PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18615209-0	2008	Assembly of a two-dimensional oxalate-bridged heterometallic Co(II)(3)Cr(III)(2) coordination polymer.	Oxalates	30-37	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	61-67	
22807751-4	2012	The title structure gives the first example of the [Co(C2O4)3]4- anion, with the distorted octa-hedral environment of Co(II) center formed by six O atoms from three oxalate residues.	Oxalates	165-172	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	118-124	
22885878-0	2012	The role of the bridging group in exchange coupling in dinuclear homo- and heterometallic Ni(II) and Co(II) complexes with oxalate, oxamidate and dithiooxamidate bridges.	Oxalates	123-130	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	101-107	
19715318-0	2009	Oxalate-bridged bimetallic complexes {NH(prol)3}[MCr(ox)3] (M = Mn(II), Fe(II), Co(II); NH(prol)3(+) = tri(3-hydroxypropyl)ammonium) exhibiting coexistent ferromagnetism and proton conduction.	Oxalates	0-7	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	80-86	
18968050-6	2000	The interfering effects among analytes ions, Fe(III), Co(II), Ni(II) and Cu(II) were more serious than by other ions, but the interfering effects could be removed by adjusting pH or adding the masking agents such as NH(3) or oxalate.	Oxalates	225-232	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	54-60	
18968358-6	2001	As for Cu(II), the interference by Co(II) was very serious, which was eliminated by oxalate ion.	Oxalates	84-91	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	35-41	
2158815-4	1990	When Mn(II) is present in combination with Zn(II), Ni(II), or Co(II), Mn(II) binds predominantly at the site defined by ligands from the protein, oxalate, and the gamma-phosphate of ATP.	Oxalates	146-153	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	62-68	
27014926-8	2016	A 2.6 A resolution X-ray crystal structure of a complex between oxalate and the Co(II)-substituted DeltaE162 OxDC variant, in which Glu(162) has been deleted from the active site loop, reveals the likely mode by which the substrate coordinates the catalytically active Mn ion prior to C-C bond cleavage.	Oxalates	64-71	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	80-85