Results 191 to 200 of about 16,136 (210)
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An accurate model of polyglutamine
Proteins: Structure, Function, and Bioinformatics, 2011AbstractPolyglutamine 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. +6 more
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Polyglutamine expansion neurodegenerative disease
Brain Research Bulletin, 2001Kennedy's disease was the first of eight neurodegenerative disorders found to be caused by expanded polyglutamine repeats. Each of these disorders is likely caused by a toxic gain of function in the disease gene product, often associated with inclusions of mutant protein in susceptible neurons.
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Polyglutamine makes the switch
Science Signaling, 2017In worms, a regulator of noncoding RNA directly catalyzes formation of toxic protein aggregates in the presence of polyglutamine.
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Molecular Pathways to Polyglutamine Aggregation
2012Over 100 human cellular proteins contain a repetitive polyglutamine tract, however, only nine ofthese proteins are associated with disease. In these proteins, the expanded polyQ tract perturbs the native conformation, resulting in an ordered aggregation process that leads to the formation of amyloid-like fibrils.
Amy L, Robertson, Stephen P, Bottomley
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Monitoring polyglutamine toxicity in yeast
Methods, 2011Experiments in yeast have significantly contributed to our understanding of general aspects of biochemistry, genetics, and cell biology. Yeast models have also delivered deep insights in to the molecular mechanism underpinning human diseases, including neurodegenerative diseases.
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Polyglutamine protein aggregates are dynamic
Nature Cell Biology, 2002Protein aggregation and the formation of inclusion bodies are hallmarks of the cytopathology of neurodegenerative diseases, including Huntington's disease, Amyotropic lateral sclerosis, Parkinson's disease and Alzheimer's disease. The cellular toxicity associated with protein aggregates has been suggested to result from the sequestration of essential ...
Soojin, Kim +4 more
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Conformation Polymorphism of Polyglutamine Proteins
Trends in Biochemical Sciences, 2018Expanded 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, Shouqing Luo, Boxun Lu
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Polyglutamine conformation in GST-polyglutamine fusion proteins
Biochemical Society Transactions, 2002L. Masino, A. Pastore
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Therapeutic opportunities in polyglutamine disease
Nature Medicine, 2001Polyglutamine diseases comprise a class of familial neurodegenerative disorders caused by expression of proteins containing expanded polyglutamine tracts. Great progress has been made in elucidating the molecular mechanisms contributing to polyglutamine pathology, and in identifying potential drug targets.
R E, Hughes, J M, Olson
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Polyglutamine and Neurodegeneration: Structural Aspects
Protein & Peptide Letters, 2004Polyglutamine (polyQ) diseases are inherited neurodegenerative disorders caused by proteins with expanded polyQ regions. Although the pathological mechanisms of these diseases have not yet been elucidated, the processes of protein misfolding and aggregation seem to be a direct cause of neurodegeneration.
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