PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16963403-7	2006	We identified a heterozygous mutation of ATT to ACT of SOD1 gene at codon 149 in exon 5 resulting in substitution of isoleucine to threonine.	Isoleucine	117-127	superoxide dismutase 1	Homo sapiens	55-59	
2492791-1	1989	Site-specific mutants of human Cu,Zn superoxide dismutase (Cu,ZnSOD) have been prepared in which the active-site arginine at position 143 (i.e., SODR143) has been replaced by either lysine (SODK143) or isoleucine (SODI143).	Isoleucine	202-212	superoxide dismutase 1	Homo sapiens	31-57	
8202463-4	1994	The water molecule present in the active site close to the copper ion in wild type (WT) SOD is missing in the MD average structure of the Thr-137-->Ile mutant, while this molecule is present in the MD average structures of all the other mutants and of WT SOD.	Isoleucine	151-154	superoxide dismutase 1	Homo sapiens	88-91	
8202463-4	1994	The water molecule present in the active site close to the copper ion in wild type (WT) SOD is missing in the MD average structure of the Thr-137-->Ile mutant, while this molecule is present in the MD average structures of all the other mutants and of WT SOD.	Isoleucine	151-154	superoxide dismutase 1	Homo sapiens	258-261	
2492791-1	1989	Site-specific mutants of human Cu,Zn superoxide dismutase (Cu,ZnSOD) have been prepared in which the active-site arginine at position 143 (i.e., SODR143) has been replaced by either lysine (SODK143) or isoleucine (SODI143).	Isoleucine	202-212	superoxide dismutase 1	Homo sapiens	59-67	
29339254-9	2018	For the future optimization of the generated inhibitors, (i) antioxidant activity against SOD, (ii) the inhibitor stabilization by pi-cation interaction with the catalytic Fe+3 and (iii) formation of hydrogen bond with Ile 676 should be regarded.	Isoleucine	219-222	superoxide dismutase 1	Homo sapiens	90-93	
3112154-1	1987	The active site arginine-143 of human Cu,Zn superoxide dismutase has been replaced by lysine or by isoleucine.	Isoleucine	99-109	superoxide dismutase 1	Homo sapiens	38-64	
26815332-2	2016	A recent experimental study has shown that the (147)GVIGIAQ(153) SOD1 C-terminal segment not only forms amyloid fibrils in isolation but also accelerates the aggregation of full-length SOD1, while substitution of isoleucine at site 149 by proline blocks its fibril formation.	Isoleucine	213-223	superoxide dismutase 1	Homo sapiens	65-69