PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23820820-1 2013 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disease caused by a polyglutamine expansion in the deubiquitinating enzyme, Ataxin-3. polyglutamine 80-93 ataxin 3 Mus musculus 0-29 23765441-1 2013 Machado-Joseph disease (MJD) is a dominantly inherited ataxia caused by a polyglutamine-coding expansion in the ATXN3 gene. polyglutamine 74-87 ataxin 3 Mus musculus 112-117 23955261-0 2014 Mutant ataxin-3 with an abnormally expanded polyglutamine chain disrupts dendritic development and metabotropic glutamate receptor signaling in mouse cerebellar Purkinje cells. polyglutamine 44-57 ataxin 3 Mus musculus 7-15 23820820-1 2013 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disease caused by a polyglutamine expansion in the deubiquitinating enzyme, Ataxin-3. polyglutamine 80-93 ataxin 3 Mus musculus 136-144 23347954-0 2013 H1152 promotes the degradation of polyglutamine-expanded ataxin-3 or ataxin-7 independently of its ROCK-inhibiting effect and ameliorates mutant ataxin-3-induced neurodegeneration in the SCA3 transgenic mouse. polyglutamine 34-47 ataxin 3 Mus musculus 57-65 23801739-1 2013 Machado-Joseph disease or spinocerebellar ataxia type 3, the most common dominantly-inherited spinocerebellar ataxia, results from translation of the polyglutamine-expanded and aggregation prone ataxin 3 protein. polyglutamine 150-163 ataxin 3 Mus musculus 195-203 23347954-1 2013 Spinocerebellar ataxia type 3 (SCA3) caused by polyglutamine-expanded ataxin-3 is the most prevalent subtype of spinocerebellar ataxias. polyglutamine 47-60 ataxin 3 Mus musculus 0-29 23347954-1 2013 Spinocerebellar ataxia type 3 (SCA3) caused by polyglutamine-expanded ataxin-3 is the most prevalent subtype of spinocerebellar ataxias. polyglutamine 47-60 ataxin 3 Mus musculus 31-35 23347954-1 2013 Spinocerebellar ataxia type 3 (SCA3) caused by polyglutamine-expanded ataxin-3 is the most prevalent subtype of spinocerebellar ataxias. polyglutamine 47-60 ataxin 3 Mus musculus 70-78 23347954-5 2013 Therefore, we tested the possibility that ROCK inhibitors, Y27632, H1152 and GSK429286, downregulate protein expression of polyglutamine-expanded ataxin-3-Q79. polyglutamine 123-136 ataxin 3 Mus musculus 146-154 23626768-1 2013 Spinocerebellar Ataxia Type 3 (SCA3), also known as Machado-Joseph disease, is an autosomal dominantly inherited neurodegenerative disease caused by an expanded polyglutamine stretch in the ataxin-3 protein. polyglutamine 161-174 ataxin 3 Mus musculus 0-29 23653622-1 2013 Machado-Joseph disease (MJD) is the most common dominant inherited ataxia worldwide, caused by an unstable CAG trinucleotide expansion mutation within the SCA3 gene resulting in an expanded polyglutamine tract within the ataxin-3 protein. polyglutamine 190-203 ataxin 3 Mus musculus 221-229 23626768-1 2013 Spinocerebellar Ataxia Type 3 (SCA3), also known as Machado-Joseph disease, is an autosomal dominantly inherited neurodegenerative disease caused by an expanded polyglutamine stretch in the ataxin-3 protein. polyglutamine 161-174 ataxin 3 Mus musculus 31-35 23626768-1 2013 Spinocerebellar Ataxia Type 3 (SCA3), also known as Machado-Joseph disease, is an autosomal dominantly inherited neurodegenerative disease caused by an expanded polyglutamine stretch in the ataxin-3 protein. polyglutamine 161-174 ataxin 3 Mus musculus 190-198 23100324-4 2013 We demonstrated in cell culture and mouse brain homogenates that cleavage of overexpressed ataxin-3 by calpains and in particular by calpain-2 occur and that polyglutamine expanded ataxin-3 is more sensitive to calpain degradation. polyglutamine 158-171 ataxin 3 Mus musculus 91-99 23100324-4 2013 We demonstrated in cell culture and mouse brain homogenates that cleavage of overexpressed ataxin-3 