PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21827905-5 2012 MJD/SCA3 is one of nine identified polyglutamine neurodegenerative diseases which share features of pathogenesis centered on protein misfolding and accumulation. polyglutamine 35-48 ataxin 3 Homo sapiens 4-8 22337953-4 2012 Conversely, transgenic expression of polyglutamine-encoding (exp)CAA ATXN3 was not toxic. polyglutamine 37-50 ataxin 3 Homo sapiens 69-74 22133674-1 2012 Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is the most common inherited spinocerebellar ataxia and one of many polyglutamine neurodegenerative diseases. polyglutamine 150-163 ataxin 3 Homo sapiens 44-73 22133674-1 2012 Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is the most common inherited spinocerebellar ataxia and one of many polyglutamine neurodegenerative diseases. polyglutamine 150-163 ataxin 3 Homo sapiens 75-79 22133674-2 2012 In MJD, a CAG repeat expansion encodes an abnormally long polyglutamine (polyQ) tract in the disease protein, ATXN3. polyglutamine 58-71 ataxin 3 Homo sapiens 110-115 22133674-2 2012 In MJD, a CAG repeat expansion encodes an abnormally long polyglutamine (polyQ) tract in the disease protein, ATXN3. polyglutamine 73-78 ataxin 3 Homo sapiens 110-115 22133674-6 2012 Expansion of the polyQ tract in ATXN3 is thought to promote an altered conformation in the protein, leading to changes in interactions with native partners and to the formation of insoluble aggregates. polyglutamine 17-22 ataxin 3 Homo sapiens 32-37 22133674-7 2012 The development of a wide range of cellular and animal models of MJD has been crucial to the emerging understanding of ATXN3 dysfunction upon polyQ expansion. polyglutamine 142-147 ataxin 3 Homo sapiens 119-124 23382880-0 2013 SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity. polyglutamine 31-36 ataxin 3 Homo sapiens 46-54 23382880-2 2013 Spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD) is an autosomal dominant neurodegenerative disease caused by polyQ-expanded ataxin-3. polyglutamine 125-130 ataxin 3 Homo sapiens 140-148 22234302-1 2012 Ataxin-3 (AT3) triggers spinocerebellar ataxia type 3 when it carries a polyglutamine stretch expanded beyond a critical threshold. polyglutamine 72-85 ataxin 3 Homo sapiens 0-8 22234302-1 2012 Ataxin-3 (AT3) triggers spinocerebellar ataxia type 3 when it carries a polyglutamine stretch expanded beyond a critical threshold. polyglutamine 72-85 ataxin 3 Homo sapiens 10-13 21827905-6 2012 The specific properties of MJD/SCA3 and its disease protein are discussed in light of what is known about the entire class of polyglutamine diseases. polyglutamine 126-139 ataxin 3 Homo sapiens 31-35 22970133-2 2012 Machado-Joseph disease (MJD) or Spinocerebellar Ataxia type 3 is caused by a polyglutamine-encoding CAG expansion in the ATXN3 gene, which encodes a 42 kDa deubiquitinating enzyme (DUB), ataxin-3. polyglutamine 77-90 ataxin 3 Homo sapiens 121-126 22970133-2 2012 Machado-Joseph disease (MJD) or Spinocerebellar Ataxia type 3 is caused by a polyglutamine-encoding CAG expansion in the ATXN3 gene, which encodes a 42 kDa deubiquitinating enzyme (DUB), ataxin-3. polyglutamine 77-90 ataxin 3 Homo sapiens 187-195 22113611-1 2011 Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of polyglutamine (polyQ)-encoding CAG repeats in the MJD1 gene (also known as ATXN3). polyglutamine 159-172 ataxin 3 Homo sapiens 209-213 22113611-1 2011 Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of polyglutamine (polyQ)-encoding CAG repeats in the MJD1 gene (also known as ATXN3). polyglutamine 174-179 ataxin 3 Homo sapiens 209-213 22113611-1 2011 Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of polyglutamine (polyQ)-encoding CAG repeats in the MJD1 gene (also known as ATXN3). polyglutamine 174-179 ataxin 3 Homo sapiens 234-239 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 103-107 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 121-129 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 131-136 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 184-189 21855799-7 2011 In addition, the results shed light on disease pathogenesis in SCA3, a neurodegenerative disorder caused by polyglutamine expansion in ataxin-3. polyglutamine 108-121 ataxin 3 Homo sapiens 63-67 21740957-0 2011 Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease. polyglutamine 0-13 ataxin 3 Homo sapiens 44-52 21740957-4 2011 Machado-Joseph disease (MJD), the most common form of spinocerebellar ataxia worldwide, is a progressive and ultimately fatal neurodegenerative disorder caused by polyQ expansion in ataxin-3 (atx3), a conserved and ubiquitous protein known to bind polyubiquitin chains and to function as a deubiquitinating enzyme. polyglutamine 163-168 ataxin 3 Homo sapiens 182-190 21740957-4 2011 Machado-Joseph disease (MJD), the most common form of spinocerebellar ataxia worldwide, is a progressive and ultimately fatal neurodegenerative disorder caused by polyQ expansion in ataxin-3 (atx3), a conserved and ubiquitous protein known to bind polyubiquitin chains and to function as a deubiquitinating enzyme. polyglutamine 163-168 ataxin 3 Homo sapiens 192-196 21740957-7 2011 Expanded atx3 pathogenicity is likely the result of a series of events implicating both atx3 dysfunction and aggregation, possibly involving both full-length atx3 and polyQ-containing fragments that may act as seeds for protein aggregation. polyglutamine 167-172 ataxin 3 Homo sapiens 9-13 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 67-72 ataxin 3 Homo sapiens 31-35 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 52-65 ataxin 3 Homo sapiens 0-29 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 52-65 ataxin 3 Homo sapiens 31-35 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 67-72 ataxin 3 Homo sapiens 0-29 21780213-2 2011 Ataxin-3, the causative protein of SCA3, contains a globular, structured N-terminal domain (the Josephin domain) and a flexible polyQ-containing C-terminal tail, the repeat-length of which modulates pathogenicity. polyglutamine 128-133 ataxin 3 Homo sapiens 0-8 21780213-2 2011 Ataxin-3, the causative protein of SCA3, contains a globular, structured N-terminal domain (the Josephin domain) and a flexible polyQ-containing C-terminal tail, the repeat-length of which modulates pathogenicity. polyglutamine 128-133 ataxin 3 Homo sapiens 35-39 21780213-3 2011 It has been suggested that the fibrillogenesis pathway of ataxin-3 begins with a non-polyQ-dependent step mediated by Josephin domain interactions, followed by a polyQ-dependent step. polyglutamine 85-90 ataxin 3 Homo sapiens 58-66 21780213-3 2011 It has been suggested that the fibrillogenesis pathway of ataxin-3 begins with a non-polyQ-dependent step mediated by Josephin domain interactions, followed by a polyQ-dependent step. polyglutamine 162-167 ataxin 3 Homo sapiens 58-66 21780213-6 2011 These data support the hypothesis that the first stage of ataxin-3 fibrillogenesis is caused by interactions involving the non-polyQ containing Josephin domain and that the thermodynamic stability of this domain is linked to the aggregation propensity of ataxin-3. polyglutamine 127-132 ataxin 3 Homo sapiens 58-66 21855799-7 2011 In addition, the results shed light on disease pathogenesis in SCA3, a neurodegenerative disorder caused by polyglutamine expansion in ataxin-3. polyglutamine 108-121 ataxin 3 Homo sapiens 135-143 21635785-8 2011 Mutated ATXN3 alleles consensually present about 61 to 87 CAG repeats, resulting in an expanded polyglutamine tract in ataxin-3. polyglutamine 96-109 ataxin 3 Homo sapiens 8-13 21635785-8 2011 Mutated ATXN3 alleles consensually present about 61 to 87 CAG repeats, resulting in an expanded polyglutamine tract in ataxin-3. polyglutamine 96-109 ataxin 3 Homo sapiens 119-127 20732421-1 2011 The presence of aggregates of abnormally expanded polyglutamine (polyQ)-containing proteins are a pathological hallmark of a number of neurodegenerative diseases including Huntington"s disease (HD) and spinocerebellar ataxia-3 (SCA3). polyglutamine 50-63 ataxin 3 Homo sapiens 228-232 21504740-3 2011 It was also shown that expanded ataxin-3 aggregates via a two-stage mechanism initially involving Josephin self-association, followed by a polyQ-dependent step. polyglutamine 139-144 ataxin 3 Homo sapiens 32-40 21533208-0 2011 A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation. polyglutamine 28-41 ataxin 3 Homo sapiens 75-83 20810784-4 2011 Ataxin-3, the protein responsible for Spinocerebellar ataxia type 3, a polyglutamine expansion disease, represents one of such examples. polyglutamine 71-84 ataxin 3 Homo sapiens 0-8 20810784-5 2011 Polyglutamine expansion is central for determining solubility and aggregation rates of ataxin-3, but these properties are profoundly modulated by its N-terminal Josephin domain. polyglutamine 0-13 ataxin 3 Homo sapiens 87-95 20810784-5 2011 Polyglutamine expansion is central for determining solubility and aggregation rates of ataxin-3, but these properties are profoundly modulated by its N-terminal Josephin domain. polyglutamine 0-13 ataxin 3 Homo sapiens 161-169 20851218-1 2011 Expansion of a polyglutamine tract in ataxin-3 (polyQ) causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation. polyglutamine 15-28 ataxin 3 Homo sapiens 38-46 20851218-1 2011 Expansion of a polyglutamine tract in ataxin-3 (polyQ) causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation. polyglutamine 48-53 ataxin 3 Homo sapiens 38-46 20732421-1 2011 The presence of aggregates of abnormally expanded polyglutamine (polyQ)-containing proteins are a pathological hallmark of a number of neurodegenerative diseases including Huntington"s disease (HD) and spinocerebellar ataxia-3 (SCA3). polyglutamine 65-70 ataxin 3 Homo sapiens 228-232 20637808-2 2010 Expansion of a polyglutamine tract in ATXN3 causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation and specific neuronal death. polyglutamine 15-28 ataxin 3 Homo sapiens 38-43 20829225-7 2010 PSA inhibition also increased the levels of polyQ-expanded ataxin-3 as well as mutant alpha-synuclein and superoxide dismutase 1. polyglutamine 44-49 ataxin 3 Homo sapiens 59-67 20140862-0 2010 [Polyglutamine-expanded ataxin-3 is degraded by autophagy]. polyglutamine 1-14 ataxin 3 Homo sapiens 24-32 20064935-0 2010 Nuclear aggregation of polyglutamine-expanded ataxin-3: fragments escape the cytoplasmic quality control. polyglutamine 23-36 ataxin 3 Homo sapiens 46-54 20140862-2 2010 METHODS: HEK293 cells expressing polyglutamine-expanded ataxin-3 were used as cell model for SCA3/MJD. polyglutamine 33-46 ataxin 3 Homo sapiens 56-64 20140862-3 2010 The level of polyglutamine-expanded ataxin-3 was detected after cells were treated with different inhibitors or inducer of autophagy. polyglutamine 13-26 ataxin 3 Homo sapiens 36-44 20140862-5 2010 CONCLUSION: The data suggested that autophagy is involved in the degradation of mutant ataxin-3, resulting in a decrease in the proportions of aggregate-containing cells and cell death in HEK293 cells expressing polyglutamine-expanded ataxin-3. polyglutamine 212-225 ataxin 3 Homo sapiens 87-95 20140862-5 2010 CONCLUSION: The data suggested that autophagy