PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15724974-2	2005	While studying the effect of the endogenously occurring S-nitroso-l-homocysteine on DDAH-1, an unusual N-thiosulfoximide modification was identified in the active site of the enzyme.	n-thiosulfoximide	103-120	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	84-90	
17600152-3	2007	Recently, we have reported on the formation of such a product, an N-thiosulfoximide, at the active site of the Cys hydrolase dimethylargininase-1 (DDAH-1) upon reaction with S-nitroso-l-homocysteine (HcyNO).	n-thiosulfoximide	66-83	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	125-145	
17600152-3	2007	Recently, we have reported on the formation of such a product, an N-thiosulfoximide, at the active site of the Cys hydrolase dimethylargininase-1 (DDAH-1) upon reaction with S-nitroso-l-homocysteine (HcyNO).	n-thiosulfoximide	66-83	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	147-153	
17600152-5	2007	Further, to explore the reason responsible for the unique formation of an N-thiosulfoximide in DDAH-1 we have expanded these studies to cytidine triphosphate synthetase (CTPS), which shows a similar active site architecture.	n-thiosulfoximide	74-91	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	95-101