Andrea Alegre‐Martí

The paper presents a new crystal structure of agonist-bound GR-LBD and proposes a model for GR multimerization, reconciling structural and functional data on glucocorticoid resistance.

This study uses computational modeling to show that polyglutamine expansion in the androgen receptor's N-terminal domain causes dynamic misfolding, altering interdomain interactions and potentially leading to SBMA pathology.

This study shows bile acids bind to an exposed cavity on the glucocorticoid receptor, affecting its self-assembly and transcriptional activity.

The paper identifies LxxLL motifs in NIPBL that regulate its interaction with MAU2 and steroid receptors, forming a ternary complex with GR to facilitate enhancer localization of cohesin.