is involved in the degradation of mutant ataxin-3, resulting in a decrease in the proportions of aggregate-containing cells and cell death in HEK293 cells expressing polyglutamine-expanded ataxin-3. polyglutamine 212-225 ataxin 3 Homo sapiens 235-243 19843543-1 2010 Spinocerebellar ataxia type 3 (SCA3)/Machado Joseph disease results from expansion of the polyglutamine domain in ataxin-3 (Atx3). polyglutamine 90-103 ataxin 3 Homo sapiens 114-122 19843543-1 2010 Spinocerebellar ataxia type 3 (SCA3)/Machado Joseph disease results from expansion of the polyglutamine domain in ataxin-3 (Atx3). polyglutamine 90-103 ataxin 3 Homo sapiens 124-128 19036964-1 2008 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in ataxin-3 (ATX3; MJD1) protein. polyglutamine 146-159 ataxin 3 Homo sapiens 0-29 19811945-3 2010 Current hypotheses regarding pathogenesis favor the view that mutated ataxin-3, with its polyglutamine expansion, is prone to adopt an abnormal conformation, engage in altered protein-protein interactions and aggregate. polyglutamine 89-102 ataxin 3 Homo sapiens 70-78 19783548-2 2009 Ataxin-3 protein with an expanded polyglutamine (polyQ) repeat causes spinocerebellar ataxia type-3 (SCA3), also called Machado-Joseph disease, and is cleaved in mammalian cells, transgenic mice and SCA3 patient brain tissue. polyglutamine 34-47 ataxin 3 Homo sapiens 0-8 19783548-2 2009 Ataxin-3 protein with an expanded polyglutamine (polyQ) repeat causes spinocerebellar ataxia type-3 (SCA3), also called Machado-Joseph disease, and is cleaved in mammalian cells, transgenic mice and SCA3 patient brain tissue. polyglutamine 49-54 ataxin 3 Homo sapiens 0-8 19429074-1 2009 Machado-Joseph disease is an autosomal dominant spinocerebellar degeneration caused by the expansion of a polyglutamine tract within the gene product, ataxin-3. polyglutamine 106-119 ataxin 3 Homo sapiens 151-159 19910924-11 2010 Indeed, HDAC6-dependent reduction of cellular aggregate formation and increased cytotoxicity of polyQ-expanded ataxin-3 were found in TDP-43 silenced cells. polyglutamine 96-101 ataxin 3 Homo sapiens 111-119 26023252-6 2009 SCA3 is caused by a polyQ expansion in the carboxy-terminal portion of a cytosolic protein ataxin-3 (Atxn3). polyglutamine 20-25 ataxin 3 Homo sapiens 0-4 26023252-6 2009 SCA3 is caused by a polyQ expansion in the carboxy-terminal portion of a cytosolic protein ataxin-3 (Atxn3). polyglutamine 20-25 ataxin 3 Homo sapiens 91-99 26023252-6 2009 SCA3 is caused by a polyQ expansion in the carboxy-terminal portion of a cytosolic protein ataxin-3 (Atxn3). polyglutamine 20-25 ataxin 3 Homo sapiens 101-106 19660550-1 2009 Spinocerebellar ataxia type 3 (SCA3) or Machado-Joseph disease (MJD) belongs to a group of autosomal dominant neurodegenerative diseases, which are caused by the expansion of a polyglutamine repeat in the affected protein, in this case ataxin-3. polyglutamine 177-190 ataxin 3 Homo sapiens 236-244 19185026-1 2009 Machado-Joseph disease (MJD)/spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by polyglutamine expansion in the ataxin-3 protein that confers a toxic gain of function. polyglutamine 128-141 ataxin 3 Homo sapiens 159-167 19492089-8 2009 Analogous cytotoxic results are observed following conformational targeting of normal or polyglutamine-expanded human ataxin-3, which partially aggregate through non-polyglutamine domains. polyglutamine 89-102 ataxin 3 Homo sapiens 118-126 19492089-8 2009 Analogous cytotoxic results are observed following conformational targeting of normal or polyglutamine-expanded human ataxin-3, which partially aggregate through non-polyglutamine domains. polyglutamine 166-179 ataxin 3 Homo sapiens 118-126 19036964-1 2008 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in ataxin-3 (ATX3; MJD1) protein. polyglutamine 146-159 ataxin 3 Homo sapiens 31-35 19036964-1 2008 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in ataxin-3 (ATX3; MJD1) protein. polyglutamine 146-159 ataxin 3 Homo sapiens 173-181 17696782-1 2007 The neurodegenerative disease spinocerebellar ataxia type 3 (SCA3) is caused by the presence of an extended polyglutamine stretch (polyQ) in the unstructured C-terminus of the human ataxin-3 (AT3) protein. polyglutamine 108-121 ataxin 3 Homo sapiens 182-190 18839019-1 2008 OBJECTIVE: Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by an expansion of polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 155-168 ataxin 3 Homo sapiens 202-206 18839019-1 2008 OBJECTIVE: Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by an expansion of polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 155-168 ataxin 3 Homo sapiens 221-229 18599482-2 2008 Here we show that the polyglutamine disease protein, ataxin-3, binds and cleaves ubiquitin chains in a manner suggesting that it functions as a mixed linkage, chain-editing enzyme. polyglutamine 22-35 ataxin 3 Homo sapiens 53-61 18599482-3 2008 Ataxin-3 cleaves ubiquitin chains through its amino-terminal Josephin domain and binds ubiquitin chains through a carboxyl-terminal cluster of ubiquitin interaction motifs neighboring the pathogenic polyglutamine tract. polyglutamine 199-212 ataxin 3 Homo sapiens 0-8 17953484-2 2007 The polyglutamine domain confers toxicity on the protein Ataxin-3 leading to neuronal dysfunction and loss. polyglutamine 4-17 ataxin 3 Homo sapiens 57-65 18665420-2 2008 These include complex diseases like Alzheimer"s disease and Parkinson"s disease, and Mendelian diseases caused by polyglutamine expansion mutations [like Huntington"s disease (HD) and various spinocerebellar ataxias (SCAs), like SCA3]. polyglutamine 114-127 ataxin 3 Homo sapiens 229-233 18385100-2 2008 MJD results from polyglutamine repeat expansion in the MJD-1 gene, conferring a toxic gain of function to the ataxin-3 protein. polyglutamine 17-30 ataxin 3 Homo sapiens 55-60 18385100-2 2008 MJD results from polyglutamine repeat expansion in the MJD-1 gene, conferring a toxic gain of function to the ataxin-3 protein. polyglutamine 17-30 ataxin 3 Homo sapiens 110-118 17983597-1 2008 Machado-Joseph disease/Spinocerebellar ataxia type 3 is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 114-127 ataxin 3 Homo sapiens 137-145 17696782-1 2007 The neurodegenerative disease spinocerebellar ataxia type 3 (SCA3) is caused by the presence of an extended polyglutamine stretch (polyQ) in the unstructured C-terminus of the human ataxin-3 (AT3) protein. polyglutamine 108-121 ataxin 3 Homo sapiens 192-195 17526020-5 2007 Here, we evaluate three different polyglutamine disease proteins--ataxin-1, ataxin-3, and huntingtin--for their ability to disrupt Cajal body localization and reduce the splicing of an artificial reporter in HeLa cells. polyglutamine 34-47 ataxin 3 Homo sapiens 76-84 17488727-0 2007 Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. polyglutamine 60-73 ataxin 3 Homo sapiens 83-91 17434145-1 2007 Machado-Joseph disease (MJD) is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract in MJD-1 gene product, ataxin-3. polyglutamine 100-113 ataxin 3 Homo sapiens 123-128 17434145-1 2007 Machado-Joseph disease (MJD) is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract in MJD-1 gene product, ataxin-3. polyglutamine 100-113 ataxin 3 Homo sapiens 143-151 17300980-1 2007 Ataxin-3 (AT3), a protein that causes spinocerebellar ataxia type 3, has a C-terminus containing a polyglutamine stretch, the length of which can be expanded in its pathological variants. polyglutamine 99-112 ataxin 3 Homo sapiens 0-8 17302910-1 2007 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD-1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 158-163 17302910-1 2007 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD-1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 178-186 17362987-0 2007 Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein. polyglutamine 97-110 ataxin 3 Homo sapiens 14-22 17300980-1 2007 Ataxin-3 (AT3), a protein that causes spinocerebellar ataxia type 3, has a C-terminus containing a polyglutamine stretch, the length of which can be expanded in its pathological variants. polyglutamine 99-112 ataxin 3 Homo sapiens 10-13 17092742-7 2007 In postmortem brain material of both Huntington disease and SCA3, E2-25K staining of polyglutamine aggregates was observed in a subset of neurons bearing intranuclear neuronal inclusions. polyglutamine 85-98 ataxin 3 Homo sapiens 60-64 16801344-5 2006 There may be a link between diseases caused by polyglutamine and polyalanine expansion mutations as it has been shown that the expanded CAG/polyglutamine tract within the SCA3 gene can shift to the GCA[corrected]/polyalanine frame. polyglutamine 47-60 ataxin 3 Homo sapiens 171-175 17172864-5 2006 These studies showed that upregulation of ban mitigates degeneration induced by the pathogenic polyglutamine (polyQ) protein Ataxin-3, which is mutated in the human polyglutamine disease spinocerebellar ataxia type 3 (SCA3). polyglutamine 95-108 ataxin 3 Homo sapiens 218-222 17172864-5 2006 These studies showed that upregulation of ban mitigates degeneration induced by the pathogenic polyglutamine (polyQ) protein Ataxin-3, which is mutated in the human polyglutamine disease spinocerebellar ataxia type 3 (SCA3). polyglutamine 110-115 ataxin 3 Homo sapiens 218-222 16765348-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant inherited neurodegenerative disease caused by the expansion of a polyglutamine repeat within the disease protein, ataxin-3. polyglutamine 127-140 ataxin 3 Homo sapiens 0-29 16765348-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant inherited neurodegenerative disease caused by the expansion of a polyglutamine repeat within the disease protein, ataxin-3. polyglutamine 127-140 ataxin 3 Homo sapiens 176-184 16624810-0 2006 The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. polyglutamine 61-74 ataxin 3 Homo sapiens 25-33 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 15-28 ataxin 3 Homo sapiens 38-46 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 15-28 ataxin 3 Homo sapiens 48-51 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 134-147 ataxin 3 Homo sapiens 38-46 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 134-147 ataxin 3 Homo sapiens 48-51 16822850-2 2006 Understanding the normal functions of AT3 as well as its function in the context of expansion of the polyglutamine tract is critical for understanding the disease process. polyglutamine 101-114 ataxin 3 Homo sapiens 38-41 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 129-142 ataxin 3 Homo sapiens 0-3 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 129-142 ataxin 3 Homo sapiens 223-226 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 129-142 ataxin 3 Homo sapiens 223-226 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 190-203 ataxin 3 Homo sapiens 0-3 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 190-203 ataxin 3 Homo sapiens 223-226 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 190-203 ataxin 3 Homo sapiens 223-226 16791428-4 2006 Using a transfected mammalian cell line, we demonstrate that ATX3 aggregation is noticeably reduced by deletion or replacement of regions other than the polyglutamine tract. polyglutamine 