PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8126749-0	1994	Antagonism of cyanide intoxication with murine carrier erythrocytes containing bovine rhodanese and sodium thiosulfate.	Cyanides	14-21	thiosulfate sulfurtransferase	Bos taurus	86-95	
7881866-12	1994	It is suggested that addition of purified, exogenous PKC may accept phosphate from phosphorylated rhodanese or HI-6 may dephosphorylate rhodanese, both of which stimulate the conversion of cyanide anion to the less toxic SCN-.	Cyanides	189-202	thiosulfate sulfurtransferase	Bos taurus	98-107	
7881866-12	1994	It is suggested that addition of purified, exogenous PKC may accept phosphate from phosphorylated rhodanese or HI-6 may dephosphorylate rhodanese, both of which stimulate the conversion of cyanide anion to the less toxic SCN-.	Cyanides	189-202	thiosulfate sulfurtransferase	Bos taurus	136-145	
7881866-13	1994	These observations support the possibility that rhodanese may be regulated by protein phosphorylation and treatments that alter the phosphorylation state of rhodanese may affect cyanide detoxification via SCN- formation.	Cyanides	178-185	thiosulfate sulfurtransferase	Bos taurus	48-57	
7881866-13	1994	These observations support the possibility that rhodanese may be regulated by protein phosphorylation and treatments that alter the phosphorylation state of rhodanese may affect cyanide detoxification via SCN- formation.	Cyanides	178-185	thiosulfate sulfurtransferase	Bos taurus	157-166	
11254178-1	2001	Cyanide detoxification is catalysed by two enzymes: rhodanese [thiosulphate: cyanide sulphurtransferase, E.C.	Cyanides	0-7	thiosulfate sulfurtransferase	Bos taurus	52-61	
7881866-0	1994	Protein kinase C modulation of rhodanese-catalyzed conversion of cyanide to thiocyanate.	Cyanides	65-72	thiosulfate sulfurtransferase	Bos taurus	31-40	
7881866-1	1994	Detoxification of cyanide is catalyzed by a sulfurtransferase, rhodanese, a phosphoprotein regulated by unknown protein kinases.	Cyanides	18-25	thiosulfate sulfurtransferase	Bos taurus	63-72	
2317511-8	1990	Sulfane sulfurtransferase, like rhodanese, catalyzes the transfer of sulfur from thiosulfate to cyanide via a persulfide intermediate, and displays remarkably similar kinetics in this process (Aird, B.A., Heinrikson, R.L.	Cyanides	96-103	thiosulfate sulfurtransferase	Bos taurus	32-41	
1667623-1	1991	We have developed a sensitive method for the measurement of rhodanese activity in human serum which is based on the colorimetric method for the determination of thiocyanate produced from methanethiosulfonate and cyanide as substrates.	Cyanides	212-219	thiosulfate sulfurtransferase	Bos taurus	60-69	
1667623-3	1991	The present method is about 70-fold more sensitive than the conventional method using cyanide and thiosulfate as substrates and correlates well (r = 0.997) with the conventional method in bovine liver rhodanese.	Cyanides	86-93	thiosulfate sulfurtransferase	Bos taurus	201-210	
20135153-2	2011	The best characterized Str is bovine rhodanese (EC 2.8.1.1) which catalyses in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate.	Cyanides	143-150	thiosulfate sulfurtransferase	Bos taurus	37-46	
3170581-1	1988	The interaction of bovine liver rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) with the acceptor substrates, dithiothreitol or cyanide, was studied.	Cyanides	55-62	thiosulfate sulfurtransferase	Bos taurus	32-41	
3170581-2	1988	When incubated in the presence of cyanide or dithiothreitol, rhodanese was inactivated in a time-dependent process.	Cyanides	34-41	thiosulfate sulfurtransferase	Bos taurus	61-70	
3170581-6	1988	Substrate-potentiated inactivation of rhodanese (with cyanide) has been reported before, but the cause and nature of this interaction were unexplained.	Cyanides	54-61	thiosulfate sulfurtransferase	Bos taurus	38-47	
2461938-8	1988	All MABs recognized rhodanese that was oxidized with peroxide and allowed to undergo a secondary cyanide-dependent reaction which also resulted in a fluorescence shift and increased proteolytic susceptibility.	Cyanides	97-104	thiosulfate sulfurtransferase	Bos taurus	20-29	
711738-5	1978	Inactivation of free rhodanese by phenylglyoxal in the presence of cyanide was shown to be caused by a novel reaction in which disulfide bonds are formed between Cys-247 and either Cys-254 or Cys-263.	Cyanides	67-74	thiosulfate sulfurtransferase	Bos taurus	21-30