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...
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Autores principales: | , , , , , |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
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Materias: | |
Acceso en línea: | https://doaj.org/article/5e621729cae84ceba3bb46f9ecec1999 |
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Sumario: | 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-resistant prostate cancer in xenografts, suggesting therapeutic potential. |
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