153-166 ataxin 3 Homo sapiens 61-65 16624810-3 2006 Ataxin-3 consists of a folded Josephin domain followed by two ubiquitin-interacting motifs and a C-terminal polyglutamine tract, which in the non-pathological form is less than 45 residues in length. polyglutamine 108-121 ataxin 3 Homo sapiens 0-8 16624810-9 2006 These observations demonstrate that ataxin-3 has an inherent capacity to aggregate through its non-polyglutamine domains. polyglutamine 99-112 ataxin 3 Homo sapiens 36-44 16407371-0 2006 Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. polyglutamine 24-37 ataxin 3 Homo sapiens 47-55 16407371-0 2006 Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. polyglutamine 24-37 ataxin 3 Homo sapiens 118-126 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 49-62 ataxin 3 Homo sapiens 0-29 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 49-62 ataxin 3 Homo sapiens 31-35 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 64-69 ataxin 3 Homo sapiens 0-29 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 64-69 ataxin 3 Homo sapiens 31-35 16407371-3 2006 We demonstrate that the removal of the N-terminus of polyQ-expanded ataxin-3 (AT3) is required for aggregation in vitro and in vivo. polyglutamine 53-58 ataxin 3 Homo sapiens 68-76 16112867-0 2006 Polyglutamine-expanded ataxin-3 activates mitochondrial apoptotic pathway by upregulating Bax and downregulating Bcl-xL. polyglutamine 0-13 ataxin 3 Homo sapiens 23-31 16112867-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Homo sapiens 0-29 16112867-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Homo sapiens 31-35 16112867-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Homo sapiens 121-129 16112867-8 2006 Our results suggest that polyglutamine-expanded ataxin-3-Q79 activates mitochondrial apoptotic pathway and induces neuronal death by upregulating Bax expression and downregulating Bcl-xL expression. polyglutamine 25-38 ataxin 3 Homo sapiens 48-56 15952105-6 2005 Interacting domain analysis revealed that an unknown protein interacted with the C-terminus near the polyglutamine tract of ataxin-3, the other four all interacted with the N-terminus. polyglutamine 101-114 ataxin 3 Homo sapiens 124-132 16118278-2 2005 The affected protein, ataxin-3, which contains an N-terminal Josephin domain followed by tandem ubiquitin (Ub)-interacting motifs (UIMs) and a polyglutamine stretch, has been implicated in the function of the Ub proteasome system. polyglutamine 143-156 ataxin 3 Homo sapiens 22-30 17046388-4 2006 In this report, we describe a purification protocol for ataxin-3, which, in its polyglutamine-expanded form, causes Machado-Joseph disease. polyglutamine 80-93 ataxin 3 Homo sapiens 56-64 16194547-1 2005 Machado-Joseph"s disease is caused by a CAG trinucleotide repeat expansion that is translated into an abnormally long polyglutamine tract in the protein ataxin-3. polyglutamine 118-131 ataxin 3 Homo sapiens 153-161 16194547-7 2005 Furthermore, non-expanded ataxin-3 oligomers are recognized by a specific antibody that targets a conformational epitope present in soluble cytotoxic species found in the fibrillization pathway of expanded polyglutamine proteins and other amyloid-forming proteins. polyglutamine 206-219 ataxin 3 Homo sapiens 26-34 15895563-2 2005 The translated proteins contain abnormally long polyglutamine stretches, and SCA-1, SCA-2, SCA-3/Machado-Joseph disease (MJD), SCA-6, SCA-7, and SCA-17 are "polyglutamine diseases". polyglutamine 157-170 ataxin 3 Homo sapiens 91-96 15767577-1 2005 The polyglutamine-containing neurodegenerative protein ataxin 3 (AT3) has deubiquitylating activity and binds ubiquitin chains with a preference for chains of four or more ubiquitins. polyglutamine 4-17 ataxin 3 Homo sapiens 55-63 15639784-5 2004 Ataxin-3 (both full length and truncated) with normal glutamine repeats are not ubiquitinated, however, ataxin-3 with expanded polyglutamine is ubiquitinated and the ubiquitination depends on the misfolding propensity of the polyglutamine expanded ataxin-3. polyglutamine 225-238 ataxin 3 Homo sapiens 104-112 15544810-1 2004 Expansion of the polyglutamine (polyQ) region in the protein ataxin-3 is associated with spinocerebellar ataxia type 3, an inherited neurodegenerative disorder that belongs to the family of polyQ diseases. polyglutamine 17-30 ataxin 3 Homo sapiens 61-69 15544810-1 2004 Expansion of the polyglutamine (polyQ) region in the protein ataxin-3 is associated with spinocerebellar ataxia type 3, an inherited neurodegenerative disorder that belongs to the family of polyQ diseases. polyglutamine 32-37 ataxin 3 Homo sapiens 61-69 15544810-3 2004 In a previous study, we determined the domain architecture of ataxin-3, suggesting that it comprises a globular domain, named Josephin, and a more flexible C-terminal region, that includes the polyQ tract. polyglutamine 193-198 ataxin 3 Homo sapiens 62-70 15504352-10 2004 In our cellular model, full-length expanded ataxin-3 that leads to neurodegenerative disorders significantly impaired the expression of Bcl-2 protein, which may be, at least in part, responsible for the weak tolerance to polyglutamine toxicity at the early stage of disease and ultimately resulted in an increase of stress-induced cell death upon apoptotic stress. polyglutamine 221-234 ataxin 3 Homo sapiens 44-52 15345714-0 2004 Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. polyglutamine 0-13 ataxin 3 Homo sapiens 27-35 15345714-3 2004 In this study, we have investigated the hypothesis that polyglutamine expansion in the protein ataxin-3 destabilizes the native protein, leading to the accumulation of a partially unfolded, aggregation-prone intermediate. polyglutamine 56-69 ataxin 3 Homo sapiens 95-103 15140190-0 2004 Caspase-mediated proteolysis of the polyglutamine disease protein ataxin-3. polyglutamine 36-49 ataxin 3 Homo sapiens 66-74 14749733-2 2004 We now show that ataxin-3, in which the abnormal expansion of a polyglutamine tract is responsible for spinocerebellar ataxia type 3 (SCA3), undergoes ubiquitylation and degradation by the proteasome. polyglutamine 64-77 ataxin 3 Homo sapiens 17-25 14749733-2 2004 We now show that ataxin-3, in which the abnormal expansion of a polyglutamine tract is responsible for spinocerebellar ataxia type 3 (SCA3), undergoes ubiquitylation and degradation by the proteasome. polyglutamine 64-77 ataxin 3 Homo sapiens 103-132 14749733-2 2004 We now show that ataxin-3, in which the abnormal expansion of a polyglutamine tract is responsible for spinocerebellar ataxia type 3 (SCA3), undergoes ubiquitylation and degradation by the proteasome. polyglutamine 64-77 ataxin 3 Homo sapiens 134-138 14659761-1 2004 Ataxin-3 is a member of the polyglutamine family of proteins, which are associated with at least nine different neurodegenerative diseases. polyglutamine 28-41 ataxin 3 Homo sapiens 0-8 14659761-6 2004 We describe here the first equilibrium folding pathway delineated for any polyglutamine protein and show that ataxin-3 folds reversibly via a single intermediate species. polyglutamine 74-87 ataxin 3 Homo sapiens 110-118 15639784-0 2004 Misfolding promotes the ubiquitination of polyglutamine-expanded ataxin-3, the defective gene product in SCA3/MJD. polyglutamine 42-55 ataxin 3 Homo sapiens 65-73 15639784-0 2004 Misfolding promotes the ubiquitination of polyglutamine-expanded ataxin-3, the defective gene product in SCA3/MJD. polyglutamine 42-55 ataxin 3 Homo sapiens 105-109 15639784-3 2004 By using ataxin-3, the defective gene product of SCA3/MJD, we demonstrate here that the misfolding propensity and the cellular toxicity of a polyglutamine protein is directly proportional to the length of the glutamine repeats and inversely dependent on the size of the corresponding protein. polyglutamine 141-154 ataxin 3 Homo sapiens 9-17 15639784-3 2004 By using ataxin-3, the defective gene product of SCA3/MJD, we demonstrate here that the misfolding propensity and the cellular toxicity of a polyglutamine protein is directly proportional to the length of the glutamine repeats and inversely dependent on the size of the corresponding protein. polyglutamine 141-154 ataxin 3 Homo sapiens 49-53 15639784-5 2004 Ataxin-3 (both full length and truncated) with normal glutamine repeats are not ubiquitinated, however, ataxin-3 with expanded polyglutamine is ubiquitinated and the ubiquitination depends on the misfolding propensity of the polyglutamine expanded ataxin-3. polyglutamine 127-140 ataxin 3 Homo sapiens 104-112 15325242-0 2004 Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin-3. polyglutamine 65-78 ataxin 3 Homo sapiens 42-50 15325242-0 2004 Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin-3. polyglutamine 65-78 ataxin 3 Homo sapiens 87-95 14661975-0 2003 Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36). polyglutamine 124-137 ataxin 3 Homo sapiens 84-92 14661975-1 2003 The protein ataxin-3 is responsible for Machado-Joseph disease/spinocerebellar ataxia type 3, a neurodegenerative disorder caused by the presence of an expanded polyglutamine tract. polyglutamine 161-174 ataxin 3 Homo sapiens 12-20 15152500-3 2003 MJD1 with expanded polyglutamine tract was more resistant to degradation than normal MJD1. polyglutamine 19-32 ataxin 3 Homo sapiens 0-4 15152500-1 2003 Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is neurodegenerative disease which is caused by polyglutamine expansion in a responsible gene product, MJD1/Ataxin3. polyglutamine 114-127 ataxin 3 Homo sapiens 169-173 15152500-1 2003 Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is neurodegenerative disease which is caused by polyglutamine expansion in a responsible gene product, MJD1/Ataxin3. polyglutamine 114-127 ataxin 3 Homo sapiens 174-181 15152500-7 2003 UFD2a markedly promoted ubiquitylation and degradation of MJD1 with expanded polyglutamine tract, resulting in the clearance of MJD1 protein. polyglutamine 77-90 ataxin 3 Homo sapiens 58-62 15152500-7 2003 UFD2a markedly promoted ubiquitylation and degradation of MJD1 with expanded polyglutamine tract, resulting in the clearance of MJD1 protein. polyglutamine 77-90 ataxin 3 Homo sapiens 128-132 15152500-9 2003 In Drosophila model, overexpression of UFD2a significantly suppressed the neurodegeneration induced by expression of MJD1 with expanded polyglutamine tract. polyglutamine 136-149 ataxin 3 Homo sapiens 117-121 12430715-4 2002 First, we examined the relationship between MBs and polyglutamine proteins and demonstrated that one of the polyglutamine proteins, ataxin-3, as well as a 19S proteasomal protein, was preferentially recruited into MBs even in the absence of expanded polyglutamine. polyglutamine 52-65 ataxin 3 Homo sapiens 132-140 12460614-1 2002 Nuclear aggregates (NAs) and neurodegeneration in brains from patients with Machado-Joseph disease (MJD) are both triggered by pathological expansion of CAG/polyglutamine repeat in ataxin-3, but it remains to be clarified whether NA formation is associated with accelerated neurodegeneration. polyglutamine 157-170 ataxin 3 Homo sapiens 181-189 12914917-1 2003 Anomalous expansion of a polyglutamine (polyQ) tract in the protein ataxin-3 causes spinocerebellar ataxia type 3, an