PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24944642-7	2014	However, the plasma SOD activity levels in the SOD3 Ala/Ala homozygote carriers (80.51+-27.68 U/ml) were significantly lower compared with the Thr allele carriers (92.18+-16.37 U/ml; P=0.031).	Alanine	52-55	superoxide dismutase 1	Homo sapiens	20-23	
26791423-5	2016	His residues constructing the Cu(2+)-binding site in denatured apo-H43R were experimentally assigned by absorption and fluorescence-based assays of SOD1 mutants, in which each of the seven His residues in H43R SOD1 is replaced with Ala.	Alanine	232-235	superoxide dismutase 1	Homo sapiens	210-214	
2853161-4	1988	The result of isoelectric gel electrophoresis showed that the difference in isoelectric point (pI) was derived from acetylation of the N-terminal amino acid (alanine) in h-SOD.	Alanine	158-165	superoxide dismutase 1	Homo sapiens	172-175	
27072680-3	2016	The most common SOD1 gene mutation in North America is a missense mutation substituting valine for alanine (A4V).	Alanine	99-106	superoxide dismutase 1	Homo sapiens	16-20	
24944642-7	2014	However, the plasma SOD activity levels in the SOD3 Ala/Ala homozygote carriers (80.51+-27.68 U/ml) were significantly lower compared with the Thr allele carriers (92.18+-16.37 U/ml; P=0.031).	Alanine	56-59	superoxide dismutase 1	Homo sapiens	20-23	
24157939-3	2014	Research on ALS relies on transgenic models and particularly on mice carrying a glycine-to-alanine conversion at the 93rd codon (G93A) of the hSOD1 gene.	Alanine	91-98	superoxide dismutase 1	Homo sapiens	142-147	
19765191-7	2009	Within the SMIR, the conserved W184, H190 and positively charged R183, R186, K187, and K189 residues are critical to the p62-mutant SOD1 interaction as substitution of these residues with alanine resulted in significantly abolished binding.	Alanine	188-195	superoxide dismutase 1	Homo sapiens	132-136	
21325350-6	2011	RESULTS: CKD patients with the SOD Ala/Val and Val/Val genotypes had a significantly greater eGFR decline compared to those with the Ala/Ala genotype (Ala/Val compared with Ala/Ala odds ratio (OR) 0.35, 95% CI 0.19 to 0.64, P = 0.001; Val/Val compared with Ala/Ala OR 0.25, 95% CI 0.10 to 0.65, P = 0.005).	Alanine	35-38	superoxide dismutase 1	Homo sapiens	31-34	
21325350-8	2011	CONCLUSION: CKD patients with the SOD Ala/Val and Val/Val genotypes have a greater decline in kidney function than those with the Ala/Ala genotype.	Alanine	38-41	superoxide dismutase 1	Homo sapiens	34-37	
17879532-1	2007	OBJECTIVE: To investigate the relationship between efficacy of Chaihu Taoren Decoction (CTD) and the polymorphism of valine-alanine missense mutation of 9th codan (Val9Ala, T1183C) of superoxide dismutase (SOD) in patients with tardive dyskinesia (TD).	Alanine	124-131	superoxide dismutase 1	Homo sapiens	184-204	
17879532-1	2007	OBJECTIVE: To investigate the relationship between efficacy of Chaihu Taoren Decoction (CTD) and the polymorphism of valine-alanine missense mutation of 9th codan (Val9Ala, T1183C) of superoxide dismutase (SOD) in patients with tardive dyskinesia (TD).	Alanine	124-131	superoxide dismutase 1	Homo sapiens	206-209	
17822322-8	2007	Carriers of the Ala/Ala genotype had higher p-SOD activity (p=0.04).	Alanine	16-19	superoxide dismutase 1	Homo sapiens	46-49	
17822322-8	2007	Carriers of the Ala/Ala genotype had higher p-SOD activity (p=0.04).	Alanine	20-23	superoxide dismutase 1	Homo sapiens	46-49	
9294870-2	1997	Human Cu,Zn SODs with single-site replacements of Lys-136 by Arg,Ala, Gln, or Glu or with a triple-site substitution (Glu-132 and Glu-133 to Gln and Lys-136 to Ala) were made to test hypotheses regarding contributions of these residues to Cu,Zn SOD activity.	Alanine	65-68	superoxide dismutase 1	Homo sapiens	6-15	
