PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25986565-11	2015	Thus, the targeting of FKBP52 proline-rich loop interactions is the most attractive therapeutic approach to disrupt FKBP52 regulation of receptor activity in steroid hormone receptor-dependent physiology and disease.	Proline	30-37	FK506 binding protein 4	Mus musculus	23-29	
25986565-11	2015	Thus, the targeting of FKBP52 proline-rich loop interactions is the most attractive therapeutic approach to disrupt FKBP52 regulation of receptor activity in steroid hormone receptor-dependent physiology and disease.	Proline	30-37	FK506 binding protein 4	Mus musculus	116-122	
21511531-5	2011	Recent studies demonstrated that the FKBP52 FK1 domain and the proline-rich loop within this domain are functionally important for FKBP52 regulation of receptor function.	Proline	63-70	FK506 binding protein 4	Mus musculus	131-137	
25986565-10	2015	The proline-rich loop overhanging the FKBP52 FK1 catalytic domain is functionally important and likely represents an interaction surface within the receptor-chaperone complex.	Proline	4-11	FK506 binding protein 4	Mus musculus	38-44