autosomal dominant neurodegenerative disease. polyglutamine 25-38 ataxin 3 Homo sapiens 68-76 12297501-4 2002 The C-terminal polyglutamine-containing domain of ataxin-3 inhibits coactivator-dependent transcription and is required for binding coactivators. polyglutamine 15-28 ataxin 3 Homo sapiens 50-58 12430715-4 2002 First, we examined the relationship between MBs and polyglutamine proteins and demonstrated that one of the polyglutamine proteins, ataxin-3, as well as a 19S proteasomal protein, was preferentially recruited into MBs even in the absence of expanded polyglutamine. polyglutamine 108-121 ataxin 3 Homo sapiens 132-140 11572863-3 2001 Here, in studies of the spinocerebellar ataxia type 3 disease protein ataxin-3, we demonstrate that the protein sequence surrounding polyQ specifies the constituents of nuclear inclusions (NI) formed by the disease protein. polyglutamine 133-138 ataxin 3 Homo sapiens 70-78 11719247-5 2001 Recently, the transglutaminase activity has been hypothesized to be involved in the pathogenetic mechanisms responsible for the formation of cellular inclusions present in Huntington disease and in all the other polyglutamine (polyQ) diseases hitherto identified, such as spinobulbar muscular atrophy or Kennedy disease, spinocerebellar ataxias (SCA-1, SCA-2, SCA-3 or Machado-Joseph disease, SCA-6 and SCA-7) and dentatorubropallidoluysian atrophy. polyglutamine 227-232 ataxin 3 Homo sapiens 360-365 11572942-1 2001 The protein ataxin-3 contains a polyglutamine region; increasing the number of glutamines beyond 55 in this region gives rise to the neurodegenerative disease spinocerebellar ataxia type 3. polyglutamine 32-45 ataxin 3 Homo sapiens 12-20 11719271-1 2001 Ataxin-3, a protein coded by the Machado-Joseph disease gene, possesses a polyglutamine stretch whose expansion is known to produce neuronal intranuclear inclusion and neurodegeneration. polyglutamine 74-87 ataxin 3 Homo sapiens 0-8 11719271-5 2001 Our data indicates that susceptibility to cell death produced by mutant truncated ataxin-3 differs significantly among different cell lines and provides useful information when using a cultured cell line as an in vitro cellular model of polyglutamine disease. polyglutamine 237-250 ataxin 3 Homo sapiens 82-90 11563629-4 2001 Triple-labeling immunofluorescence demonstrated colocalization of ataxin-2 and ataxin-3 in NIIs containing expanded polyglutamine, irrespective of the disease examined. polyglutamine 116-129 ataxin 3 Homo sapiens 79-87 11561037-3 2001 Because this nuclear inclusion is thought to be formed in response to cellular stress, as occurs in hepatic encephalopathy, even in the absence of an expanded CAG/polyglutamine repeat, recruitment of ataxin-3 and ubiquitin into Marinesco bodies may represent a cellular response to noxious external stimuli unrelated to expanded CAG/polyglutamine. polyglutamine 333-346 ataxin 3 Homo sapiens 200-208 10993685-2 2000 The gene responsible for the disease, a novel gene of unknown function, encodes ataxin-3 containing a polyglutamine stretch. polyglutamine 102-115 ataxin 3 Homo sapiens 80-88 10556285-0 1999 Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix. polyglutamine 55-68 ataxin 3 Homo sapiens 0-8 10928570-4 2000 The first type of mutation present in SCA1, SCA2, SCA3, and SCA7 is an expanded CAG repeat in genes of unknown function that are translated into proteins with expanded polyglutamine tracts. polyglutamine 168-181 ataxin 3 Homo sapiens 50-54 10712199-2 2000 The mutant proteins have shown an expanded polyglutamine tract in SCA1, SCA2, MJD/SCA3, SCA6, SCA7, and DRPLA; a glycine-to-arginine substitution was found in SCA6 as well. polyglutamine 43-56 ataxin 3 Homo sapiens 82-86 10915768-1 2000 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 158-162 10915768-1 2000 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 177-185 10556285-7 1999 Fractionation and immunochemical experiments indicate that this novel conformation of intranuclear ataxin-3 is not due to proteolysis, suggesting instead that association with nuclear protein(s) alters the structure of full-length ataxin-3 which exposes the polyglutamine domain. polyglutamine 258-271 ataxin 3 Homo sapiens 99-107 10556285-7 1999 Fractionation and immunochemical experiments indicate that this novel conformation of intranuclear ataxin-3 is not due to proteolysis, suggesting instead that association with nuclear protein(s) alters the structure of full-length ataxin-3 which exposes the polyglutamine domain. polyglutamine 258-271 ataxin 3 Homo sapiens 231-239 10556285-9 1999 The pathological form of ataxin-3 with an expanded polyglutamine domain also associates with the nuclear matrix. polyglutamine 51-64 ataxin 3 Homo sapiens 25-33 10556285-10 1999 These data suggest that an early event in the pathogenesis of SCA3/MJD may be an altered conformation of ataxin-3 within the nucleus that exposes the polyglutamine domain. polyglutamine 150-163 ataxin 3 Homo sapiens 62-66 10556285-10 1999 These data suggest that an early event in the pathogenesis of SCA3/MJD may be an altered conformation of ataxin-3 within the nucleus that exposes the polyglutamine domain. polyglutamine 150-163 ataxin 3 Homo sapiens 67-70 10556285-10 1999 These data suggest that an early event in the pathogenesis of SCA3/MJD may be an altered conformation of ataxin-3 within the nucleus that exposes the polyglutamine domain. polyglutamine 150-163 ataxin 3 Homo sapiens 105-113 10072437-0 1999 Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. polyglutamine 39-52 ataxin 3 Homo sapiens 100-104 10072437-0 1999 Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. polyglutamine 39-52 ataxin 3 Homo sapiens 105-108 10072437-1 1999 Spinocerebellar ataxia type 3, also known as Machado-Joseph disease (SCA3/MJD), is one of at least eight inherited neurodegenerative diseases caused by expansion of a polyglutamine tract in the disease protein. polyglutamine 167-180 ataxin 3 Homo sapiens 69-73 10072437-1 1999 Spinocerebellar ataxia type 3, also known as Machado-Joseph disease (SCA3/MJD), is one of at least eight inherited neurodegenerative diseases caused by expansion of a polyglutamine tract in the disease protein. polyglutamine 167-180 ataxin 3 Homo sapiens 74-77 9852144-2 1998 Here in cell-based studies of the spinocerebellar ataxia type-3 disease protein, ataxin-3, we address two issues central to aggregation: the role of polyglutamine in recruiting proteins into NI and the role of nuclear localization in promoting aggregation. polyglutamine 149-162 ataxin 3 Homo sapiens 81-89 35386195-0 2022 Plasma PolyQ-ATXN3 Levels Associate With Cerebellar Degeneration and Behavioral Abnormalities in a New AAV-Based SCA3 Mouse Model. polyglutamine 7-12 ataxin 3 Homo sapiens 13-18 9580663-1 1998 It has been reported that the ataxin-3 protein containing a polyglutamine sequence in the pathological range (61-84Q) is localized within the nucleus of neuronal cells, whereas ataxin-3 with a normal repeat length (12-37Q) is predominantly a cytoplasmic protein. polyglutamine 60-73 ataxin 3 Homo sapiens 30-38 34938609-1 2022 Spinocerebellar ataxia type 3 (SCA3) is caused by an expanded polyglutamine stretch in ataxin-3. polyglutamine 62-75 ataxin 3 Homo sapiens 0-29 34938609-1 2022 Spinocerebellar ataxia type 3 (SCA3) is caused by an expanded polyglutamine stretch in ataxin-3. polyglutamine 62-75 ataxin 3 Homo sapiens 87-95 34938609-8 2022 This study provides proof of principle that allele-specific lowering of poly(Q)-expanded ataxin-3 by selective ASOs is feasible and long lasting, with sparing of wild-type ataxin-3 expression in a human cell culture model that is genetically identical to SCA3 patients. polyglutamine 72-79 ataxin 3 Homo sapiens 89-97 34397117-0 2021 Polyglutamine-Expanded Ataxin-3: A Target Engagement Marker for Spinocerebellar Ataxia Type 3 in Peripheral Blood. polyglutamine 0-13 ataxin 3 Homo sapiens 23-31 34397117-6 2021 RESULTS: Statistical analyses revealed a correlation with clinical parameters and a stability of polyQ-expanded ataxin-3 during conversion from the pre-ataxic to the ataxic phases. polyglutamine 97-102 ataxin 3 Homo sapiens 112-120 34397117-7 2021 CONCLUSIONS: The novel immunoassay is able to quantify polyQ-expanded ataxin-3 in plasma and CSF, whereas ataxin-3 levels in plasma correlate with disease severity. polyglutamine 55-60 ataxin 3 Homo sapiens 70-78 34397117-8 2021 Longitudinal analyses demonstrated a high stability of polyQ-expanded ataxin-3 over a short period. polyglutamine 55-60 ataxin 3 Homo sapiens 70-78 34416891-3 2021 We found that treatment with valproate improved the swimming of the MJD zebrafish, affected levels of acetylated histones 3 and 4, but also increased expression of polyglutamine expanded human ataxin-3. polyglutamine 164-177 ataxin 3 Homo sapiens 193-201 34303201-0 2021 Urine levels of the polyglutamine ataxin-3 protein are elevated in patients with spinocerebellar ataxia type 3. polyglutamine 20-33 ataxin 3 Homo sapiens 34-42 34303201-0 2021 Urine levels of the polyglutamine ataxin-3 protein are elevated in patients with spinocerebellar ataxia type 3. polyglutamine 20-33 ataxin 3 Homo sapiens 81-110 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 30-43 ataxin 3 Homo sapiens 52-60 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 30-43 ataxin 3 Homo sapiens 62-67 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 30-43 ataxin 3 Homo sapiens 104-133 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 45-50 ataxin 3 Homo sapiens 52-60 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 45-50 ataxin 3 Homo sapiens 62-67 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 45-50 ataxin 3 Homo sapiens 104-133 34303201-2 2021 Recently, we showed that polyQ ATXN3 is elevated in the plasma and cerebrospinal fluid (CSF) of SCA3 patients, and has the potential to serve as a biological marker for this disease (1). polyglutamine 25-30 ataxin 3 Homo sapiens 31-36 34303201-3 2021 Based on these findings, we investigated whether polyQ ATXN3 can also be detected in urine samples from SCA3 patients. polyglutamine 49-54 ataxin 3 Homo sapiens 55-60 34303201-6 2021 RESULTS: PolyQ ATXN3 can be detected in the urine of SCA3 patients, but not in urine samples from healthy controls or other forms of ataxia. polyglutamine 9-14 ataxin 3 Homo sapiens 15-20 10069576-1 1998 Spinocerebellar ataxia type 3 or Machado-Joseph disease (SCA3/MJD) is an autosomal dominant neurodegenerative disorder caused by an unstable and expanded CAG trinucleotide repeat that leads to the expansion of a polyglutamine tract in a protein of unknown function, ataxin-3. polyglutamine 212-225 ataxin 3 Homo sapiens 266-274 10069576-6 1998 In the brain, only one ataxin-3 isoform containing the polyglutamine stretch was detected, and normal and mutated proteins were found equally expressed in all patient brain regions analyzed. polyglutamine 55-68 ataxin 3 Homo sapiens 23-31 8968739-1 1996 Expansion of trinucleotide CAG repeats coding for polyglutamine has been implicated in five neurodegenerative disorders, including spinocerebellar ataxia (SCA) 1 and SCA3 or Machado-Joseph disease (SCA3/MJD), two forms of type I autosomal dominant cerebellar