iNOS with formation of NO, because the k(off) (app) of the corresponding N-hydroxyguanidine is particularly low.	hydroxyguanidine	184-202	nitric oxide synthase 2	Homo sapiens	111-115
12437343-4	2002	However, the former binds to nNOS in an unexpected fashion, thus providing new insights into the mechanism on how the hydroxyguanidine moiety leads to NO formation.	hydroxyguanidine	118-134	nitric oxide synthase 1	Homo sapiens	29-33
15219986-4	2004	We characterized these proteins and tested their ability to generate NO from the oxidation of natural substrates L-Arg and NOHA, and from N-hydroxyguanidines previously identified as alternative substrates for nNOS.	hydroxyguanidine	138-157	nitric oxide synthase 1	Rattus norvegicus	210-214
15955074-0	2005	Relationship between the structure of guanidines and N-hydroxyguanidines, their binding to inducible nitric oxide synthase (iNOS) and their iNOS-catalysed oxidation to NO.	hydroxyguanidine	53-72	nitric oxide synthase 2	Homo sapiens	91-122
15955074-0	2005	Relationship between the structure of guanidines and N-hydroxyguanidines, their binding to inducible nitric oxide synthase (iNOS) and their iNOS-catalysed oxidation to NO.	hydroxyguanidine	53-72	nitric oxide synthase 2	Homo sapiens	124-128
15955074-0	2005	Relationship between the structure of guanidines and N-hydroxyguanidines, their binding to inducible nitric oxide synthase (iNOS) and their iNOS-catalysed oxidation to NO.	hydroxyguanidine	53-72	nitric oxide synthase 2	Homo sapiens	140-144
15955074-1	2005	The binding of several alkyl- and aryl-guanidines and N-hydroxyguanidines to the oxygenase domain of inducible NO-synthase (iNOS(oxy)) was studied by UV/Vis difference spectroscopy.	hydroxyguanidine	54-73	nitric oxide synthase 2	Homo sapiens	101-122
15955074-1	2005	The binding of several alkyl- and aryl-guanidines and N-hydroxyguanidines to the oxygenase domain of inducible NO-synthase (iNOS(oxy)) was studied by UV/Vis difference spectroscopy.	hydroxyguanidine	54-73	nitric oxide synthase 2	Homo sapiens	124-128
15955074-2	2005	In a very general manner, monosubstituted guanidines exhibited affinities for iNOS(oxy) that were very close to those of the corresponding N-hydroxyguanidines.	hydroxyguanidine	139-158	nitric oxide synthase 2	Homo sapiens	78-82
12667076-2	2003	N-Hydroxyguanidines interact with the oxygenase domain of BH(4)-free inducible NOS (BH(4)-free iNOS(oxy)), depending on the nature of their substituent, with formation of two types of complexes that are characterized by peaks around 395 (type I) and 438 nm (type II") during difference visible spectroscopy.	hydroxyguanidine	0-19	nitric oxide synthase 2	Homo sapiens	95-99
12667076-5	2003	Similar iron(III)-ligand complexes were formed upon reaction of 1 and several other N-hydroxyguanidines with BH(4)-free full-length iNOS and BH(4)-free nNOS(oxy).	hydroxyguanidine	84-103	nitric oxide synthase 2	Homo sapiens	132-136
12667076-11	2003	Comparison of the spectral and physicochemical properties of the N-hydroxyguanidine complexes of BH(4)-free iNOS(oxy) (type II") with those of the previously described corresponding complexes of microperoxidase (MP-8) suggests that, in both cases, N-hydroxyguanidines bind to iron(III) via their oxygen atom after deprotonation or weakening of the O-H bond.	hydroxyguanidine	65-83	nitric oxide synthase 2	Homo sapiens	108-112
12667076-11	2003	Comparison of the spectral and physicochemical properties of the N-hydroxyguanidine complexes of BH(4)-free iNOS(oxy) (type II") with those of the previously described corresponding complexes of microperoxidase (MP-8) suggests that, in both cases, N-hydroxyguanidines bind to iron(III) via their oxygen atom after deprotonation or weakening of the O-H bond.	hydroxyguanidine	248-267	nitric oxide synthase 2	Homo sapiens	108-112
12214669-4	2002	By contrast, NO synthase (NOS) containing BH4 catalyze the selective monooxygenation of some N-hydroxyguanidines by NADPH and O2 with formation of NO and the corresponding ureas in a 1:1 molar ratio.	hydroxyguanidine	93-112	nitric oxide synthase 2	Homo sapiens	13-24