PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30277764-2	2018	By exploiting X-ray and ultraviolet photoelectron spectroscopy combined with an electrochemical cell (EC-XPS/UPS), we can electrochemically control the Fc SAMs and spectroscopically probe the induced changes with the ferrocene/ferrocenium (Fc/Fc+) redox center (Fe oxidation state), formation of 1:1 Fc+-ClO4- ion pairs, molecular orientation, and monolayer thickness.	perchlorate	304-308	methionine adenosyltransferase 1A	Homo sapiens	155-159	
30277764-6	2018	The oxidation to Fc+ is also met with an increase in work function ascribed to the induced negative interfacial dipole caused by the presence of Fc+-ClO4- ion pairs along with a contribution from the reorientation of the Fc+ SAMs.	perchlorate	149-153	methionine adenosyltransferase 1A	Homo sapiens	225-229	
18163611-1	2008	1-methyl-5-aminotetrazole (4, MAT) can easily be protonated by strong acids, yielding known but largely uninvestigated 1-methyl-5-aminotetrazolium nitrate (4a) and perchlorate (4b).	perchlorate	164-175	methionine adenosyltransferase 1A	Homo sapiens	30-33