ataxias (ADCA). polyglutamine 50-63 ataxin 3 Homo sapiens 166-170 34685571-1 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. polyglutamine 212-225 ataxin 3 Homo sapiens 0-29 34685571-1 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. polyglutamine 212-225 ataxin 3 Homo sapiens 113-118 34685571-1 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. polyglutamine 212-225 ataxin 3 Homo sapiens 183-191 34685571-1 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. polyglutamine 227-232 ataxin 3 Homo sapiens 0-29 34685571-1 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. polyglutamine 227-232 ataxin 3 Homo sapiens 113-118 34685571-1 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. polyglutamine 227-232 ataxin 3 Homo sapiens 183-191 34535635-2 2021 The accumulation of the mutant ataxin-3 proteins carrying expanded polyglutamine (polyQ) leads to selective degeneration of neurons. polyglutamine 67-80 ataxin 3 Homo sapiens 31-39 34535635-2 2021 The accumulation of the mutant ataxin-3 proteins carrying expanded polyglutamine (polyQ) leads to selective degeneration of neurons. polyglutamine 82-87 ataxin 3 Homo sapiens 31-39 34303201-7 2021 There was a significant statistical association between polyQ ATXN3 levels in urine samples and those in plasma. polyglutamine 56-61 ataxin 3 Homo sapiens 62-67 34303201-8 2021 Further, the levels of polyQ ATXN3 urine associated with an earlier age of SCA3 disease onset. polyglutamine 23-28 ataxin 3 Homo sapiens 29-34 34345727-11 2021 Mutation in Ataxin3 polyQ repeats shows pathologically long CAG repeats, 72,10; 72,10; and 72,23 respectively in mutant and wild type allele. polyglutamine 20-25 ataxin 3 Homo sapiens 12-19 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 148-161 ataxin 3 Homo sapiens 0-29 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 148-161 ataxin 3 Homo sapiens 199-207 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 148-161 ataxin 3 Homo sapiens 214-219 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 163-168 ataxin 3 Homo sapiens 0-29 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 163-168 ataxin 3 Homo sapiens 199-207 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 163-168 ataxin 3 Homo sapiens 214-219 35587620-0 2022 Comment on: Polyglutamine-Expanded Ataxin-3: A Target Engagement Marker for Spinocerebellar Ataxia Type 3 in Peripheral Blood. polyglutamine 12-25 ataxin 3 Homo sapiens 35-43 35587632-0 2022 Reply to: "Comment on: Polyglutamine-Expanded Ataxin-3: A Target Engagement Marker for Spinocerebellar Ataxia Type 3 in Peripheral Blood". polyglutamine 23-36 ataxin 3 Homo sapiens 46-54 35488942-2 2022 This disorder is caused by polyglutamine (polyQ)-containing mutant ataxin-3, which tends to misfold and aggregate in neuron cells. polyglutamine 27-40 ataxin 3 Homo sapiens 67-75 35488942-2 2022 This disorder is caused by polyglutamine (polyQ)-containing mutant ataxin-3, which tends to misfold and aggregate in neuron cells. polyglutamine 42-47 ataxin 3 Homo sapiens 67-75 35111747-9 2021 Moreover, miR-409-3p mimic reduced the aggregation of polyglutamine-expanded mutant of ATXN3 and apoptosis. polyglutamine 54-67 ataxin 3 Homo sapiens 87-92 35386195-0 2022 Plasma PolyQ-ATXN3 Levels Associate With Cerebellar Degeneration and Behavioral Abnormalities in a New AAV-Based SCA3 Mouse Model. polyglutamine 7-12 ataxin 3 Homo sapiens 113-117 33741019-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a rare neurodegenerative disorder resulting from an aberrant expansion of a polyglutamine stretch in the ataxin-3 protein and subsequent neuronal death. polyglutamine 116-129 ataxin 3 Homo sapiens 0-29 33837238-0 2021 PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates. polyglutamine 0-5 ataxin 3 Homo sapiens 56-64 33106888-0 2021 PolyQ-expanded ataxin-3 protein levels in peripheral blood mononuclear cells correlate with clinical parameters in SCA3: a pilot study. polyglutamine 0-5 ataxin 3 Homo sapiens 15-23 33106888-0 2021 PolyQ-expanded ataxin-3 protein levels in peripheral blood mononuclear cells correlate with clinical parameters in SCA3: a pilot study. polyglutamine 0-5 ataxin 3 Homo sapiens 115-119 33106888-5 2021 Additionally, polyQ-expanded ataxin-3 protein levels correlated with disease progression and clinical severity as assessed by the Scale for the Assessment and Rating of Ataxia. polyglutamine 14-19 ataxin 3 Homo sapiens 29-37 33106888-10 2021 In conclusion, the polyQ-expanded ataxin-3 protein is a promising candidate as a molecular target engagement marker in SCA3 in future clinical trials, determinable even in-easily accessible-peripheral blood biomaterials. polyglutamine 19-24 ataxin 3 Homo sapiens 34-42 33106888-10 2021 In conclusion, the polyQ-expanded ataxin-3 protein is a promising candidate as a molecular target engagement marker in SCA3 in future clinical trials, determinable even in-easily accessible-peripheral blood biomaterials. polyglutamine 19-24 ataxin 3 Homo sapiens 119-123 33741019-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a rare neurodegenerative disorder resulting from an aberrant expansion of a polyglutamine stretch in the ataxin-3 protein and subsequent neuronal death. polyglutamine 116-129 ataxin 3 Homo sapiens 145-153 31927329-4 2020 Here we show that repeat-targeting short hairpin RNAs preferentially reduce the levels of mutant huntingtin, atrophin-1, ataxin-3, and ataxin-7 proteins in patient-derived fibroblasts and may serve as universal allele-selective reagents for polyglutamine (polyQ) diseases. polyglutamine 241-254 ataxin 3 Homo sapiens 121-129 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Homo sapiens 119-148 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Homo sapiens 150-154 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 15-20 ataxin 3 Homo sapiens 119-148 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 15-20 ataxin 3 Homo sapiens 150-154 33542212-10 2021 Our data suggest that Exoc7/exo70 exerts its ATXN3-polyQ-modifying effect through regulating the E3 ligase function of Prpf19/prp19. polyglutamine 51-56 ataxin 3 Homo sapiens 45-50 33065068-0 2021 Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. polyglutamine 58-71 ataxin 3 Homo sapiens 80-88 33425926-1 2020 DNA damage response (DDR) and apoptosis are reported to be involved in the pathogenesis of many neurodegenerative diseases including polyglutamine (polyQ) disorders, such as Spinocerebellar ataxia type 3 (SCA3) and Huntington"s disease (HD). polyglutamine 133-146 ataxin 3 Homo sapiens 174-203 33425926-1 2020 DNA damage response (DDR) and apoptosis are reported to be involved in the pathogenesis of many neurodegenerative diseases including polyglutamine (polyQ) disorders, such as Spinocerebellar ataxia type 3 (SCA3) and Huntington"s disease (HD). polyglutamine 148-153 ataxin 3 Homo sapiens 174-203 33425926-2 2020 Consistently, an increasing body of studies provide compelling evidence for the crucial roles of ATX3, whose polyQ expansion is defined as the cause of SCA3, in the maintenance of genome integrity and regulation of apoptosis. polyglutamine 109-114 ataxin 3 Homo sapiens 97-101 33425926-3 2020 The polyQ expansion in ATX3 seems to affect its physiological functions in these distinct pathways. polyglutamine 4-9 ataxin 3 Homo sapiens 23-27 32643791-2 2020 Mutations in ataxin-3 cause spinocerebellar ataxia type 3 (SCA3), a neurodegenerative disorder that is a member of the polyglutamine family of diseases. polyglutamine 119-132 ataxin 3 Homo sapiens 13-21 32643791-2 2020 Mutations in ataxin-3 cause spinocerebellar ataxia type 3 (SCA3), a neurodegenerative disorder that is a member of the polyglutamine family of diseases. polyglutamine 119-132 ataxin 3 Homo sapiens 28-57 32361312-1 2020 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is autosomal-dominant neurodegenerative disease caused by an expansion of polyglutamine-encoding CAG repeats in the ATXN3 gene. polyglutamine 156-169 ataxin 3 Homo sapiens 0-29 32361312-1 2020 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is autosomal-dominant neurodegenerative disease caused by an expansion of polyglutamine-encoding CAG repeats in the ATXN3 gene. polyglutamine 156-169 ataxin 3 Homo sapiens 31-35 32361312-1 2020 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is autosomal-dominant neurodegenerative disease caused by an expansion of polyglutamine-encoding CAG repeats in the ATXN3 gene. polyglutamine 156-169 ataxin 3 Homo sapiens 198-203 33629274-1 2021 Spinocerebellar ataxia type 3 (SCA3) is the most common type of SCA worldwide caused by abnormal polyglutamine expansion in the coding region of the ataxin-3 gene. polyglutamine 97-110 ataxin 3 Homo sapiens 0-29 33629274-1 2021 Spinocerebellar ataxia type 3 (SCA3) is the most common type of SCA worldwide caused by abnormal polyglutamine expansion in the coding region of the ataxin-3 gene. polyglutamine 97-110 ataxin 3 Homo sapiens 31-35 33629274-1 2021 Spinocerebellar ataxia type 3 (SCA3) is the most common type of SCA worldwide caused by abnormal polyglutamine expansion in the coding region of the ataxin-3 gene. polyglutamine 97-110 ataxin 3 Homo sapiens 149-157 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 0-29 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 78-86 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 93-98 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 152-157 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 0-29 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 78-86 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 93-98 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 152-157 33087504-2 2020 Although there is no cure for SCA3, gene-silencing approaches to reduce toxic polyQ ATXN3 showed promise in preclinical models. polyglutamine 78-83 ataxin 3 Homo sapiens 84-89 33087504-5 2020 We show that polyQ ATXN3 serves as a marker of target engagement in human fibroblasts, which may bode well for its use in clinical trials. polyglutamine 13-18 ataxin 3 Homo sapiens 19-24 31970864-1 2020 Expansion above a certain threshold in the polyglutamine (polyQ) tract of ataxin-3 is the main cause of neurodegeneration in Machado-Joseph disease. polyglutamine 43-56 ataxin 3 Homo sapiens 74-82 31970864-1 2020 Expansion above a certain threshold in the polyglutamine (polyQ) tract of ataxin-3 is the main cause of neurodegeneration in Machado-Joseph disease. polyglutamine 58-63 ataxin 3 Homo sapiens 74-82 31970864-2 2020 Ataxin-3 contains an N-terminal catalytic domain, called Josephin domain, and a highly aggregation-prone C-terminal domain containing the polyQ tract. polyglutamine 138-143 ataxin 3 Homo sapiens 0-8 31970864-5 2020 We hypothesize that the expansion of the polyQ tract in ataxin-3 could impact CME. polyglutamine 41-46 ataxin 3 Homo sapiens 56-64 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 168-181 ataxin 3 Homo sapiens 0-29 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 183-188 ataxin 3 Homo sapiens 0-29 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 183-188 ataxin 3 Homo sapiens 220-228 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 183-188 ataxin 3 Homo sapiens 230-235 31783119-5 2020 We screened a