PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26698166-6	2016	Bypassing ALAS-2 function in Alas2 cis element-mutant cells by providing its catalytic product 5-aminolevulinic acid rescues heme biosynthesis and the GATA-1-dependent genetic network.	5-amino levulinic acid	95-116	5'-aminolevulinate synthase 2	Homo sapiens	10-16	
26698166-6	2016	Bypassing ALAS-2 function in Alas2 cis element-mutant cells by providing its catalytic product 5-aminolevulinic acid rescues heme biosynthesis and the GATA-1-dependent genetic network.	5-amino levulinic acid	95-116	5'-aminolevulinate synthase 2	Homo sapiens	29-34	
25450364-3	2014	ALAS2 is a mitochondrial enzyme, which utilizes glycine and succinyl-CoA to form 5-aminolevulinic acid (ALA), a crucial precursor in heme synthesis.	5-amino levulinic acid	81-102	5'-aminolevulinate synthase 2	Homo sapiens	0-5	
25450364-15	2014	ALA may represent a novel therapeutic option for CSA treatment, particularly for cases harboring ALAS2 mutations.	5-amino levulinic acid	0-3	5'-aminolevulinate synthase 2	Homo sapiens	97-102	
25450364-4	2014	Therefore, ALA supplementation could be an effective therapeutic strategy to restore heme synthesis in CSA caused by ALAS2 defects.	5-amino levulinic acid	11-14	5'-aminolevulinate synthase 2	Homo sapiens	117-122	
12393718-1	2002	X-linked sideroblastic anemia (XLSA) is caused by mutations in the erythroid-specific 5-aminolevulinic acid synthase (ALAS2) gene.	5-amino levulinic acid	86-107	5'-aminolevulinate synthase 2	Homo sapiens	118-123	
11110715-1	2000	X-linked sideroblastic anemia (XLSA) is caused by mutations in the erythroid-specific 5-aminolevulinic acid synthase (ALAS2) gene.	5-amino levulinic acid	86-107	5'-aminolevulinate synthase 2	Homo sapiens	118-123