PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1445844-0	1992	Interaction of CPa-1 with the manganese-stabilizing protein of photosystem II: identification of domains on CPa-1 which are shielded from N-hydroxysuccinimide biotinylation by the manganese-stabilizing protein.	Manganese	30-39	carboxypeptidase A1	Homo sapiens	15-20	
1445844-0	1992	Interaction of CPa-1 with the manganese-stabilizing protein of photosystem II: identification of domains on CPa-1 which are shielded from N-hydroxysuccinimide biotinylation by the manganese-stabilizing protein.	Manganese	30-39	carboxypeptidase A1	Homo sapiens	108-113	
1445844-0	1992	Interaction of CPa-1 with the manganese-stabilizing protein of photosystem II: identification of domains on CPa-1 which are shielded from N-hydroxysuccinimide biotinylation by the manganese-stabilizing protein.	Manganese	180-189	carboxypeptidase A1	Homo sapiens	15-20	
1445844-0	1992	Interaction of CPa-1 with the manganese-stabilizing protein of photosystem II: identification of domains on CPa-1 which are shielded from N-hydroxysuccinimide biotinylation by the manganese-stabilizing protein.	Manganese	180-189	carboxypeptidase A1	Homo sapiens	108-113	
1445844-2	1992	We have previously shown that the presence of the extrinsic, manganese-stabilizing protein on photosystem II membranes prevents the modification of lysyl residues located on the chlorophyll protein CPa-1 (CP-47) by NHS-biotin [Bricker, T. M., Odom, W. R., & Queirolo, C. B.	Manganese	61-70	carboxypeptidase A1	Homo sapiens	198-203	
1445844-5	1992	Upon removal of the manganese-stabilizing protein by calcium chloride-washing, CPa-1 can be specifically modified by treatment with NHS-biotin.	Manganese	20-29	carboxypeptidase A1	Homo sapiens	79-84	
1445844-12	1992	These results strongly suggest that two NHS-biotinylated domains, 304K-321K and 389K-419K, become exposed on CPa-1 when the manganese-stabilizing protein is removed by CaCl2 treatment.	Manganese	124-133	carboxypeptidase A1	Homo sapiens	109-114	
1610808-0	1992	Interaction of CPa-1 with the manganese-stabilizing protein of photosystem II: identification of domains cross-linked by 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide.	Manganese	30-39	carboxypeptidase A1	Homo sapiens	15-20	
1610808-5	1992	Cleavage of the 110-kDa cross-linked species with cyanogen bromide followed by N-terminal sequence analysis was used to identify the peptide fragments of CPa-1 and the manganese-stabilizing protein which were cross-linked.	Manganese	168-177	carboxypeptidase A1	Homo sapiens	154-159	
1610808-7	1992	N-Terminal sequence analysis of the 50-kDa cyanogen bromide fragment indicates that this consists of the C-terminal 16.7-kDa fragment of CPa-1 and the intact manganese-stabilizing protein.	Manganese	158-167	carboxypeptidase A1	Homo sapiens	137-142	
1610808-8	1992	This strongly suggests that the manganese-stabilizing protein is cross-linked to the large extrinsic loop domain of CPa-1.	Manganese	32-41	carboxypeptidase A1	Homo sapiens	116-121	
2479576-5	1989	These results suggest that, upon release of the chloride-insensitive manganese from photosystem II membranes, a conformational change occurs which leads to the exposure of 360Pro(-391)Ser on CPa-1 to the monoclonal antibody FAC2.	Manganese	69-78	carboxypeptidase A1	Homo sapiens	191-196