collection of siRNAs targeting 2742 druggable human genes using a cell-based assay based on luminescence readout of polyQ-expanded ATXN3. polyglutamine 130-135 ataxin 3 Homo sapiens 145-150 31927329-4 2020 Here we show that repeat-targeting short hairpin RNAs preferentially reduce the levels of mutant huntingtin, atrophin-1, ataxin-3, and ataxin-7 proteins in patient-derived fibroblasts and may serve as universal allele-selective reagents for polyglutamine (polyQ) diseases. polyglutamine 256-261 ataxin 3 Homo sapiens 121-129 31669734-0 2020 Pathogenesis of SCA3 and implications for other polyglutamine diseases. polyglutamine 48-61 ataxin 3 Homo sapiens 16-20 31625269-1 2020 The pathology of spinocerebellar ataxia type 3, also known as Machado-Joseph disease, is triggered by aggregation of toxic ataxin-3 (ATXN3) variants containing expanded polyglutamine repeats. polyglutamine 169-182 ataxin 3 Homo sapiens 123-131 32274760-4 2020 The genetic cause of MJD is a polyglutamine (polyQ) repeat expansion in the gene that encodes ataxin-3. polyglutamine 30-43 ataxin 3 Homo sapiens 94-102 32274760-4 2020 The genetic cause of MJD is a polyglutamine (polyQ) repeat expansion in the gene that encodes ataxin-3. polyglutamine 45-50 ataxin 3 Homo sapiens 94-102 32274760-5 2020 This polyQ-containing protein displays a well-defined catalytic activity as ataxin-3 is a deubiquitylating enzyme that removes and disassembles ubiquitin chains from specific substrates. polyglutamine 5-10 ataxin 3 Homo sapiens 76-84 32274760-6 2020 While mutant ataxin-3 with an expanded polyQ repeat induces cellular stress due to its propensity to aggregate, the native functions of wild-type ataxin-3 are linked to the cellular countermeasures against the very same stress conditions inflicted by polyQ-containing and other aggregation-prone proteins. polyglutamine 39-44 ataxin 3 Homo sapiens 13-21 32274760-6 2020 While mutant ataxin-3 with an expanded polyQ repeat induces cellular stress due to its propensity to aggregate, the native functions of wild-type ataxin-3 are linked to the cellular countermeasures against the very same stress conditions inflicted by polyQ-containing and other aggregation-prone proteins. polyglutamine 251-256 ataxin 3 Homo sapiens 13-21 32274760-6 2020 While mutant ataxin-3 with an expanded polyQ repeat induces cellular stress due to its propensity to aggregate, the native functions of wild-type ataxin-3 are linked to the cellular countermeasures against the very same stress conditions inflicted by polyQ-containing and other aggregation-prone proteins. polyglutamine 251-256 ataxin 3 Homo sapiens 146-154 31625269-1 2020 The pathology of spinocerebellar ataxia type 3, also known as Machado-Joseph disease, is triggered by aggregation of toxic ataxin-3 (ATXN3) variants containing expanded polyglutamine repeats. polyglutamine 169-182 ataxin 3 Homo sapiens 133-138 31683630-7 2019 Significant downregulation of both the expanded and non-expanded protein was induced by the morpholino antisense oligomer, with a greater proportion of ataxin-3 protein missing the polyglutamine tract. polyglutamine 181-194 ataxin 3 Homo sapiens 152-160 31767406-3 2020 Here, we demonstrate that the same agents also deplete other polyglutamine disease-related proteins: mutant ataxin-3 and ataxin-7 in cells from spino-cerebellar ataxia patients, and mutant atrophin-1 in cells from dentatorubral-pallidoluysian atrophy patients. polyglutamine 61-74 ataxin 3 Homo sapiens 108-116 31683630-0 2019 Removal of the Polyglutamine Repeat of Ataxin-3 by Redirecting pre-mRNA Processing. polyglutamine 15-28 ataxin 3 Homo sapiens 39-47 31683630-2 2019 One of nine polyglutamine disorders known to date, SCA3 is clinically heterogeneous and the main feature is progressive ataxia, which in turn affects speech, balance and gait of the affected individual. polyglutamine 12-25 ataxin 3 Homo sapiens 51-55 31683630-3 2019 SCA3 is caused by an expanded polyglutamine tract in the ataxin-3 protein, resulting in conformational changes that lead to toxic gain of function. polyglutamine 30-43 ataxin 3 Homo sapiens 0-4 31683630-3 2019 SCA3 is caused by an expanded polyglutamine tract in the ataxin-3 protein, resulting in conformational changes that lead to toxic gain of function. polyglutamine 30-43 ataxin 3 Homo sapiens 57-65 31683630-6 2019 Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2"-O-methyl modified bases on a phosphorothioate backbone. polyglutamine 66-79 ataxin 3 Homo sapiens 89-97 31310802-1 2019 The most commonly inherited dominant ataxia, Spinocerebellar Ataxia Type 3 (SCA3), is caused by a CAG repeat expansion that encodes an abnormally long polyglutamine (polyQ) repeat in the disease protein ataxin-3, a deubiquitinase. polyglutamine 151-164 ataxin 3 Homo sapiens 76-80 31310802-1 2019 The most commonly inherited dominant ataxia, Spinocerebellar Ataxia Type 3 (SCA3), is caused by a CAG repeat expansion that encodes an abnormally long polyglutamine (polyQ) repeat in the disease protein ataxin-3, a deubiquitinase. polyglutamine 166-171 ataxin 3 Homo sapiens 76-80 31691128-1 2019 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is a neurodegenerative disorder caused by a polyglutamine expansion in the ATXN3 gene. polyglutamine 126-139 ataxin 3 Homo sapiens 0-29 31828177-2 2019 The expanded CAG repeat is translated into a prolonged polyglutamine repeat in the ataxin-3 protein and accumulates within inclusions, acquiring toxic properties, which results in degeneration of the cerebellum and brain stem. polyglutamine 55-68 ataxin 3 Homo sapiens 83-91 31687087-2 2019 The expanded CAG repeats encode a polyglutamine (polyQ) tract at the C-terminus of the ATXN3 protein. polyglutamine 49-54 ataxin 3 Homo sapiens 87-92 31687087-3 2019 ATXN3 containing expanded polyQ forms aggregates, leading to subsequent cellular dysfunctions including an impaired ubiquitin-proteasome system (UPS). polyglutamine 26-31 ataxin 3 Homo sapiens 0-5 31691128-1 2019 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is a neurodegenerative disorder caused by a polyglutamine expansion in the ATXN3 gene. polyglutamine 126-139 ataxin 3 Homo sapiens 31-35 31691128-1 2019 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is a neurodegenerative disorder caused by a polyglutamine expansion in the ATXN3 gene. polyglutamine 126-139 ataxin 3 Homo sapiens 157-162 31374463-3 2019 Referred to as SCA3-hESC, this line is heterozygous for the mutant polyglutamine-encoding CAG repeat expansion in the ATXN3 gene. polyglutamine 67-80 ataxin 3 Homo sapiens 118-123 30455355-6 2019 At the pathological level, we found that the expansion of the polyglutamine repeat leads to a stabilization of ataxin-3 and that ataxin-3 isoforms differ in their aggregation properties. polyglutamine 62-75 ataxin 3 Homo sapiens 111-119 30707359-7 2019 We show its usefulness by performing a comparative study of the interactome of the nine polyglutamine (polyQ) disease proteins, namely androgen receptor (AR), atrophin-1 (ATN1), ataxin 1 (ATXN1), ataxin 2 (ATXN2), ataxin 3 (ATXN3), ataxin 7 (ATXN7), calcium voltage-gated channel subunit alpha1 A (CACNA1A), Huntingtin (HTT), and TATA-binding protein (TBP). polyglutamine 88-101 ataxin 3 Homo sapiens 214-222 30707359-7 2019 We show its usefulness by performing a comparative study of the interactome of the nine polyglutamine (polyQ) disease proteins, namely androgen receptor (AR), atrophin-1 (ATN1), ataxin 1 (ATXN1), ataxin 2 (ATXN2), ataxin 3 (ATXN3), ataxin 7 (ATXN7), calcium voltage-gated channel subunit alpha1 A (CACNA1A), Huntingtin (HTT), and TATA-binding protein (TBP). polyglutamine 88-101 ataxin 3 Homo sapiens 224-229 30455355-7 2019 Interestingly, we observed a functional interaction between normal and polyglutamine-expanded ATXN3 allelic variants. polyglutamine 71-84 ataxin 3 Homo sapiens 94-99 31188927-2 2019 Due to an expanded polyglutamine at ataxin-3, SCA3/MJD presents a relentless course with no current disease modifying treatment. polyglutamine 19-32 ataxin 3 Homo sapiens 36-44 31188927-2 2019 Due to an expanded polyglutamine at ataxin-3, SCA3/MJD presents a relentless course with no current disease modifying treatment. polyglutamine 19-32 ataxin 3 Homo sapiens 51-54 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 3 Homo sapiens 67-72 31378764-2 2019 The nuclear presence of polyglutamine-expanded ataxin-3 is of critical importance for the pathogenesis of SCA3. polyglutamine 24-37 ataxin 3 Homo sapiens 47-55 31378764-6 2019 To our knowledge, this is direct evidence that disulfiram elevated the nuclear localization of polyglutamine-expanded ataxin-3 and enhanced the cytotoxicity in a cell model of SCA3. polyglutamine 95-108 ataxin 3 Homo sapiens 118-126 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 105-118 ataxin 3 Homo sapiens 12-41 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 105-118 ataxin 3 Homo sapiens 152-160 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 105-118 ataxin 3 Homo sapiens 162-167 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 120-125 ataxin 3 Homo sapiens 12-41 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 120-125 ataxin 3 Homo sapiens 152-160 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 120-125 ataxin 3 Homo sapiens 162-167 30147021-2 2019 Silencing the expression of polyQ-expanded ATXN3 rescues the cellular disease phenotype. polyglutamine 28-33 ataxin 3 Homo sapiens 43-48 30036587-1 2018 An expansion of the polyglutamine (polyQ) tract within the deubiquitinase ataxin-3 protein is believed to play a role in a neurodegenerative disorder. polyglutamine 20-33 ataxin 3 Homo sapiens 74-82 30036587-1 2018 An expansion of the polyglutamine (polyQ) tract within the deubiquitinase ataxin-3 protein is believed to play a role in a neurodegenerative disorder. polyglutamine 35-40 ataxin 3 Homo sapiens 74-82 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 3 Homo sapiens 73-77 30042316-1 2018 The protein ataxin-3 contains a polyglutamine stretch that triggers amyloid aggregation when it is expanded beyond a critical threshold. polyglutamine 32-45 ataxin 3 Homo sapiens 12-20 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 3-32 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 34-38 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 229-237 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 239-244 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 3-32 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 34-38 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 229-237 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 239-244 30190267-5 2018 In contrast, neurons cultured from zebrafish expressing human ataxin-3 with disease-associated expanded polyQ repeats did not accumulate within nuclei in a manner often reported to occur in SCA3. polyglutamine 104-109 ataxin 3 Homo sapiens 62-70 29972812-6 2018 Ataxin-3 is a 42-kDa protein containing a globular N-terminal Josephin domain and a C-terminal tail that comprises 13 polyglutamine repeats within a low complexity region. polyglutamine 118-131 ataxin 3 Homo sapiens 0-8 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 129-142 ataxin 3 Homo sapiens 100-108 29229556-1 2018 