PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24874800-0	2014	Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity.	bis(3',5')-cyclic diguanylic acid	57-65	lon peptidase 1, mitochondrial	Homo sapiens	82-85	
24874800-2	2014	Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity.	bis(3',5')-cyclic diguanylic acid	45-63	lon peptidase 1, mitochondrial	Homo sapiens	20-23	
24874800-2	2014	Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity.	bis(3',5')-cyclic diguanylic acid	65-73	lon peptidase 1, mitochondrial	Homo sapiens	20-23	
24874800-4	2014	Inhibition of in vitro Lon activity occurred for polyP, cAMP, ppGpp, and c-di-GMP.	bis(3',5')-cyclic diguanylic acid	73-81	lon peptidase 1, mitochondrial	Homo sapiens	23-26	
24874800-5	2014	We also demonstrated by HPLC that Lon is able to bind c-di-GMP.	bis(3',5')-cyclic diguanylic acid	54-62	lon peptidase 1, mitochondrial	Homo sapiens	34-37