PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15930519-7	2005	Site-directed mutagenesis was used to support proposals for the identity of the iron binding ligands (His-175, Asp-177, His-264) of the 2-His-1-carboxylate motif of PAHX.	Iron	80-84	phytanoyl-CoA 2-hydroxylase	Homo sapiens	165-169	
16822677-3	2006	The recombinant Ln1 assembled into 24-mer ferritin shells with low efficiency, however, it was able to form heteropolymers that showed a reduced capacity to incorporate iron in vitro.	Iron	169-173	phytanoyl-CoA 2-hydroxylase	Homo sapiens	16-19	
16822677-4	2006	The Ln1 expressed in HeLa cells formed hybrid ferritins, with the endogenous H and L chains, and caused an iron excess phenotype.	Iron	107-111	phytanoyl-CoA 2-hydroxylase	Homo sapiens	4-7	
16822677-5	2006	Ferritin inactivation and faster degradation in Ln1 transfectants concurred in increasing iron availability, which was probably responsible for the higher sensitivity to H(2)O(2) toxicity and higher level of oxidized proteins.	Iron	90-94	phytanoyl-CoA 2-hydroxylase	Homo sapiens	48-51	
16822677-6	2006	The findings suggest that the pathogenic effects of Ln1 expression are more likely due to deregulation of cellular iron homeostasis rather than to protein conformational problems.	Iron	115-119	phytanoyl-CoA 2-hydroxylase	Homo sapiens	52-55	
16186124-4	2005	Like other 2OG oxygenases, PAHX possesses a double-stranded beta-helix core, which supports three iron binding ligands (His(175), Asp(177), and His(264)); the 2-oxoacid group of 2OG binds to the Fe(II) in a bidentate manner.	Iron	98-102	phytanoyl-CoA 2-hydroxylase	Homo sapiens	27-31	
11549466-1	2001	Phytanoyl-CoA 2-hydroxylase (PAHX), an iron(II) and 2-oxoglutarate-dependent oxygenase, catalyses an essential step in the mammalian metabolism of beta-methylated fatty acids.	Iron	39-43	phytanoyl-CoA 2-hydroxylase	Homo sapiens	0-27	
11549466-1	2001	Phytanoyl-CoA 2-hydroxylase (PAHX), an iron(II) and 2-oxoglutarate-dependent oxygenase, catalyses an essential step in the mammalian metabolism of beta-methylated fatty acids.	Iron	39-43	phytanoyl-CoA 2-hydroxylase	Homo sapiens	29-33	
9326939-5	1997	Human PAHX is targetted to peroxisomes, requires the PTS2 receptor for peroxisomal localization, interacts with the PTS2 receptor in the yeast two-hybrid assay and has intrinsic phytanoyl-CoA alpha-hydroxylase activity that requires the dioxygenase cofactor iron and cosubstrate 2-oxoglutarate.	Iron	258-262	phytanoyl-CoA 2-hydroxylase	Homo sapiens	6-10