Spinocerebellar ataxia

T Klockgether, C Mariotti, HL Paulson - Nature reviews Disease primers, 2019 - nature.com
The spinocerebellar ataxias (SCAs) are a genetically heterogeneous group of autosomal
dominantly inherited progressive disorders, the clinical hallmark of which is loss of balance …

Proteins containing expanded polyglutamine tracts and neurodegenerative disease

A Adegbuyiro, F Sedighi, AW Pilkington IV… - Biochemistry, 2017 - ACS Publications
Several hereditary neurological and neuromuscular diseases are caused by an abnormal
expansion of trinucleotide repeats. To date, there have been 10 of these trinucleotide repeat …

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 …

Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation

E Monsellier, V Redeker, G Ruiz-Arlandis… - Journal of Biological …, 2015 - ASBMB
The aggregation of polyglutamine (polyQ)-containing proteins is at the origin of nine
neurodegenerative diseases. Molecular chaperones prevent the aggregation of polyQ …

Mechanism of antibodies purification by protein A

M Zarrineh, IS Mashhadi, M Farhadpour… - Analytical …, 2020 - Elsevier
Protein A, a major cell wall component of Staphylococcus aureus, is one of the first
immunoglobulin-binding proteins that is discovered about 80 years ago. However, a great …

The protein structure context of polyQ regions

F Totzeck, MA Andrade-Navarro, P Mier - PloS one, 2017 - journals.plos.org
Proteins containing glutamine repeats (polyQ) are known to be structurally unstable.
Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to …

Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins

HM Saunders, SP Bottomley - Protein engineering, design & …, 2009 - academic.oup.com
The polyglutamine (polyQ) diseases consist of nine neurodegenerative diseases in which a
polyQ tract expansion leads to protein misfolding and subsequent aggregation. Even when …

Trinucleotide repeats: a structural perspective

B Almeida, S Fernandes, IA Abreu… - Frontiers in …, 2013 - frontiersin.org
Trinucleotide repeat (TNR) expansions are present in a wide range of genes involved in
several neurological disorders, being directly involved in the molecular mechanisms …

Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation

AL Robertson, SJ Headey… - Proceedings of the …, 2010 - National Acad Sciences
Small heat-shock proteins (sHsps) are molecular chaperones that play an important
protective role against cellular protein misfolding by interacting with partially unfolded …

Polyglutamine disease proteins: Commonalities and differences in interaction profiles and pathological effects

M Bonsor, O Ammar, S Schnoegl, EE Wanker… - …, 2024 - Wiley Online Library
Currently, nine polyglutamine (polyQ) expansion diseases are known. They include
spinocerebellar ataxias (SCA1, 2, 3, 6, 7, 17), spinal and bulbar muscular atrophy (SBMA) …