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Reduced mesencephalic astrocyte-derived neurotrophic factor expression by mutant androgen receptor contributes to neurodegeneration in a model of spinal and bulbar muscular atrophy pathology. [PDF]

Neural Regen Res
Qin Y, Zhu W, Guo T, Zhang Y, Xing T, Yin P, Li S, Li XJ, Yang S.   +8 more
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Conformation Polymorphism of Polyglutamine Proteins.

Trends in Biochemical Sciences, 2018
Expanded polyglutamine (polyQ) stretches within endogenous proteins cause at least nine human diseases. The structural basis of polyQ pathogenesis is the key to understanding fundamental mechanisms of these diseases, but it remains unclear and controversial due to a lack of polyQ protein structures at the single-atom level. Various hypotheses have been
Xinran Feng, S. Luo, B. Lu
semanticscholar   +4 more sources

Trehalose Conjugated, Catechin Loaded Polylactide Nanoparticle for Improved Neuroprotection against Intracellular Polyglutamine Aggregate.

Biomacromolecules, 2020
Intracellular/extracellular protein aggregation is linked to variety of neurodegenerative diseases. Current research focusses on identifying anti-amyloidogenic small molecules to inhibit such protein aggregation and associated cytotoxicity.
S. Mandal, Koushik Debnath, N. Jana, N. Jana   +3 more
semanticscholar   +1 more source

An accurate model of polyglutamine

Proteins: Structure, Function, and Bioinformatics, 2011
AbstractPolyglutamine repeats in proteins are highly correlated with amyloid formation and neurological disease. To better understand the molecular basis of glutamine repeat diseases, structural analysis of polyglutamine peptides as soluble monomers, oligomers, and insoluble amyloid fibrils is necessary.
Digambaranath, Jyothi L., Campbell, Tyler V., Chung, Alfred, McPhail, Michael J., Stevenson, Karis E., Zhody, Mohamed A., Finke, John M.   +6 more
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Autophagy and Polyglutamine Disease

2020
Polyglutamine (polyQ) disease is a type of fatal neurodegenerative disease caused by an expansion of CAG repeats in a specific gene, resulting in a protein with an abnormal polyQ fragment. The age of onset and the degree of pathological deterioration are related to the length of the polyQ fragment.
Zongbing Hao, Guanghui Wang, Haigang Ren
openaire   +2 more sources

Folding of polyglutamine chains

The Journal of Chemical Physics, 2008
Long polyglutamine chains have been associated with a number of neurodegenerative diseases. These include Huntington’s disease, where expanded polyglutamine (PolyQ) sequences longer than 36 residues are correlated with the onset of symptoms. In this paper we study the folding pathway of a 54-residue PolyQ chain into a β-helical structure.
Allam S. Reddy, Nicholas L. Abbott, Manan Chopra, J. J. de Pablo   +3 more
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Purification of Polyglutamine Proteins1

2006
The misfolding and formation of fibrillar-like aggregates by polyglutamine proteins is believed to be a key factor in the development of the neurodegenerative polyglutamine diseases; however, relatively little is known about structural and conformational aspects of polyglutamine-induced misfolding and aggregation.
Stephen P. Bottomley, Lisa D. Cabrita, Michelle K M Chow, Andrew M. Ellisdon   +3 more
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Proteomics of Polyglutamine Aggregates

2006
In nine members of polyglutamine (polyQ) diseases, CAG repeat expansions of their responsible genes are observed. The disease is considered to be caused by the formation of polyQ aggregates that sequester proteins essential for cell viability. To understand the pathological process of polyQ diseases, a proteomic approach was used to identify aggregate ...
Nobuyuki Nukina, Kenichi Mitsui, Hiroshi Doi   +2 more
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Biodegradable Nanoparticles Containing Mechanism Based Peptide Inhibitors Reduce Polyglutamine Aggregation in Cell Models and Alleviate Motor Symptoms in a Drosophila Model of Huntington's Disease.

ACS Chemical Neuroscience, 2018
Detailed study of the molecular mechanism behind the pathogenesis of Huntington's disease (HD) suggests that polyglutamine aggregation is one of the fundamental reasons for HD.
Abhayraj S. Joshi, Virender Singh, A. Gahane, A. Thakur   +3 more
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