PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12429022-4	2003	The anti-PrP monoclonal antibodies were reactive by Western blot and ELISA with recombinant murine PrPc refolded in the presence or absence of either copper or manganese, and with the disease-susceptible allelic form V136R154Q171 ("VRQ"; where single-letter amino-acid notation has been used) and disease-resistant allelic form A136R154R171 ("ARR") of recombinant ovine PrPc.	Manganese	160-169	prion protein	Mus musculus	9-12	
20070537-1	2010	AIMS: Copper and manganese levels are altered in mice both lacking PrPc and prion-infected brains.	Manganese	17-26	prion protein	Mus musculus	67-71	
18332141-2	2008	However, there have also been suggestions that prion protein (PrP) binds manganese.	Manganese	73-82	prion protein	Mus musculus	62-65	
18332141-3	2008	We used isothermal titration calorimetry to identify the manganese binding sites in wild-type mouse PrP.	Manganese	57-66	prion protein	Mus musculus	100-103	
18332141-5	2008	This indicates that PrP binds manganese with affinity similar to other known manganese-binding proteins.	Manganese	30-39	prion protein	Mus musculus	20-23	
18332141-8	2008	Under these conditions, manganese binding resulted in an altered conformation of PrP, displacement of copper, and altered redox chemistry of the metal-protein complex.	Manganese	24-33	prion protein	Mus musculus	81-84	
18332141-9	2008	Cyclic voltammetric measurements suggested a complex redox chemistry involving manganese bound to PrP, whereas copper-bound PrP was able to undergo fully reversible electron cycling.	Manganese	79-88	prion protein	Mus musculus	98-101	
18332141-10	2008	Additionally, manganese binding to PrP converted it to a form able to catalyze aggregation of metal-free PrP.	Manganese	14-23	prion protein	Mus musculus	35-38	
18332141-10	2008	Additionally, manganese binding to PrP converted it to a form able to catalyze aggregation of metal-free PrP.	Manganese	14-23	prion protein	Mus musculus	105-108	
18332141-11	2008	These results further support the notion that manganese binding could cause a conformation change in PrP and trigger changes in the protein similar to those associated with prion disease.	Manganese	46-55	prion protein	Mus musculus	101-104	
35038117-8	2022	PrP refolded with nickle or manganese behave similar to apo-PrP, and PrP refolded with copper is least effective.	Manganese	28-37	prion protein	Mus musculus	0-3