PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17785456-0	2007	Cellular oligomerization of alpha-synuclein is determined by the interaction of oxidized catechols with a C-terminal sequence.	Catechols	89-98	synuclein alpha	Homo sapiens	28-43	
17785456-2	2007	A critically important modulator of alpha-syn aggregation in vitro is dopamine and other catechols, which can prevent the formation of alpha-syn aggregates in cell-free and cellular model systems.	Catechols	89-98	synuclein alpha	Homo sapiens	36-45	
17785456-2	2007	A critically important modulator of alpha-syn aggregation in vitro is dopamine and other catechols, which can prevent the formation of alpha-syn aggregates in cell-free and cellular model systems.	Catechols	89-98	synuclein alpha	Homo sapiens	135-144	
17785456-3	2007	Despite the profound importance of this interaction for the pathogenesis of PD, the processes by which catechols alter alpha-syn aggregation are unclear.	Catechols	103-112	synuclein alpha	Homo sapiens	119-128	
17785456-5	2007	The data show that the intracellular inhibition of alpha-syn aggregation requires the oxidation of catechols and the specific noncovalent interaction of the oxidized catechols with residues (125)YEMPS(129) in the C-terminal region of the protein.	Catechols	99-108	synuclein alpha	Homo sapiens	51-60	
17785456-5	2007	The data show that the intracellular inhibition of alpha-syn aggregation requires the oxidation of catechols and the specific noncovalent interaction of the oxidized catechols with residues (125)YEMPS(129) in the C-terminal region of the protein.	Catechols	166-175	synuclein alpha	Homo sapiens	51-60