PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30735496-2	2019	The successive folding, metal ion binding, and disulphide acquisition steps in this pathway can be catalysed through a direct interaction with the copper chaperone for SOD1 (CCS).	disulphide	47-57	superoxide dismutase 1	Homo sapiens	168-172	
30735496-7	2019	Complexation specifically stabilises the SOD1 disulphide sub-loop, priming it and the active site for copper transfer, while delaying disulphide formation and complex dissociation.	disulphide	46-56	superoxide dismutase 1	Homo sapiens	41-45	
30735496-7	2019	Complexation specifically stabilises the SOD1 disulphide sub-loop, priming it and the active site for copper transfer, while delaying disulphide formation and complex dissociation.	disulphide	134-144	superoxide dismutase 1	Homo sapiens	41-45	
17070542-0	2007	The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.	disulphide	21-31	superoxide dismutase 1	Homo sapiens	84-110	
16330499-6	2006	The major proportion of these SOD1s in the CNS were inactive due to insufficient Cu charging and all contained subfractions with a reduced C57-C146 intrasubunit disulphide bond.	disulphide	161-171	superoxide dismutase 1	Homo sapiens	30-34	
16330499-8	2006	These mutants were also enriched in the CNS relative to other organs, suggesting inefficient recognition and degradation of misfolded disulphide-reduced SOD1 in susceptible tissues.	disulphide	134-144	superoxide dismutase 1	Homo sapiens	153-157	
16330499-12	2006	The findings suggest that the motoneuron degeneration could be due to long-term exposure to misfolded aggregation-prone disulphide-reduced SOD1, which constitutes minute subfractions of the stable mutants and larger proportions of the unstable mutants.	disulphide	120-130	superoxide dismutase 1	Homo sapiens	139-143	
29703933-4	2018	Here we report that the cysteine-reactive molecule ebselen efficiently confers the SOD1 intra-subunit disulphide and directs correct SOD1 folding, depopulating the globally unfolded precursor associated with aggregation and toxicity.	disulphide	102-112	superoxide dismutase 1	Homo sapiens	83-87	
29703933-5	2018	Assisted formation of the unusual SOD1 cytosolic disulphide bond could have potential therapeutic applications.	disulphide	49-59	superoxide dismutase 1	Homo sapiens	34-38