PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9745361-3	1998	Specific "redox-sensing" elements, consisting of cysteine residues, have been identified in the structures of at least three transporter subtypes (GLT1, GLAST and EAAC1) and shown to regulate transport rate via thiol-disulphide redox interconversion.	disulphide	217-227	solute carrier family 1 member 1	Homo sapiens	163-168	
9421181-9	1997	The electrogenic currents of EAAC1 were significantly reduced by peroxynitrite, an endogenously occurring oxidant formed in certain pathological brain processes, and the mechanism of inhibition partially depended on the formation of disulphide groups.	disulphide	233-243	solute carrier family 1 member 1	Homo sapiens	29-34