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine (polyQ) tract in the ataxin-3 protein. polyglutamine 152-165 ataxin 3 Homo sapiens 0-29 29229556-1 2018 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine (polyQ) tract in the ataxin-3 protein. polyglutamine 167-172 ataxin 3 Homo sapiens 0-29 29229556-1 2018 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine (polyQ) tract in the ataxin-3 protein. polyglutamine 167-172 ataxin 3 Homo sapiens 187-195 29334808-0 2018 Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1. polyglutamine 101-114 ataxin 3 Homo sapiens 54-62 29334808-4 2018 Ataxin-3 consists of a globular N-terminal Josephin domain, which can aggregate into curvilinear protofibrils, and an unstructured, dynamically disordered C-terminal domain containing three ubiquitin interacting motifs separated by a polyglutamine stretch. polyglutamine 234-247 ataxin 3 Homo sapiens 0-8 29334808-5 2018 Upon expansion of the polyglutamine region above 50 residues, ataxin-3 undergoes a second stage of aggregation in which long, straight amyloid fibrils form. polyglutamine 22-35 ataxin 3 Homo sapiens 62-70 29334808-6 2018 A peptide inhibitor of polyglutamine aggregation, known as polyQ binding peptide 1, has been shown previously to prevent the maturation of ataxin-3 fibrils. polyglutamine 23-36 ataxin 3 Homo sapiens 139-147 29334808-8 2018 Using nanoelectrospray ionisation-mass spectrometry, we demonstrate that polyQ binding peptide 1 binds to monomeric ataxin-3. polyglutamine 73-78 ataxin 3 Homo sapiens 116-124 29334808-9 2018 By investigating the ability of polyQ binding peptide 1 to bind to truncated ataxin-3 constructs lacking one or more domains, we localise the site of this interaction to a 39-residue sequence immediately C-terminal to the Josephin domain. polyglutamine 32-37 ataxin 3 Homo sapiens 77-85 29427106-12 2018 While misfolding of ataxin-3 due to overly long polyglutamine stretches is a critical contributor to the pathogenesis of SCA-3/MJD, the great neuropathological complexity of the disorder remains largely unexplained. polyglutamine 48-61 ataxin 3 Homo sapiens 20-28 29427106-12 2018 While misfolding of ataxin-3 due to overly long polyglutamine stretches is a critical contributor to the pathogenesis of SCA-3/MJD, the great neuropathological complexity of the disorder remains largely unexplained. polyglutamine 48-61 ataxin 3 Homo sapiens 121-130 29427109-0 2018 Polyglutamine-Independent Features in Ataxin-3 Aggregation and Pathogenesis of Machado-Joseph Disease. polyglutamine 0-13 ataxin 3 Homo sapiens 38-46 29111377-0 2018 Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. polyglutamine 41-54 ataxin 3 Homo sapiens 64-72 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 101-114 ataxin 3 Homo sapiens 64-68 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 101-114 ataxin 3 Homo sapiens 71-79 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 116-121 ataxin 3 Homo sapiens 64-68 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 116-121 ataxin 3 Homo sapiens 71-79 29111377-5 2018 Hence, we analyzed the repertoire of proteins interacting with normal and polyQ expanded ataxin-3 by mass spectrometry. polyglutamine 74-79 ataxin 3 Homo sapiens 89-97 29111377-6 2018 This showed that both normal and polyQ expanded ataxin-3 interacted with components of the protein quality control system and mitochondria. polyglutamine 33-38 ataxin 3 Homo sapiens 48-56 29111377-7 2018 Five proteins showed increased interaction with polyQ expanded ataxin-3 relative to normal and three of these were mitochondrial proteins. polyglutamine 48-53 ataxin 3 Homo sapiens 63-71 28722507-6 2017 Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. polyglutamine 24-29 ataxin 3 Homo sapiens 102-107 28722507-6 2017 Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. polyglutamine 24-29 ataxin 3 Homo sapiens 145-150 28722507-6 2017 Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. polyglutamine 108-113 ataxin 3 Homo sapiens 102-107 28065793-0 2017 Polyglutamine expansion of ataxin-3 alters its degree of ubiquitination and phosphorylation at specific sites. polyglutamine 0-13 ataxin 3 Homo sapiens 27-35 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 129-142 ataxin 3 Homo sapiens 65-69 29661116-0 2018 CRISPR/Cas9-Targeted Deletion of Polyglutamine in Spinocerebellar Ataxia Type 3-Derived Induced Pluripotent Stem Cells. polyglutamine 33-46 ataxin 3 Homo sapiens 50-79 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 0-29 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 121-126 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 187-195 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 197-202 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 0-29 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 121-126 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 187-195 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 197-202 29042637-1 2017 The protein ataxin-3 carries a polyglutamine stretch close to the C-terminus that triggers a neurodegenerative disease in humans when its length exceeds a critical threshold. polyglutamine 31-44 ataxin 3 Homo sapiens 12-20 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 0-29 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 31-35 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 156-161 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 200-204 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 144-149 ataxin 3 Homo sapiens 65-69 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 144-149 ataxin 3 Homo sapiens 100-108 28065793-8 2017 However, the distribution of ubiquitinated lysine residues was altered in polyQ expanded ataxin-3, with increased ubiquitination at the new identified ubiquitination site lysine-8. polyglutamine 74-79 ataxin 3 Homo sapiens 89-97 28065793-11 2017 However, the observed differences between the normal and polyQ expanded ataxin-3 with respect to the degree of ubiquitination and phosphorylation on specific sites may have an impact on ataxin-3 function and SCA3 pathogenesis. polyglutamine 57-62 ataxin 3 Homo sapiens 72-80 28065793-11 2017 However, the observed differences between the normal and polyQ expanded ataxin-3 with respect to the degree of ubiquitination and phosphorylation on specific sites may have an impact on ataxin-3 function and SCA3 pathogenesis. polyglutamine 57-62 ataxin 3 Homo sapiens 186-194 28065793-11 2017 However, the observed differences between the normal and polyQ expanded ataxin-3 with respect to the degree of ubiquitination and phosphorylation on specific sites may have an impact on ataxin-3 function and SCA3 pathogenesis. polyglutamine 57-62 ataxin 3 Homo sapiens 208-212 28449807-10 2017 A significant reduction of cancer as cause of death was observed in SCA3/MJD, suggesting a common effect to all polyglutamine diseases. polyglutamine 112-125 ataxin 3 Homo sapiens 73-76 28236575-1 2017 Machado-Joseph disease (MJD) is a genetic neurodegenerative disease caused by an expanded polyglutamine tract within the protein ataxin-3 (ATXN3). polyglutamine 90-103 ataxin 3 Homo sapiens 129-137 28236575-1 2017 Machado-Joseph disease (MJD) is a genetic neurodegenerative disease caused by an expanded polyglutamine tract within the protein ataxin-3 (ATXN3). polyglutamine 90-103 ataxin 3 Homo sapiens 139-144 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 70-83 ataxin 3 Homo sapiens 28-57 26861241-0 2017 Effects of the enlargement of polyglutamine segments on the structure and folding of ataxin-2 and ataxin-3 proteins. polyglutamine 30-43 ataxin 3 Homo sapiens 98-106 26861241-3 2017 In this study, using the I-TASSER method for 3D structure prediction, we investigated the effect of poly-Q tract enlargement on the structure and folding of ataxin-2 and ataxin-3 proteins. polyglutamine 100-106 ataxin 3 Homo sapiens 170-178 26861241-5 2017 The changes observed in the predicted models of the UIM domains in ataxin-3 when the poly-Q track is enlarged provide new insights on possible pathogenic mechanisms. polyglutamine 85-91 ataxin 3 Homo sapiens 67-75 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. polyglutamine 227-240 ataxin 3 Homo sapiens 0-29 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. polyglutamine 227-240 ataxin 3 Homo sapiens 162-167 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. polyglutamine 227-240 ataxin 3 Homo sapiens 200-208 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 70-83 ataxin 3 Homo sapiens 59-63 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 85-90 ataxin 3 Homo sapiens 28-57 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 85-90 ataxin 3 Homo sapiens 59-63 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 52-65 ataxin 3 Homo sapiens 87-95 27878228-1 2016 Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of the polyglutamine domain of the ataxin-3 (ATX3) protein. polyglutamine 148-161 ataxin 3 Homo sapiens 32-61 27878228-1 2016 Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of the polyglutamine domain of the ataxin-3 (ATX3) protein. polyglutamine 148-161 ataxin 3 Homo sapiens 176-184 27878228-1 2016 Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of the polyglutamine domain of the ataxin-3 (ATX3) protein. polyglutamine 148-161 ataxin 3 Homo sapiens 186-190 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 52-65 ataxin 3 Homo sapiens 0-4 27731380-1 2016 Spinocerebellar ataxia type-3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine repeat expansion in the ataxin-3 protein. polyglutamine 81-94 ataxin 3 Homo sapiens 0-29 27731380-1 2016 Spinocerebellar ataxia type-3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine repeat expansion in the ataxin-3 protein. polyglutamine 81-94 ataxin 3 Homo sapiens 119-127 27731380-2 2016 Cleavage of mutant ataxin-3 by proteolytic enzymes yields ataxin-3 fragments containing the polyglutamine stretch. polyglutamine 92-105 ataxin 3 Homo sapiens 19-27 27731380-2 2016 Cleavage of mutant ataxin-3 by proteolytic enzymes yields ataxin-3 fragments containing the polyglutamine stretch. polyglutamine 92-105 ataxin 3 Homo sapiens 58-66 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 77-82 ataxin 3 Homo sapiens 0-4 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 77-82 ataxin 3 Homo sapiens 87-95 27328712-2 2016 This expansion translates into a polyglutamine tract within the ataxin-3 protein that confers a toxic gain-of-function to the mutant protein ataxin-3, contributing to protein misfolding and intracellular accumulation of aggregates and neuronal degeneration. polyglutamine 33-46 ataxin 3 Homo sapiens 64-72 27328712-2 2016 This expansion translates into a polyglutamine tract within the ataxin-3 protein that confers a toxic gain-of-function to the mutant protein ataxin-3, contributing to protein misfolding and intracellular accumulation of aggregates and neuronal degeneration. polyglutamine 33-46 ataxin 3 Homo sapiens 141-149 27133716-3 2016 In this study, we report that a novel J-protein, DNAJ (HSP40) Homolog, Subfamily C, Member 8 (DNAJC8), suppresses the aggregation of polyQ-containing protein in a cellular model of spinocerebellar ataxia type 3 (SCA3), which is also known as