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 …
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 …
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 …
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 …
Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to …
The polyglutamine (polyQ) diseases consist of nine neurodegenerative diseases in which a polyQ tract expansion leads to protein misfolding and subsequent aggregation. Even when …
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 …
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 …
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) …