Evidence map›Paper›PMID 36674785›Full record

ArticleInternational journal of molecular sciences2023

Mechanistic Investigation of the Androgen Receptor DNA-Binding Domain and Modulation via Direct Interactions with DNA Abasic Sites: Understanding the Mechanisms Involved in Castration-Resistant Prostate Cancer.

Shangze Xu, Matthew D Kondal, Ayaz Ahmad, Ruidi Zhu, Lanyu Fan, Piotr Zaborniak, Katrina S Madden, João V de Souza, Agnieszka K Bronowska

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Shangze XuChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.ORCID 0000-0001-8736-2298
Matthew D KondalChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.
Ayaz AhmadChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.
Ruidi ZhuChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.
Lanyu FanChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.
Piotr ZaborniakChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.
Katrina S MaddenChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.ORCID 0000-0002-3834-148X
João V de SouzaChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.
Agnieszka K BronowskaChemistry-School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK.ORCID 0000-0003-3663-3224
Newcastle University · GB

Funding

Engineering and Physical Sciences Research Council EPR51209X1Engineering and Physical Sciences Research Council EP/S022791/1
6 · The paper itself

Abstract

The androgen receptor (AR) is an important drug target in prostate cancer and a driver of castration-resistant prostate cancer (CRPC). A significant challenge in designing effective drugs lies in targeting constitutively active AR variants and, most importantly, nearly all AR variants lacking the ligand-binding domain (LBD). Recent findings show that an AR's constitutive activity may occur in the presence of somatic DNA mutations within non-coding regions, but the role of these mutations remains elusive. The discovery of new drugs targeting CRPC is hampered by the limited molecular understanding of how AR binds mutated DNA sequences, frequently observed in prostate cancer, and how mutations within the protein and DNA regulate AR-DNA interactions. Using atomistic molecular dynamics (MD) simulations and quantum mechanical calculations, we focused our efforts on (i) rationalising the role of several activating DBD mutations linked to prostate cancer, and (ii) DBD interactions in the presence of abasic DNA lesions, which frequently occur in CRPC. Our results elucidate the role of mutations within DBD through their modulation of the intrinsic dynamics of the DBD-DNA ternary complex. Furthermore, our results indicate that the DNA apurinic lesions occurring in the androgen-responsive element (ARE) enhance direct AR-DNA interactions and stabilise the DBD homodimerisation interface. Moreover, our results strongly suggest that those abasic lesions may form reversible covalent crosslinks between DNA and lysine residues of an AR via a Schiff base. In addition to providing an atomistic model explaining how protein mutations within the AR DNA-binding domain affect AR dimerisation and AR-DNA interactions, our findings provide insight into how somatic mutations occurring in DNA non-coding regions may activate ARs. These mutations are frequently observed in prostate cancer and may contribute to disease progression by enhancing direct AR-DNA interactions.

Indexed as

Prostatic Neoplasms, Castration-ResistantReceptors, AndrogenAndrogensDNAHumansMaleProtein DomainsAndrogensDNAReceptors, Androgenandrogen receptorcastration-resistant prostate cancerdimerisationDNA-protein adductsDNA-protein interactionsmolecular dynamics simulationsprotein-protein interactions

Identifiers

PMID36674785
PMCPMC9864221
OpenAlexW4313891470

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.