PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19914207-3	2010	We recently characterized iron-dependent toxic alpha-syn oligomer species by confocal single molecule fluorescence techniques and used this aggregation model to identify several N"-benzylidene-benzohydrazide (NBB) derivatives inhibiting oligomer formation in vitro.	N-butylbenzenesulfonamide	209-212	synuclein alpha	Homo sapiens	47-56	
19914207-5	2010	Similar to our previous findings in vitro, we found a converse modulation of toxic alpha-syn oligomers by NBB derivates and ferric iron, which was characterized by an increase in aggregate formation by iron and an inhibitory effect of certain NBB compounds.	N-butylbenzenesulfonamide	106-109	synuclein alpha	Homo sapiens	83-92	
19914207-5	2010	Similar to our previous findings in vitro, we found a converse modulation of toxic alpha-syn oligomers by NBB derivates and ferric iron, which was characterized by an increase in aggregate formation by iron and an inhibitory effect of certain NBB compounds.	N-butylbenzenesulfonamide	243-246	synuclein alpha	Homo sapiens	83-92