PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15214085-4	2004	Whereas the paramagnetic metal cations Cu(II), Fe(II), Ni(II), Co(II), and Mn(II) result in fluorescence quenching, the emission response is not altered by millimolar concentrations of Ca(II) or Mg(II), rendering the sensors selective for Zn(II) among all biologically important metal cations.	mg(ii)	195-201	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	63-68	
12203329-10	2002	The Zn(II) and Mg(II) complexes were all far less stable than the corresponding Ni(II) and Co(II) complexes.	mg(ii)	15-21	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	91-97	
12465804-4	2003	Also, for the first time a plausible correlation between the released Mg(II) ions from sepiolite matrix and those adsorbed Co(II) ions is made.	mg(ii)	70-76	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	123-129	
11106490-9	2000	The only other metal ion to cause slight activation of the enzyme was Co(II), with Ca(II), Cu(II), Mg(II), Ni(II), and Zn(II) all being inhibitory.	mg(ii)	99-105	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	70-76	
9328176-9	1997	Interestingly, in the absence of Mg(II), the activity of the enzymes could be restored by Co(II) to 73% of that with Mg(II) alone for MutT, and 34% for MTH1, the other metals being much less or non-effective.	mg(ii)	117-123	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	90-96	
117692-1	1978	In the present study use was made of the chelating ability of EDTA and the activating property of some metal ions Ca(II), Mg(II) or Mn(II) to counteract the inhibitory effect of Cu(II), Co(II), Pb(II) or Zn(II) ions on the B6-dependent kynurenine hydrolase and on kynurenine aminotransferase.	mg(ii)	122-128	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	186-192	
30667210-9	2019	Density functional theory calculations elucidate the discrepancy in CO affinity: Co(II) and Ni(II) form strong pi-back-donating bonds with CO via electron transfer from the d orbitals of the transition metals to the antibonding molecular orbitals of CO, whereas Mg(II) does not participate in electron transfer or orbital overlap with CO.	mg(ii)	262-268	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	81-87