PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16569739-6	2006	The position of arginine at codon 96 was modeled using the CYP17 structure 2c17 (www.rcsb.org).	Arginine	16-24	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	59-64	
16176874-7	2005	Analysis of the CYP17 gene by polymerase chain reaction amplification and direct sequencing demonstrated a novel homozygous mutation of codon 440 from CGC (Arg) to TGC (Cys) in both patients.	Arginine	156-159	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	16-21	
15555906-4	2004	In the present study it was found that substitution of human CYP17 amino acids, Arg(347), Arg(358) and Arg(449), with non-cationic residues, yielded variants that were impaired in the two acyl-carbon bond cleavage activities, quantitatively to the same extent and these were reduced to between 3 and 4% of the wild-type protein.	Arginine	80-83	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	61-66	
15555906-4	2004	In the present study it was found that substitution of human CYP17 amino acids, Arg(347), Arg(358) and Arg(449), with non-cationic residues, yielded variants that were impaired in the two acyl-carbon bond cleavage activities, quantitatively to the same extent and these were reduced to between 3 and 4% of the wild-type protein.	Arginine	90-93	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	61-66	
15555906-4	2004	In the present study it was found that substitution of human CYP17 amino acids, Arg(347), Arg(358) and Arg(449), with non-cationic residues, yielded variants that were impaired in the two acyl-carbon bond cleavage activities, quantitatively to the same extent and these were reduced to between 3 and 4% of the wild-type protein.	Arginine	90-93	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	61-66	
15555906-7	2004	The results suggest that the bifurcated cationic charges at Arg(347), Arg(358) and Arg(449) make important contributions to the formation of catalytically competent CYP17.cytochrome b(5) complex.	Arginine	60-63	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	165-170	
15555906-7	2004	The results suggest that the bifurcated cationic charges at Arg(347), Arg(358) and Arg(449) make important contributions to the formation of catalytically competent CYP17.cytochrome b(5) complex.	Arginine	70-73	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	165-170	
15555906-7	2004	The results suggest that the bifurcated cationic charges at Arg(347), Arg(358) and Arg(449) make important contributions to the formation of catalytically competent CYP17.cytochrome b(5) complex.	Arginine	70-73	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	165-170	
12446594-8	2002	Surprisingly, the greatest difference in enzymatic activities was a marked increase in 17alpha-hydroxylase activity of P450c17 in the baboon, which differs from rhesus only at residue 255 [arginine (Arg) in baboon, histine (His) in rhesus].	Arginine	189-197	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	119-126	
12446594-8	2002	Surprisingly, the greatest difference in enzymatic activities was a marked increase in 17alpha-hydroxylase activity of P450c17 in the baboon, which differs from rhesus only at residue 255 [arginine (Arg) in baboon, histine (His) in rhesus].	Arginine	199-202	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	119-126	
32820515-5	2020	RESULTS: Sanger sequencing revealed that the patient has carried homozygous variant c.1486C>T in the exon 8 of the CYP17A1 gene, which resulted in substitution of arginine by cysteine (p.Arg496Cys).	Arginine	163-171	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	115-122	
10455016-2	1999	Single amino acid mutations in human CYP17, Arg(347)-->His and Arg(358)-->Gln, have been reported to result in the loss of the lyase activity and to cause sexual phenotypic changes in 46XY male patients.	Arginine	44-47	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	37-42	
10455016-2	1999	Single amino acid mutations in human CYP17, Arg(347)-->His and Arg(358)-->Gln, have been reported to result in the loss of the lyase activity and to cause sexual phenotypic changes in 46XY male patients.	Arginine	66-69	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	37-42	
10455016-3	1999	By using site-directed mutagenesis we show here that another mutation in human CYP17, Arg(449)-->Ala, for which human variants have yet not been described, also leads to selective lyase deficiency.	Arginine	86-89	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	79-84	
10455016-5	1999	That the defect could be essentially reversed by lysine mutagenesis has led to the conclusion that the cationic charges on all three residues (at the positions of Arg(347), Arg(358), Arg(449)) are vital for the functional interaction of CYP17 with cytochrome b(5) and that the loss of any one of these cationic charges is catastrophic.	Arginine	163-166	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	237-242	
10455016-5	1999	That the defect could be essentially reversed by lysine mutagenesis has led to the conclusion that the cationic charges on all three residues (at the positions of Arg(347), Arg(358), Arg(449)) are vital for the functional interaction of CYP17 with cytochrome b(5) and that the loss of any one of these cationic charges is catastrophic.	Arginine	173-176	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	237-242	
10455016-5	1999	That the defect could be essentially reversed by lysine mutagenesis has led to the conclusion that the cationic charges on all three residues (at the positions of Arg(347), Arg(358), Arg(449)) are vital for the functional interaction of CYP17 with cytochrome b(5) and that the loss of any one of these cationic charges is catastrophic.	Arginine	173-176	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	237-242	
8027220-4	1994	Analysis of her P450c17 gene by polymerase chain reaction amplification and direct sequencing showed mutation of codon 440 from CGC (Arg) to CAC (His).	Arginine	133-136	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	16-23	
28992603-4	2017	Moreover, two SNPs (CYP17 -34 T:C (MSP AI) and CYP19 T:C (Trp:Arg)) of cytochrome P450, which is involved in steroid metabolism pathways, were analysed between the groups.	Arginine	62-65	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	20-25	
19636199-4	2009	The molecular analysis of CYP17A1 revealed a novel homozygous missense mutation resulting in the substitution of arginine to lysine at the amino acid position 21 (p.R21L).	Arginine	113-121	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	26-33