16309674-2	2006	There is evidence that mutations in the Cu/Zn superoxide dismutase (SOD1) gene are implicated in about 20% of familiar ALS and transgenic mice overexpressing the human Cu/Zn superoxide dismutase (GLY(93) --> ALA) mutation show an ALS-like phenotype.	Alanine	211-214	superoxide dismutase 1	Homo sapiens	40-66	
13129803-1	2003	We present three members of a pedigree with familial amyotrophic lateral sclerosis (FALS) who have a rare mutation in exon 4 of Cu/Zn superoxide dismutase (SOD1) codon position 89, converting alanine to valine.	Alanine	192-199	superoxide dismutase 1	Homo sapiens	128-154	
13129803-1	2003	We present three members of a pedigree with familial amyotrophic lateral sclerosis (FALS) who have a rare mutation in exon 4 of Cu/Zn superoxide dismutase (SOD1) codon position 89, converting alanine to valine.	Alanine	192-199	superoxide dismutase 1	Homo sapiens	156-160	
12699776-0	2003	Altered long-term corticostriatal synaptic plasticity in transgenic mice overexpressing human CU/ZN superoxide dismutase (GLY(93)-->ALA) mutation.	Alanine	135-138	superoxide dismutase 1	Homo sapiens	94-120	
9633809-1	1998	Transgenic mice that highly over-express a mutated human CuZn superoxide dismutase (SOD1) gene [gly93-->ala; TgN(SOD1-G93A)G1H line] found in some patients with familial ALS (FALS) have been shown to develop motor neuron disease that is characterized by motor neuron loss in the lumbar and cervical spinal regions and a progressive loss of motor activity.	Alanine	104-107	superoxide dismutase 1	Homo sapiens	57-82	
9633809-1	1998	Transgenic mice that highly over-express a mutated human CuZn superoxide dismutase (SOD1) gene [gly93-->ala; TgN(SOD1-G93A)G1H line] found in some patients with familial ALS (FALS) have been shown to develop motor neuron disease that is characterized by motor neuron loss in the lumbar and cervical spinal regions and a progressive loss of motor activity.	Alanine	104-107	superoxide dismutase 1	Homo sapiens	84-88	
15737434-1	2005	Transgenic mice carrying the human mutated SOD1 gene with a glycine/alanine substitution at codon 93 (G93A) are a widely used model for the fatal human disease amyotrophic lateral sclerosis (ALS).	Alanine	68-75	superoxide dismutase 1	Homo sapiens	43-47	
10749988-2	2000	Transgenic mice over- expressing a mutated form of human SOD1 containing a Gly-->Ala substitution at position 93 (SOD1(G93A)) develop a severe, progressive motoneuron disease.	Alanine	84-87	superoxide dismutase 1	Homo sapiens	57-61	
10749988-2	2000	Transgenic mice over- expressing a mutated form of human SOD1 containing a Gly-->Ala substitution at position 93 (SOD1(G93A)) develop a severe, progressive motoneuron disease.	Alanine	84-87	superoxide dismutase 1	Homo sapiens	117-121	
7951249-0	1994	A frequent ala 4 to val superoxide dismutase-1 mutation is associated with a rapidly progressive familial amyotrophic lateral sclerosis.	Alanine	11-14	superoxide dismutase 1	Homo sapiens	24-46	
9006413-4	1997	We recently described a family with amyotrophic lateral sclerosis associated with a mutation in the superoxide dismutase 1 (SOD1) gene substituting an aspartate for an alanine (D9OA).	Alanine	168-175	superoxide dismutase 1	Homo sapiens	100-122	
9006413-4	1997	We recently described a family with amyotrophic lateral sclerosis associated with a mutation in the superoxide dismutase 1 (SOD1) gene substituting an aspartate for an alanine (D9OA).	Alanine	168-175	superoxide dismutase 1	Homo sapiens	124-128