PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
10465698-1	1999	We have measured the expression and activity of peptidylarginine deiminase (PAD, EC 3.5.3.15), the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate.	arginyl	133-140	paddle	Mus musculus	48-74
13130468-2	2003	Citrulline is a nonstandard amino acid that can be incorporated into proteins only by posttranslational modification of arginine by peptidylarginine deiminase (PAD) enzymes.	Citrulline	0-10	paddle	Mus musculus	132-158
13130468-2	2003	Citrulline is a nonstandard amino acid that can be incorporated into proteins only by posttranslational modification of arginine by peptidylarginine deiminase (PAD) enzymes.	Citrulline	0-10	paddle	Mus musculus	160-163
13130468-2	2003	Citrulline is a nonstandard amino acid that can be incorporated into proteins only by posttranslational modification of arginine by peptidylarginine deiminase (PAD) enzymes.	Arginine	120-128	paddle	Mus musculus	132-158
13130468-2	2003	Citrulline is a nonstandard amino acid that can be incorporated into proteins only by posttranslational modification of arginine by peptidylarginine deiminase (PAD) enzymes.	Arginine	120-128	paddle	Mus musculus	160-163
12654293-0	2003	ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets.	epad	0-4	paddle	Mus musculus	42-68
12654293-3	2003	Comparison of the deduced amino acid sequence with the nonredundant database demonstrated that the protein was approximately 40% identical to the calcium-dependent peptidylarginine deiminase (PAD) enzyme family.	Calcium	146-153	paddle	Mus musculus	164-190
12654293-3	2003	Comparison of the deduced amino acid sequence with the nonredundant database demonstrated that the protein was approximately 40% identical to the calcium-dependent peptidylarginine deiminase (PAD) enzyme family.	Calcium	146-153	paddle	Mus musculus	192-195
10465698-1	1999	We have measured the expression and activity of peptidylarginine deiminase (PAD, EC 3.5.3.15), the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate.	arginyl	133-140	paddle	Mus musculus	76-79
10465698-1	1999	We have measured the expression and activity of peptidylarginine deiminase (PAD, EC 3.5.3.15), the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate.	Citrulline	165-176	paddle	Mus musculus	48-74
10465698-1	1999	We have measured the expression and activity of peptidylarginine deiminase (PAD, EC 3.5.3.15), the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate.	Citrulline	165-176	paddle	Mus musculus	76-79
7872804-6	1995	However, the alpha-amino group of the amino-terminal methionine residue of the recombinant PAD was not acetylated as was that of the native enzyme.	Methionine	53-63	paddle	Mus musculus	91-94
3935304-5	1985	A modified medium (mPA-D; addition of cetrimide, omission of sulphapyridine and actidione) was more selective and sufficiently recovered noninjured cells.	Cetrimonium	38-47	paddle	Mus musculus	19-24
3085589-1	1986	In the present study, mPA-D and mPA-E agar, modifications of mPA-C agar that reduce background fecal streptococci that interfere with the differentiation and enumeration of the Pseudomonas aeruginosa colonies grown in other mPA media, are proposed for use in analyzing natural water samples.	Agar	67-71	paddle	Mus musculus	22-27
3935304-5	1985	A modified medium (mPA-D; addition of cetrimide, omission of sulphapyridine and actidione) was more selective and sufficiently recovered noninjured cells.	Cycloheximide	80-89	paddle	Mus musculus	19-24
27819302-3	2016	We recently found that Cl-amidine, a peptidylarginine deiminase (PAD) inhibitor, improves survival in a mouse model of cecal ligation and puncture (CLP)-induced septic shock.	N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide	23-33	paddle	Mus musculus	37-63
27819302-3	2016	We recently found that Cl-amidine, a peptidylarginine deiminase (PAD) inhibitor, improves survival in a mouse model of cecal ligation and puncture (CLP)-induced septic shock.	N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide	23-33	paddle	Mus musculus	65-68
23722903-5	2013	NZM mice were treated with Cl-amidine, an inhibitor of peptidylarginine deiminases (PAD), to block NET formation and were evaluated for lupus-like disease activity, endothelial function, and prothrombotic phenotype.	N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide	27-37	paddle	Mus musculus	55-82
