Results 31 to 40 of about 14,352 (184)
Biochemistry Research International, 2012 Huntington’s disease is a progressive neurodegenerative disease, caused by a polyglutamine expansion in the huntingtin protein. A prominent hallmark of the disease is the presence of intracellular aggregates initiated by N-terminal huntingtin fragments ...
Sabine Schipper-Krom +2 more
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Autophagy Modulation as a Treatment of Amyloid Diseases
Molecules, 2019 Amyloids are fibrous proteins aggregated into toxic forms that are implicated in several chronic disorders. More than 30 diseases show deposition of fibrous amyloid proteins associated with cell loss and degeneration in the affected tissues.
Zoe Mputhia +5 more
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Skeletal Muscle Pathogenesis in Polyglutamine Diseases
Cells, 2022 Polyglutamine diseases are characterized by selective dysfunction and degeneration of specific types of neurons in the central nervous system. In addition, nonneuronal cells can also be affected as a consequence of primary degeneration or due to neuronal
Caterina Marchioretti +5 more
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Polyglutamines Placed into Context
Neuron, 2003 Nine inherited neurodegenerative disorders result from polyglutamine expansions. Two recently published papers on spinocerebellar ataxia type 1, together with studies on spinobulbar muscular atrophy last year, indicate that host protein context is the key arbiter of polyglutamine disease protein toxicity.
La Spada, Albert R, Taylor, J.Paul
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Polyglutamine (polyQ) disorders [PDF]
Nucleus, 2012 Polyglutamine (PolyQ)-related diseases are dominant late-onset genetic disorders that are manifested by progressive neurodegeneration, leading to behavioral and physical impairments. An increased body of evidence suggests that chromatin structure and epigenetic regulation are involved in disease pathology.
Cohen-Carmon D, Meshorer E
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Cells, 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region ...
Katherine J. Robinson +4 more
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Hosting Neurotoxicity in Polyglutamine Disease [PDF]
Cell, 2006 Polyglutamine diseases are caused by an expanded glutamine domain thought to confer a toxic activity onto the respective disease proteins. In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion.
Liu, Nan, Bonini, Nancy M.
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The emerging role of the first 17 amino acids of huntingtin in Huntington’s disease
Biomolecular Concepts, 2015 Huntington’s disease (HD) is caused by a polyglutamine (polyQ) domain that is expanded beyond a critical threshold near the N-terminus of the huntingtin (htt) protein, directly leading to htt aggregation. While full-length htt is a large (on the order of
Arndt James R. +2 more
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Altered Metabolic Signaling and Potential Therapies in Polyglutamine Diseases
MetabolitesPolyglutamine diseases comprise a cluster of genetic disorders involving neurodegeneration and movement disabilities. In polyglutamine diseases, the target proteins become aberrated due to polyglutamine repeat formation.
Alisha Vohra +2 more
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Pharmaceuticals, 2014 Histone deacetylases (HDACs) enzymes, which affect the acetylation status of histones and other important cellular proteins, have been recognized as potentially useful therapeutic targets for a broad range of human disorders.
Elizabeth A. Thomas
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