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:	Jacky K. Leung, Yusuke Imamura, Minoru Kato, Jun Wang, Nasrin R. Mawji, Marianne D. Sadar
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/5e621729cae84ceba3bb46f9ecec1999
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spelling	oai:doaj.org-article:5e621729cae84ceba3bb46f9ecec19992021-12-02T13:24:25ZPin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor10.1038/s42003-021-01927-32399-3642https://doaj.org/article/5e621729cae84ceba3bb46f9ecec19992021-03-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01927-3https://doaj.org/toc/2399-3642Leung 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.Jacky K. LeungYusuke ImamuraMinoru KatoJun WangNasrin R. MawjiMarianne D. SadarNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Jacky K. Leung Yusuke Imamura Minoru Kato Jun Wang Nasrin R. Mawji Marianne D. Sadar Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
description	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.
format	article
author	Jacky K. Leung Yusuke Imamura Minoru Kato Jun Wang Nasrin R. Mawji Marianne D. Sadar
author_facet	Jacky K. Leung Yusuke Imamura Minoru Kato Jun Wang Nasrin R. Mawji Marianne D. Sadar
author_sort	Jacky K. Leung
title	Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
title_short	Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
title_full	Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
title_fullStr	Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
title_full_unstemmed	Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor
title_sort	pin1 inhibition improves the efficacy of ralaniten compounds that bind to the n-terminal domain of androgen receptor
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5e621729cae84ceba3bb46f9ecec1999
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Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor

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