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Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of a...

Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of a...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5e621729cae84ceba3bb46f9ecec1999

Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor

About this item

Full title

Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor

Publisher

London: Nature Publishing Group UK

Journal title

Communications biology, 2021-03, Vol.4 (1), p.381-16, Article 381

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Therapies for lethal castration-resistant prostate cancer (CRPC) are an unmet medical need. One mechanism underlying CRPC and resistance to hormonal therapies is the expression of constitutively active splice variant(s) of androgen receptor (AR-Vs) that lack its C-terminus ligand-binding domain. Transcriptional activities of AR-Vs and full-length A...

Alternative Titles

Full title

Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_5e621729cae84ceba3bb46f9ecec1999

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5e621729cae84ceba3bb46f9ecec1999

Other Identifiers

ISSN

2399-3642

E-ISSN

2399-3642

DOI

10.1038/s42003-021-01927-3

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