Title : Therapeutic Targeting of the FKBP52 Co-Chaperone in Steroid Hormone Receptor-Regulated Physiology and Disease.

Pub. Date : 2015

PMID : 25986565






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 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 FK506 binding protein 4 Mus musculus
2 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 FK506 binding protein 4 Mus musculus
3 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 FK506 binding protein 4 Mus musculus