PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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.	Disulfides	127-136	thiosulfate sulfurtransferase	Bos taurus	21-30	
3466649-12	1987	Tetrathionate modification of rhodanese may proceed through the formation of sulfenylthiosulfate intermediates at sulfhydryl groups, close to but not identical with the active-site sulfhydryl group, which then can react further with the active-site sulfhydryl group to form disulfide bridges.	Disulfides	274-283	thiosulfate sulfurtransferase	Bos taurus	30-39	
11131146-1	2000	Unfolded bovine rhodanese, a sulfurtransferase, does not regain full activity upon refolding due to the formation of aggregates and disulfide-linked misfolded states unless a large excess of reductant such as 200 mM beta-ME and 5 mg/ml detergent are present [Tandon and Horowitz (1990), J. Biol.	Disulfides	132-141	thiosulfate sulfurtransferase	Bos taurus	16-25