PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26257890-9	2015	Although catechol was a known NGAL-Siderocalin co-factor, our purification directly confirmed its presence in urine as well as its capacity to serve as an iron trap with NGAL-Siderocalin.	catechol	9-17	lipocalin 2	Homo sapiens	30-34	
34939797-4	2022	Catechol siderophore-like compounds are known to bind siderocalin (Scn)/lipocalin-2 to form stable siderophore:Fe:Scn complexes.	catechol	0-8	lipocalin 2	Homo sapiens	72-83	
29355013-5	2018	Thermodynamic analyses suggest that ETC with more catechol moieties has a stronger binding capacity with NGAL especially in the presence of Fe3+.	catechol	50-58	lipocalin 2	Homo sapiens	105-109	
26257890-0	2015	Purification and Structural Characterization of "Simple Catechol", the NGAL-Siderocalin Siderophore in Human Urine.	catechol	56-64	lipocalin 2	Homo sapiens	71-75	
35574260-7	2022	Then, the same NGAL but bound with the iron-catechol complexes through the cation-pi interactions as a holo-form was characterized.	catechol	44-52	lipocalin 2	Homo sapiens	15-19	
26257890-9	2015	Although catechol was a known NGAL-Siderocalin co-factor, our purification directly confirmed its presence in urine as well as its capacity to serve as an iron trap with NGAL-Siderocalin.	catechol	9-17	lipocalin 2	Homo sapiens	170-174	
24018130-3	2013	The selective binding of Fe(III)-catechol ligands to NGAL is here studied by using iron coordination structures with one, two, and three catecholate ligands.	catechol	33-41	lipocalin 2	Homo sapiens	53-57	
24798325-5	2014	We demonstrate that similar to lipocalin 2, Bet v 1 is capable of binding iron via catechol-based siderophores.	catechol	83-91	lipocalin 2	Homo sapiens	31-42	
20581821-7	2010	As catechols derive from bacterial and mammalian metabolism of dietary compounds, the Scn-Ngal-catechol-Fe(III) complex represents an unforeseen microbial-host interaction, which mimics Scn-Ngal-siderophore interactions but instead traffics iron in aseptic tissues.	catechol	3-11	lipocalin 2	Homo sapiens	90-94	
20581821-0	2010	Iron traffics in circulation bound to a siderocalin (Ngal)-catechol complex.	catechol	59-67	lipocalin 2	Homo sapiens	53-57	
20581821-4	2010	Using chemical screens, crystallography and fluorescence methods, we report that Scn-Ngal binds iron together with a small metabolic product called catechol.	catechol	148-156	lipocalin 2	Homo sapiens	85-89	
20581821-7	2010	As catechols derive from bacterial and mammalian metabolism of dietary compounds, the Scn-Ngal-catechol-Fe(III) complex represents an unforeseen microbial-host interaction, which mimics Scn-Ngal-siderophore interactions but instead traffics iron in aseptic tissues.	catechol	3-11	lipocalin 2	Homo sapiens	190-194