PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26278353-4	2015	Incubation of EdAG with human Grx-1 or Grx-2 results in facile adduction of cys-23 and cys-77, respectively, as determined by ESI-MS/MS.	Cysteine	76-79	glutaredoxin 2	Homo sapiens	39-44	
26278353-4	2015	Incubation of EdAG with human Grx-1 or Grx-2 results in facile adduction of cys-23 and cys-77, respectively, as determined by ESI-MS/MS.	Cysteine	87-90	glutaredoxin 2	Homo sapiens	39-44	
19292455-1	2009	Mitochondrial Grx2 is a new member of the thioredoxin superfamily that has been found to bind a [2Fe-2S] cluster in a novel coordination motif at the interface of a homodimer, where cluster binding occurs via a catalytic cysteine residue and a molecule of GSH (per monomer).	Cysteine	221-229	glutaredoxin 2	Homo sapiens	14-18	
19290777-3	2009	Grx2 is involved in glutathionylation of protein cysteine sulfhydryl residues in the mitochondria.	Cysteine	49-57	glutaredoxin 2	Homo sapiens	0-4	
17355958-5	2007	Human Grx1 and Grx2 contain Cys-Pro-Tyr-Cys and Cys-Ser-Tyr-Cys active sites and have three and two additional structural Cys residues, respectively.	Cysteine	28-31	glutaredoxin 2	Homo sapiens	15-19	
18816065-7	2008	A key distinction between Grx1- and Grx2-mediated deglutathionylation is decreased catalytic efficiency ( k cat/ K M) of Grx2 for protein deglutathionylation (due primarily to a decreased k cat), reflecting a higher p K a of its catalytic cysteine, as well as a decreased enhancement of nucleophilicity of the second substrate, GSH.	Cysteine	239-247	glutaredoxin 2	Homo sapiens	36-40	
18816065-7	2008	A key distinction between Grx1- and Grx2-mediated deglutathionylation is decreased catalytic efficiency ( k cat/ K M) of Grx2 for protein deglutathionylation (due primarily to a decreased k cat), reflecting a higher p K a of its catalytic cysteine, as well as a decreased enhancement of nucleophilicity of the second substrate, GSH.	Cysteine	239-247	glutaredoxin 2	Homo sapiens	121-125	
15917333-3	2005	Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2.	Cysteine	55-63	glutaredoxin 2	Homo sapiens	126-130	
15917333-3	2005	Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2.	Cysteine	55-63	glutaredoxin 2	Homo sapiens	194-198	
15917333-3	2005	Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2.	Cysteine	160-163	glutaredoxin 2	Homo sapiens	126-130	
17121859-0	2007	Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.	Cysteine	40-49	glutaredoxin 2	Homo sapiens	101-115