23722903-5	2013	NZM mice were treated with Cl-amidine, an inhibitor of peptidylarginine deiminases (PAD), to block NET formation and were evaluated for lupus-like disease activity, endothelial function, and prothrombotic phenotype.	N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide	27-37	paddle	Mus musculus	84-87
19093029-3	2008	Deimination, the conversion of protein-bound arginine to citrulline, is mediated by the peptidylarginine deiminase (PAD) family of enzymes, of which the PAD2 and PAD4 isoforms are present in myelin.	Arginine	45-53	paddle	Mus musculus	88-114
19093029-3	2008	Deimination, the conversion of protein-bound arginine to citrulline, is mediated by the peptidylarginine deiminase (PAD) family of enzymes, of which the PAD2 and PAD4 isoforms are present in myelin.	Arginine	45-53	paddle	Mus musculus	116-119
19093029-3	2008	Deimination, the conversion of protein-bound arginine to citrulline, is mediated by the peptidylarginine deiminase (PAD) family of enzymes, of which the PAD2 and PAD4 isoforms are present in myelin.	Citrulline	57-67	paddle	Mus musculus	88-114
19093029-3	2008	Deimination, the conversion of protein-bound arginine to citrulline, is mediated by the peptidylarginine deiminase (PAD) family of enzymes, of which the PAD2 and PAD4 isoforms are present in myelin.	Citrulline	57-67	paddle	Mus musculus	116-119
428003-3	1979	Two strains of L5178Y murine lymphoma, inversely cross-sensitive to X-rays and UV light, were shown previously to respond to treatment with an antitumour platinum complex, cis-dichlorobis(cyclopentylamine)-platinum(II) (cis-PAD), in a similar manner as to UV.	Platinum	154-162	paddle	Mus musculus	224-227
428003-3	1979	Two strains of L5178Y murine lymphoma, inversely cross-sensitive to X-rays and UV light, were shown previously to respond to treatment with an antitumour platinum complex, cis-dichlorobis(cyclopentylamine)-platinum(II) (cis-PAD), in a similar manner as to UV.	dichlorobis(cyclopentylamine)platinum	172-214	paddle	Mus musculus	224-227
428003-4	1979	Enhancement of chromosomal damage and potentiation of lethal effect of cis-PAD by 0.75 mM caffeine were found in cis-PAD and UV light-resistant L5178Y-S strain but not in cis-PAD and UV light-sensitive L5178Y-R strain.	Caffeine	90-98	paddle	Mus musculus	75-78
428003-4	1979	Enhancement of chromosomal damage and potentiation of lethal effect of cis-PAD by 0.75 mM caffeine were found in cis-PAD and UV light-resistant L5178Y-S strain but not in cis-PAD and UV light-sensitive L5178Y-R strain.	Caffeine	90-98	paddle	Mus musculus	117-120
428003-4	1979	Enhancement of chromosomal damage and potentiation of lethal effect of cis-PAD by 0.75 mM caffeine were found in cis-PAD and UV light-resistant L5178Y-S strain but not in cis-PAD and UV light-sensitive L5178Y-R strain.	Caffeine	90-98	paddle	Mus musculus	117-120
428003-5	1979	These results suggest that the extreme sensitivity of L5178Y-R strain to cis-PAD and UV light is caused to some extent by deficiency in a caffeine-sensitive post-replication repair system.	Caffeine	138-146	paddle	Mus musculus	77-80
31764615-1	2020	BACKGROUND: The peptidylarginine deiminase (PAD) family converts arginine into citrulline through protein citrullination.	Arginine Vasopressin	24-32	paddle	Mus musculus	44-47
30285515-2	2019	METHODS: Cl-amidine, a PAD inhibitor, was injected into pGIA.	N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide	9-19	paddle	Mus musculus	23-26
29293656-7	2018	Pharmacological treatment of mice with the protein arginine deiminase (PAD)-inhibitor Cl-amidine abrogated NET formation, reduced arterial thrombosis and limited injury in a model of myocardial infarction.	N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide	86-96	paddle	Mus musculus	71-74
21697043-1	2011	Deimination, the conversion of protein-bound arginines into citrullines, is a post-translational modification catalyzed by a peptidylarginine deiminase (Pad).	Arginine	45-54	paddle	Mus musculus	125-151
21697043-1	2011	Deimination, the conversion of protein-bound arginines into citrullines, is a post-translational modification catalyzed by a peptidylarginine deiminase (Pad).	Arginine	45-54	paddle	Mus musculus	153-156
21697043-1	2011	Deimination, the conversion of protein-bound arginines into citrullines, is a post-translational modification catalyzed by a peptidylarginine deiminase (Pad).	Citrulline	60-71	paddle	Mus musculus	125-151
21697043-1	2011	Deimination, the conversion of protein-bound arginines into citrullines, is a post-translational modification catalyzed by a peptidylarginine deiminase (Pad).	Citrulline	60-71	paddle	Mus musculus	153-156