Protein aggregation and neurodegenerative disease

CA Ross, MA Poirier - Nature medicine, 2004 - nature.com
Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD),
Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases are …

Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence

R Wetzel - Journal of molecular biology, 2012 - Elsevier
Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …

Pathologic polyglutamine aggregation begins with a self-poisoning polymer crystal

T Kandola, S Venkatesan, J Zhang, BT Lerbakken… - Elife, 2023 - elifesciences.org
A long-standing goal of amyloid research has been to characterize the structural basis of the
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …

The role of interruptions in polyQ in the pathology of SCA1

RP Menon, S Nethisinghe, S Faggiano… - PLoS …, 2013 - journals.plos.org
At least nine dominant neurodegenerative diseases are caused by expansion of CAG
repeats in coding regions of specific genes that result in abnormal elongation of …

From pathways to targets: understanding the mechanisms behind polyglutamine disease

JJ Weber, AS Sowa, T Binder… - BioMed research …, 2014 - Wiley Online Library
The history of polyglutamine diseases dates back approximately 20 years to the discovery of
a polyglutamine repeat in the androgen receptor of SBMA followed by the identification of …

Expansion, mosaicism and interruption: mechanisms of the CAG repeat mutation in spinocerebellar ataxia type 1

C Kraus-Perrotta, S Lagalwar - Cerebellum & Ataxias, 2016 - Springer
Abstract Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative
disorder that primarily affects the cerebellum and brainstem. The genetic mutation is an …

Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues

M Kim - Prion, 2013 - Taylor & Francis
Huntington disease is an autosomal-dominant neurodegenerative disorder caused by a
polyglutamine (polyQ) expansion (> 35Q) in the first exon (EX1) of huntingtin protein (Htt) …

Insights into the aggregation mechanism of PolyQ proteins with different glutamine repeat lengths

T Yushchenko, E Deuerling, K Hauser - Biophysical journal, 2018 - cell.com
Polyglutamine (polyQ) diseases, including Huntington's disease, result from the aggregation
of an abnormally expanded polyQ repeat in the affected protein. The length of the polyQ …

Pathogenic and non-pathogenic polyglutamine tracts have similar structural properties: towards a length-dependent toxicity gradient

FAC Klein, A Pastore, L Masino, G Zeder-Lutz… - Journal of molecular …, 2007 - Elsevier
Abnormally expanded polyglutamine (polyQ) tracts provide a gain of toxic functions to nine
otherwise unrelated human proteins and induce progressive neurodegenerative diseases …

Pathogenic mechanisms underlying spinocerebellar ataxia type 1

L Tejwani, J Lim - Cellular and Molecular Life Sciences, 2020 - Springer
The family of hereditary cerebellar ataxias is a large group of disorders with heterogenous
clinical manifestations and genetic etiologies. Among these, over 30 autosomal dominantly …