PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8940060-2	1996	In Escherichia coli, Lon protease is responsible for the rate-limiting step in degradation of highly unstable proteins such as SulA, RcsA, and lambdaN protein, as well as for about 50% of the rapid degradation of abnormal proteins such as canavanine-containing proteins.	Canavanine	239-249	putative ATP-dependent Lon protease	Escherichia coli	21-24	
8940060-3	1996	We found that Lon-dependent degradation of both SulA and lambdaN protein was unaffected in cells lacking functional DnaJ, whereas Lon-dependent turnover of canavanine-containing proteins was slower in dnaJ mutant cells.	Canavanine	156-166	putative ATP-dependent Lon protease	Escherichia coli	130-133	
2185124-3	1990	Pre-growth of lon+ cells in the presence of canavanine induced proteolytic activity following growth in minimal media as did stress agents such as heat, alcohol and puromycin: the lon mutant did not show the increased activity following canavanine treatment.	Canavanine	44-54	putative ATP-dependent Lon protease	Escherichia coli	14-17