PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19284878-10	2009	Other findings indicated that the mechanisms by which NO activates KATP channels involve direct S-nitrosylation of cysteine residues in the SUR1 subunit.	Cysteine	115-123	ATP binding cassette subfamily C member 8	Homo sapiens	140-144	
21199866-12	2011	The mutant allele only contains a mutation in a conserved amino-terminal cysteine, producing SUR1 that fails to reach the cell surface.	Cysteine	73-81	ATP binding cassette subfamily C member 8	Homo sapiens	93-97	
20863361-8	2010	One patient had a heterozygous mutation leading to the substitution of arginine at residue 1530 of SUR1 (ABCC8) by cysteine.	Cysteine	115-123	ATP binding cassette subfamily C member 8	Homo sapiens	99-103	
20863361-8	2010	One patient had a heterozygous mutation leading to the substitution of arginine at residue 1530 of SUR1 (ABCC8) by cysteine.	Cysteine	115-123	ATP binding cassette subfamily C member 8	Homo sapiens	105-110	
19284878-13	2009	CONCLUSION: NO activates KATP channels in large DRG neurons via direct S-nitrosylation of cysteine residues in the SUR1 subunit.	Cysteine	90-98	ATP binding cassette subfamily C member 8	Homo sapiens	115-119	
10570926-4	1999	However, when the cysteine residue in the Walker A motif of the first nucleotide binding fold (NBF1) of SUR1 was replaced with serine (C717S), photoaffinity labeling was not inhibited by 100 microM NEM.	Cysteine	18-26	ATP binding cassette subfamily C member 8	Homo sapiens	104-108