Machado-Joseph disease. polyglutamine 133-138 ataxin 3 Homo sapiens 212-216 27133716-3 2016 In this study, we report that a novel J-protein, DNAJ (HSP40) Homolog, Subfamily C, Member 8 (DNAJC8), suppresses the aggregation of polyQ-containing protein in a cellular model of spinocerebellar ataxia type 3 (SCA3), which is also known as Machado-Joseph disease. polyglutamine 133-138 ataxin 3 Homo sapiens 181-210 27133716-7 2016 These results indicate that DNAJC8 can suppress the polyQ aggregation via a distinct mechanism independent of HSP70-based chaperone machinery and have a unique protective role against the aggregation of expanded polyQ-containing proteins such as pathogenic ataxin-3 proteins. polyglutamine 212-217 ataxin 3 Homo sapiens 257-265 27047745-1 2016 An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. polyglutamine 16-29 ataxin 3 Homo sapiens 50-58 26997655-1 2016 BACKGROUND: Spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD) is one of 10 known polyglutamine (polyQ) diseases. polyglutamine 95-108 ataxin 3 Homo sapiens 71-74 26997655-1 2016 BACKGROUND: Spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD) is one of 10 known polyglutamine (polyQ) diseases. polyglutamine 110-115 ataxin 3 Homo sapiens 71-74 27047745-1 2016 An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. polyglutamine 31-36 ataxin 3 Homo sapiens 50-58 27047745-2 2016 The crystal structure of the polyQ-containing carboxy-terminal fragment of human ataxin-3 was solved at 2.2-A resolution. polyglutamine 29-34 ataxin 3 Homo sapiens 81-89 26808260-0 2016 Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone. polyglutamine 76-89 ataxin 3 Homo sapiens 99-107 26073430-1 2015 BACKGROUND: Machado-Joseph Disease (MJD), a form of dominantly inherited ataxia belonging to the group of polyQ expansion neurodegenerative disorders, occurs when a threshold value for the number of glutamines in Ataxin-3 (Atx3) polyglutamine region is exceeded. polyglutamine 229-242 ataxin 3 Homo sapiens 213-221 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. polyglutamine 201-214 ataxin 3 Homo sapiens 26-30 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. polyglutamine 201-214 ataxin 3 Homo sapiens 164-169 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. polyglutamine 201-214 ataxin 3 Homo sapiens 232-237 26260925-3 2015 For example, polyglutamine expansion in ataxin-3 allosterically triggers the aggregation of the catalytic Josephin domain. polyglutamine 13-26 ataxin 3 Homo sapiens 40-48 26260925-5 2015 Here, we establish that polyglutamine expansion increases the molecular mobility of two juxtaposed helices critical to ataxin-3 deubiquitinase activity. polyglutamine 24-37 ataxin 3 Homo sapiens 119-127 26123252-1 2015 Machado-Joseph disease (MJD, also known as spinocerebellar ataxia type 3, SCA3), an autosomal dominant neurological disorder, is caused by an abnormal expanded polyglutamine (polyQ) repeat in the ataxin-3 protein. polyglutamine 160-173 ataxin 3 Homo sapiens 196-204 26123252-1 2015 Machado-Joseph disease (MJD, also known as spinocerebellar ataxia type 3, SCA3), an autosomal dominant neurological disorder, is caused by an abnormal expanded polyglutamine (polyQ) repeat in the ataxin-3 protein. polyglutamine 175-180 ataxin 3 Homo sapiens 196-204 26037349-7 2015 Wide type and polyQ-expanded ataxin-3 both showed partial co-localization with ER marker calnexin. polyglutamine 14-19 ataxin 3 Homo sapiens 29-37 26037349-9 2015 CONCLUSION: PolyQ-expanded ataxin-3 protein may indirectly affect the integrity of mitochondria, but may cause no effect on the structure and functions of golgi apparatus. polyglutamine 12-17 ataxin 3 Homo sapiens 27-35 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 131-144 ataxin 3 Homo sapiens 15-23 25006867-1 2015 The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). polyglutamine 19-32 ataxin 3 Homo sapiens 55-62 25006867-1 2015 The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). polyglutamine 19-32 ataxin 3 Homo sapiens 70-99 25006867-1 2015 The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). polyglutamine 19-32 ataxin 3 Homo sapiens 101-105 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 146-151 ataxin 3 Homo sapiens 25-30 25700012-3 2015 To complicate matters further, several of the polyglutamine-disease related proteins, including ataxin-3, have a multistage aggregation mechanism in which flanking domain self-assembly precedes polyglutamine aggregation yet is influenced by polyglutamine expansion. polyglutamine 46-59 ataxin 3 Homo sapiens 96-104 25700012-6 2015 We show that the conformational dynamics of the flanking Josephin domain in ataxin-3 with an expanded polyglutamine tract are altered in comparison to those exhibited by its nonexpanded counterpart, specifically within the aggregation-prone region of the Josephin domain (amino acid residues 73-96). polyglutamine 102-115 ataxin 3 Homo sapiens 76-84 25700012-7 2015 Expansion thus exposes this region more frequently in ataxin-3 containing an expanded polyglutamine tract, providing a molecular explanation of why aggregation is accelerated upon polyglutamine expansion. polyglutamine 86-99 ataxin 3 Homo sapiens 54-62 25700012-7 2015 Expansion thus exposes this region more frequently in ataxin-3 containing an expanded polyglutamine tract, providing a molecular explanation of why aggregation is accelerated upon polyglutamine expansion. polyglutamine 180-193 ataxin 3 Homo sapiens 54-62 25700012-11 2015 Overall, the results enable the effect of polyglutamine expansion on every stage of ataxin-3 self-assembly, from monomer through to fibril, to be described and a rationale for expedited aggregation upon polyglutamine expansion to be provided. polyglutamine 42-55 ataxin 3 Homo sapiens 84-92 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 131-144 ataxin 3 Homo sapiens 25-30 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 146-151 ataxin 3 Homo sapiens 15-23 25158237-0 2014 p62/sequestosome 1 regulates aggresome formation of pathogenic ataxin-3 with expanded polyglutamine. polyglutamine 86-99 ataxin 3 Homo sapiens 63-71 25268243-1 2014 Spinocerebellar ataxia (SCA) 3, the most common form of SCA, is a neurodegenerative rare disease characterized by polyglutamine tract expansion and self-assembly of Ataxin3 (At3) misfolded proteins into highly organized fibrillar aggregates. polyglutamine 114-127 ataxin 3 Homo sapiens 0-30 25451224-0 2014 miR-25 alleviates polyQ-mediated cytotoxicity by silencing ATXN3. polyglutamine 18-23 ataxin 3 Homo sapiens 59-64 25231079-0 2014 Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology. polyglutamine 15-28 ataxin 3 Homo sapiens 38-46 25231079-3 2014 We found that the aggregates formed by polyQ-expanded Atx3 sequester its interacting partners, such as P97/VCP and ubiquitin conjugates, into the protein inclusions through specific interactions both in vitro and in cells. polyglutamine 39-44 ataxin 3 Homo sapiens 54-58 25231079-5 2014 However, expansion of polyQ tract in Atx3 does not alter the conformation of its surrounding regions and the interaction affinities with the interacting partners, although it indeed facilitates misfolding and aggregation of the Atx3 protein. polyglutamine 22-27 ataxin 3 Homo sapiens 37-41 25231079-5 2014 However, expansion of polyQ tract in Atx3 does not alter the conformation of its surrounding regions and the interaction affinities with the interacting partners, although it indeed facilitates misfolding and aggregation of the Atx3 protein. polyglutamine 22-27 ataxin 3 Homo sapiens 228-232 25158237-4 2014 In this study we demonstrate that p62 directly interacts with pathogenic Machado Joseph Disease (MJD)-associated protein ataxin-3 with polyglutamine (polyQ) expansion. polyglutamine 135-148 ataxin 3 Homo sapiens 121-129 25158237-4 2014 In this study we demonstrate that p62 directly interacts with pathogenic Machado Joseph Disease (MJD)-associated protein ataxin-3 with polyglutamine (polyQ) expansion. polyglutamine 150-155 ataxin 3 Homo sapiens 121-129 25144244-1 2014 Polyglutamine repeat expansion in ataxin-3 causes neurodegeneration in the most common dominant ataxia, spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Homo sapiens 34-42 23659897-1 2013 Spinocerebellar ataxia type 3 is caused by a polyglutamine expansion in the ataxin-3 protein, resulting in gain of toxic function of the mutant protein. polyglutamine 45-58 ataxin 3 Homo sapiens 76-84 23659897-4 2013 Here, we propose a novel protein modification approach to reduce mutant ataxin-3 toxicity by removing the toxic polyglutamine repeat from the ataxin-3 protein through antisense oligonucleotide-mediated exon skipping while maintaining important wild type functions of the protein. polyglutamine 112-125 ataxin 3 Homo sapiens 72-80 23659897-4 2013 Here, we propose a novel protein modification approach to reduce mutant ataxin-3 toxicity by removing the toxic polyglutamine repeat from the ataxin-3 protein through antisense oligonucleotide-mediated exon skipping while maintaining important wild type functions of the protein. polyglutamine 112-125 ataxin 3 Homo sapiens 142-150 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 52-65 ataxin 3 Homo sapiens 0-29 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 52-65 ataxin 3 Homo sapiens 31-35 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 67-72 ataxin 3 Homo sapiens 0-29 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 67-72 ataxin 3 Homo sapiens 31-35 23894474-8 2013 These results highlight the effect of intracellular factors on the ataxin-3 misfolding landscape and their implications in SCA3 and polyQ diseases in general are discussed. polyglutamine 132-137 ataxin 3 Homo sapiens 67-75 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 124-137 ataxin 3 Homo sapiens 0-8 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 124-137 ataxin 3 Homo sapiens 10-13 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 139-144 ataxin 3 Homo sapiens 0-8 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 139-144 ataxin 3 Homo sapiens 10-13 24293103-2 2014 The C-terminus of the ataxin-3 protein contains a polyglutamine (PolyQ) region that, when mutationally expanded to over 52 glutamines, causes the neurodegenerative disease spinocerebellar ataxia 3 (SCA3). polyglutamine 65-70 ataxin 3 Homo sapiens 22-30 24293103-2 2014 The C-terminus of the ataxin-3 protein contains a polyglutamine (PolyQ) region that, when mutationally expanded to over 52 glutamines, causes the neurodegenerative disease spinocerebellar ataxia 3 (SCA3). polyglutamine 65-70 ataxin 3 Homo sapiens 198-202 24293103-5 2014 Instead, the soluble PolyQ containing fragments arising from proteolytic cleavage of ataxin-3 by caspases and calpains are now regarded to be of greater influence in pathogenesis. polyglutamine 21-26 ataxin 3 Homo sapiens 85-93 23562578-1 2013 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder associated with polyglutamine (polyQ) protein ataxin-3. polyglutamine 85-98 ataxin 3 Homo sapiens 0-29 23562578-1 2013 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder associated with polyglutamine (polyQ) protein ataxin-3. polyglutamine 85-98 ataxin 3 Homo sapiens 115-123