PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	35-44	superoxide dismutase 1	Homo sapiens	9-13	
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	35-44	superoxide dismutase 1	Homo sapiens	15-20	
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	111-120	superoxide dismutase 1	Homo sapiens	9-13	
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	111-120	superoxide dismutase 1	Homo sapiens	15-20	
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	154-164	superoxide dismutase 1	Homo sapiens	9-13	
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	154-164	superoxide dismutase 1	Homo sapiens	15-20	
25096579-6	2014	Here, we adapt recently developed single-bond chemistry techniques to study individual disulfide isomerization reactions in hSOD1.	Disulfides	87-96	superoxide dismutase 1	Homo sapiens	124-129	
25096579-7	2014	Mechanical unfolding of hSOD1 leads to the formation of a polypeptide loop held by the disulfide.	Disulfides	87-96	superoxide dismutase 1	Homo sapiens	24-29