PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9060994-2	1997	We previously reported that nickel (Ni2+) specifically inhibits the binding of activated alpha 2-macroglobulin (alpha 2 M*) at 4 degrees C to LRP and had no effect on the binding of other ligands to the receptor (Hussain et al.	Nickel(2+)	36-40	alpha-2-macroglobulin	Homo sapiens	89-110	
11811950-5	2002	In addition, although it is known that the binding of alpha2-M-proteinase complexes to LRP can be blocked by Ni2+, the effect on PZP-proteinase has never been examined.	Nickel(2+)	109-113	alpha-2-macroglobulin	Homo sapiens	54-62	
11811950-8	2002	We also demonstrated that Ni2+ blocks the binding of alpha2-M-chymotrypsin complexes, but not PZP-chymotrypsin complexes, to LRP.	Nickel(2+)	26-30	alpha-2-macroglobulin	Homo sapiens	53-61	
9376342-1	1997	A previous study demonstrated that activated alpha2-macroglobulin (alpha2M*) binding to the low-density receptor-related protein/alpha2-macroglobulin receptor (LRP/alpha2MR) is blocked by Ni2+ [Hussain, M. M., et al.	Nickel(2+)	188-192	alpha-2-macroglobulin	Homo sapiens	45-65	
9376342-1	1997	A previous study demonstrated that activated alpha2-macroglobulin (alpha2M*) binding to the low-density receptor-related protein/alpha2-macroglobulin receptor (LRP/alpha2MR) is blocked by Ni2+ [Hussain, M. M., et al.	Nickel(2+)	188-192	alpha-2-macroglobulin	Homo sapiens	67-75	
9376342-1	1997	A previous study demonstrated that activated alpha2-macroglobulin (alpha2M*) binding to the low-density receptor-related protein/alpha2-macroglobulin receptor (LRP/alpha2MR) is blocked by Ni2+ [Hussain, M. M., et al.	Nickel(2+)	188-192	alpha-2-macroglobulin	Homo sapiens	129-149	
9376342-3	1997	We now report that the effect of Ni2+ is on a region of the alpha2M molecule upstream of the carboxyl terminal receptor recognition domain.	Nickel(2+)	33-37	alpha-2-macroglobulin	Homo sapiens	60-67	
9060994-2	1997	We previously reported that nickel (Ni2+) specifically inhibits the binding of activated alpha 2-macroglobulin (alpha 2 M*) at 4 degrees C to LRP and had no effect on the binding of other ligands to the receptor (Hussain et al.	Nickel(2+)	36-40	alpha-2-macroglobulin	Homo sapiens	112-121	
9060994-5	1997	In the current investigation, we have examined the effect of Ni2+ on the catabolism of 125 I-labeled alpha 2M*, receptor-associated protein (RAP) and lactoferrin at physiologic temperatures by fibroblasts.	Nickel(2+)	61-65	alpha-2-macroglobulin	Homo sapiens	101-109	
9060994-6	1997	Nickel completely inhibited the degradation of alpha 2M* over a wide range of concentrations (0.3-2.4 nM); 50% inhibition for the degradation of 1.2 nM alpha 2M* was observed at 0.5 mM Ni2+.	Nickel(2+)	185-189	alpha-2-macroglobulin	Homo sapiens	47-55	
9060994-6	1997	Nickel completely inhibited the degradation of alpha 2M* over a wide range of concentrations (0.3-2.4 nM); 50% inhibition for the degradation of 1.2 nM alpha 2M* was observed at 0.5 mM Ni2+.	Nickel(2+)	185-189	alpha-2-macroglobulin	Homo sapiens	152-160	
9060994-11	1997	These data suggest that Ni2+ is a specific inhibitor for the degradation of alpha 2M*.	Nickel(2+)	24-28	alpha-2-macroglobulin	Homo sapiens	76-84	
2420357-1	1986	An alpha-macroglobulin (alpha 2M), which is a dimer consisting of two non-disulfide-bonded subunits, was identified and purified from frog plasma by Ni2+ chelate affinity chromatography.	Nickel(2+)	149-153	alpha-2-macroglobulin	Homo sapiens	24-32	
1700994-3	1990	Characterization of optimal conditions for binding 125I IL-1 beta to H alpha 2M showed that H alpha 2M-IL-1 beta complex formation could be obtained over a pH range of 6.3 to 9 in the presence of some metal cations (i.e., Zn2+, Cd2+, Cu2+, Ni2+).	Nickel(2+)	240-244	alpha-2-macroglobulin	Homo sapiens	94-102