PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18166048-5	2008	It is shown that the borohydride ion, a known reducing agent for GR, is catalytically oxidized by larger GR-nanoparticle (>or=150 gold atoms) complexes generating catalytic currents, whereas NADPH (the natural reducing agent for GR) is not.	Borohydrides	21-32	glutathione-disulfide reductase	Homo sapiens	65-67	
18166048-5	2008	It is shown that the borohydride ion, a known reducing agent for GR, is catalytically oxidized by larger GR-nanoparticle (>or=150 gold atoms) complexes generating catalytic currents, whereas NADPH (the natural reducing agent for GR) is not.	Borohydrides	21-32	glutathione-disulfide reductase	Homo sapiens	105-107	
18166048-5	2008	It is shown that the borohydride ion, a known reducing agent for GR, is catalytically oxidized by larger GR-nanoparticle (>or=150 gold atoms) complexes generating catalytic currents, whereas NADPH (the natural reducing agent for GR) is not.	Borohydrides	21-32	glutathione-disulfide reductase	Homo sapiens	105-107	
18166048-7	2008	The catalytic currents with borohydride begin at the potential of GR-bound FAD, showing that there is essentially zero resistance to electron transfer (i.e., zero overpotential) from GR-bound FAD through the gold nanoparticle to the electrode.	Borohydrides	28-39	glutathione-disulfide reductase	Homo sapiens	66-68	
18166048-7	2008	The catalytic currents with borohydride begin at the potential of GR-bound FAD, showing that there is essentially zero resistance to electron transfer (i.e., zero overpotential) from GR-bound FAD through the gold nanoparticle to the electrode.	Borohydrides	28-39	glutathione-disulfide reductase	Homo sapiens	183-185