Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
Leung et al. find that the peptidyl-prolyl isomerase Pin1 targets the intrinsically disordered N-terminal domain of the androgen receptor (AR). They show that combining Pin1 inhibition with ralaniten compounds that bind to the AR N-terminal domain has enhanced antitumor activity on castration-resist...
Guardado en:
Autores principales: | Jacky K. Leung, Yusuke Imamura, Minoru Kato, Jun Wang, Nasrin R. Mawji, Marianne D. Sadar |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/5e621729cae84ceba3bb46f9ecec1999 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structure of the homodimeric androgen receptor ligand-binding domain
por: Marta Nadal, et al.
Publicado: (2017) -
Superior polarization retention through engineered domain wall pinning
por: Dawei Zhang, et al.
Publicado: (2020) -
Racetrack memory based on in-plane-field controlled domain-wall pinning
por: Fanny Ummelen, et al.
Publicado: (2017) -
N-terminal domain of nuclear IL-1α shows structural similarity to the C-terminal domain of Snf1 and binds to the HAT/core module of the SAGA complex.
por: Blanka Zamostna, et al.
Publicado: (2012) -
Magnetic domains and domain wall pinning in atomically thin CrBr3 revealed by nanoscale imaging
por: Qi-Chao Sun, et al.
Publicado: (2021)