PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12556469-3	2003	Using electron microscopy and dynamic light scattering, we demonstrate that precipitation inhibition by Ahsg is caused by the transient formation of soluble, colloidal spheres, containing Ahsg, calcium, and phosphate.	Calcium	194-201	alpha-2-HS-glycoprotein	Mus musculus	104-108	
12556469-5	2003	Solubilization in Ahsg-containing calciprotein particles provides a novel conceptual framework to explain how insoluble calcium precipitates may be transported and removed in the bodies of mammals.	Calcium	120-127	alpha-2-HS-glycoprotein	Mus musculus	18-22	
11374033-7	2001	A mineral binding structure is proposed for domain D1 of AHSG suggesting that the proposed EF-hand motif for calcium binding does not exist in AHSG.	Calcium	109-116	alpha-2-HS-glycoprotein	Mus musculus	57-61	
31203904-4	2019	However, recent evidence indicates that fetuin-A can form nucleation seeds or nidi that grow in size through ion sedimentation to become larger amorphous nanoparticles in the presence of excess calcium and apatite ions.	Calcium	194-201	alpha-2-HS-glycoprotein	Mus musculus	40-48	
32001068-4	2020	Calciprotein particles are nanoparticles of calcium-phosphate precipitates bound to serum protein fetuin-A and are generated spontaneously in solution containing calcium, phosphate, and fetuin-A to be dispersed as colloids.	Calcium	44-51	alpha-2-HS-glycoprotein	Mus musculus	98-106