PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25615817-1	2016	X-linked protoporphyria (XLP), a rare erythropoietic porphyria, results from terminal exon gain-of-function mutations in the ALAS2 gene causing increased ALAS2 activity and markedly increased erythrocyte protoporphyrin levels.	protoporphyrin IX	204-218	5'-aminolevulinate synthase 2	Homo sapiens	125-130	
31076252-11	2019	The increase in ALAS2 enzyme contributes to the accumulation in PPIX in the patients.	protoporphyrin IX	64-68	5'-aminolevulinate synthase 2	Homo sapiens	16-21	
31395332-3	2019	Aminolevulinic acid synthase 2 (ALAS2), the rate limiting enzyme of the heme pathway in the erythron, is a therapeutic target in EPP because inhibiting enzyme function would reduce downstream production of protoporphyrin IX (PPIX), preventing accumulation of the toxic molecule and thereby ameliorating symptoms.	protoporphyrin IX	206-223	5'-aminolevulinate synthase 2	Homo sapiens	0-30	
31395332-3	2019	Aminolevulinic acid synthase 2 (ALAS2), the rate limiting enzyme of the heme pathway in the erythron, is a therapeutic target in EPP because inhibiting enzyme function would reduce downstream production of protoporphyrin IX (PPIX), preventing accumulation of the toxic molecule and thereby ameliorating symptoms.	protoporphyrin IX	206-223	5'-aminolevulinate synthase 2	Homo sapiens	32-37	
31395332-3	2019	Aminolevulinic acid synthase 2 (ALAS2), the rate limiting enzyme of the heme pathway in the erythron, is a therapeutic target in EPP because inhibiting enzyme function would reduce downstream production of protoporphyrin IX (PPIX), preventing accumulation of the toxic molecule and thereby ameliorating symptoms.	protoporphyrin IX	225-229	5'-aminolevulinate synthase 2	Homo sapiens	0-30	
31395332-3	2019	Aminolevulinic acid synthase 2 (ALAS2), the rate limiting enzyme of the heme pathway in the erythron, is a therapeutic target in EPP because inhibiting enzyme function would reduce downstream production of protoporphyrin IX (PPIX), preventing accumulation of the toxic molecule and thereby ameliorating symptoms.	protoporphyrin IX	225-229	5'-aminolevulinate synthase 2	Homo sapiens	32-37	
26300302-2	2015	Mutations in the C-terminal region of human erythroid-specific ALAS (hALAS2) are associated with X-linked protoporphyria (XLPP), a disease characterized by extreme photosensitivity, with elevated blood concentrations of free protoporphyrin IX and zinc protoporphyrin.	protoporphyrin IX	225-242	5'-aminolevulinate synthase 2	Homo sapiens	69-75	
25179834-10	2015	Furthermore, we hypothesize that EPP patients may benefit from a mild iron deficiency since it would limit PPIX production by restricting ALAS2 over-expression.	protoporphyrin IX	107-111	5'-aminolevulinate synthase 2	Homo sapiens	138-143	
23263862-1	2013	Frameshift mutations in the last coding exon of the 5-aminolevulinate synthase (ALAS) 2 gene were described to activate the enzyme causing increased levels of zinc- and metal-free protoporphyrin in patients with X-linked dominant protoporphyria (XLDPP).	protoporphyrin IX	180-194	5'-aminolevulinate synthase 2	Homo sapiens	80-87	
21627978-4	2011	MATERIALS AND METHODS: Four patients had a deletion in ALAS2 that causes enzyme gain-of-function, resulting in increased formation of protoporphyrin; one had a heterozygous major deletion in FECH DNA.	protoporphyrin IX	134-148	5'-aminolevulinate synthase 2	Homo sapiens	55-60	
24718052-4	2014	ALAS2 variants that cause high levels of PPIX accumulation provide a new means of targeted, and potentially enhanced, photosensitization.	protoporphyrin IX	41-45	5'-aminolevulinate synthase 2	Homo sapiens	0-5	
24718052-5	2014	In order to assess the prospective utility of ALAS2 variants in PPIX production for PDT, K562 human erythroleukemia cells and HeLa human cervical carcinoma cells were transfected with expression plasmids for ALAS2 variants with greater enzymatic activity than the wild-type enzyme.	protoporphyrin IX	64-68	5'-aminolevulinate synthase 2	Homo sapiens	46-51	
24718052-6	2014	The levels of accumulated PPIX in ALAS2-expressing cells were analyzed using flow cytometry with fluorescence detection.	protoporphyrin IX	26-30	5'-aminolevulinate synthase 2	Homo sapiens	34-39	
24718052-9	2014	Light treatments revealed that ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid (ALA) treatment producing a similar amount of PPIX.	protoporphyrin IX	168-172	5'-aminolevulinate synthase 2	Homo sapiens	31-36	
24509859-6	2014	IRP1 attenuates protoporphyrin biosynthesis by binding to the 5"-iron response element (IRE) of alas2 mRNA, inhibiting its translation.	protoporphyrin IX	16-30	5'-aminolevulinate synthase 2	Homo sapiens	96-101	
24135682-4	2013	Protoporphyrin levels in serum and feces were significantly elevated and a heterozygous frameshift mutation in the exon 11 of the ALAS2 gene: c.1706-1709del (p.Glu569GlyfsX24) was identified.	protoporphyrin IX	0-14	5'-aminolevulinate synthase 2	Homo sapiens	130-135	
20850938-11	2010	Finally, about 4% of unrelated EPP patients have X-linked dominant protoporphyria (XLDPP) (MIM 300752) caused by gain-of-function mutations in the ALAS2 gene leading to an increased erythroid heme biosynthesis and subsequently an accumulation of protoporphyrin without any FECH deficiency.	protoporphyrin IX	246-260	5'-aminolevulinate synthase 2	Homo sapiens	147-152	
10522552-7	1999	Because the 5"-untranslated region of the erythroid-specific ALA-S2 mRNA contains the iron-responsive element, a cis-acting sequence responsible for translational induction of erythroid ALA-S2 by iron, the availability of iron controls protoporphyrin IX levels in hemoglobin-synthesizing cells.	protoporphyrin IX	236-253	5'-aminolevulinate synthase 2	Homo sapiens	61-67