Trinucleotide repeats and protein folding and disease: The perspective from studies with the androgen receptor

Folake A. Orafidiya; Iain J. McEwan

doi:10.4155/fso.15.47

Trinucleotide repeats and protein folding and disease: The perspective from studies with the androgen receptor

Folake A. Orafidiya, Iain J. McEwan^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

The androgen receptor (AR), a ligand activated transcription factor plays a number of roles in reproduction, homeostasis and pathogenesis of disease. It has two major polymorphic sequences; a polyglutamine and a polyglycine repeat that determine the length of the protein and influence receptor folding, structure and function. Here, we review the role the folding of the AR plays in the pathogenesis of spinal-bulbar muscular atrophy (SBMA), a neuromuscular degenerative disease arising from expansion of the polyglutamine repeat. We discuss current management for SBMA patients and how research on AR structure function may lead to future drug treatments.

Original language	English
Article number	FSO47
Pages (from-to)	1-10
Number of pages	10
Journal	Future Science OA
Volume	1
Issue number	2
Early online date	15 Jul 2015
DOIs	https://doi.org/10.4155/fso.15.47
Publication status	Published - 1 Sept 2015

Keywords

androgen receptor
androstanolone
heat shock protein 70
heat shock protein 90
huntingtin
cell nucleus inclusion body
degenerative disease
DNA binding
human
kennedy disease
Multicenter Study
nonhuman
phase 2 clinical trial
priority journal
protein expression
Protein Folding
protein structure
Randomized Controlled Trial
trinucleotide repeat

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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abstract = "The androgen receptor (AR), a ligand activated transcription factor plays a number of roles in reproduction, homeostasis and pathogenesis of disease. It has two major polymorphic sequences; a polyglutamine and a polyglycine repeat that determine the length of the protein and influence receptor folding, structure and function. Here, we review the role the folding of the AR plays in the pathogenesis of spinal-bulbar muscular atrophy (SBMA), a neuromuscular degenerative disease arising from expansion of the polyglutamine repeat. We discuss current management for SBMA patients and how research on AR structure function may lead to future drug treatments.",

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Trinucleotide repeats and protein folding and disease: The perspective from studies with the androgen receptor

Abstract

Keywords

UN SDGs

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