by calpains and in particular by calpain-2 occur and that polyglutamine expanded ataxin-3 is more sensitive to calpain degradation. polyglutamine 158-171 ataxin 3 Mus musculus 181-189 22037589-2 2012 An expansion of Cytosine-Adenine-Guanine (CAG) repeats in the ATXN3 gene is translated as an expanded polyglutamine domain in the disease protein, ataxin-3. polyglutamine 102-115 ataxin 3 Mus musculus 62-67 24683430-1 2013 Ataxin-3 is a deubiquitinating enzyme (DUB) that participates in ubiquitin-dependent protein quality control pathways and, based on studies in model systems, may be neuroprotective against toxic polyglutamine proteins such as the Huntington"s disease (HD) protein, huntingtin (htt). polyglutamine 195-208 ataxin 3 Mus musculus 0-8 22843411-2 2012 Over-repetition of a CAG trinucleotide in the MJD1 gene translates into a polyglutamine tract within the ataxin 3 protein, which upon proteolysis may trigger Machado-Joseph disease. polyglutamine 74-87 ataxin 3 Mus musculus 46-50 22843411-2 2012 Over-repetition of a CAG trinucleotide in the MJD1 gene translates into a polyglutamine tract within the ataxin 3 protein, which upon proteolysis may trigger Machado-Joseph disease. polyglutamine 74-87 ataxin 3 Mus musculus 105-113 22037589-2 2012 An expansion of Cytosine-Adenine-Guanine (CAG) repeats in the ATXN3 gene is translated as an expanded polyglutamine domain in the disease protein, ataxin-3. polyglutamine 102-115 ataxin 3 Mus musculus 147-155 21047555-1 2011 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Mus musculus 0-29 21092747-10 2011 Our results suggest that polyglutamine-expanded ataxin-3 upregulates mRNA expression of Bax and PUMA and causes apoptotic death of affected neurons by enhancing phosphorylation and transcriptional activity of p53. polyglutamine 25-38 ataxin 3 Mus musculus 48-56 21944750-1 2011 Polyglutamine(polyQ)-expanded proteins are potential therapeutic targets for the treatment of polyQ expansion disorders such as Huntington"s disease (HD) and spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Mus musculus 158-187 21944750-1 2011 Polyglutamine(polyQ)-expanded proteins are potential therapeutic targets for the treatment of polyQ expansion disorders such as Huntington"s disease (HD) and spinocerebellar ataxia type 3 (SCA3). polyglutamine 14-19 ataxin 3 Mus musculus 158-187 21944750-1 2011 Polyglutamine(polyQ)-expanded proteins are potential therapeutic targets for the treatment of polyQ expansion disorders such as Huntington"s disease (HD) and spinocerebellar ataxia type 3 (SCA3). polyglutamine 94-99 ataxin 3 Mus musculus 158-187 21092747-0 2011 p53 activation mediates polyglutamine-expanded ataxin-3 upregulation of Bax expression in cerebellar and pontine nuclei neurons. polyglutamine 24-37 ataxin 3 Mus musculus 47-55 21092747-1 2011 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by polyglutamine-expanded ataxin-3. polyglutamine 99-112 ataxin 3 Mus musculus 0-29 21092747-1 2011 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by polyglutamine-expanded ataxin-3. polyglutamine 99-112 ataxin 3 Mus musculus 31-35 21092747-1 2011 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by polyglutamine-expanded ataxin-3. polyglutamine 99-112 ataxin 3 Mus musculus 122-130 21092747-3 2011 Polyglutamine-expanded ataxin-3-Q79 caused apoptotic death of cerebellar and pontine nuclei neurons by upregulating mRNA expression of pro-apoptotic Bax and activating mitochondria-mediated apoptotic cascade. polyglutamine 0-13 ataxin 3 Mus musculus 23-31 21047555-1 2011 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Mus musculus 121-129 20940148-1 2011 Machado-Joseph disease (MJD), the most common dominantly inherited ataxia worldwide, is caused by a polyglutamine (polyQ) expansion in the deubiquitinating (DUB) enzyme ataxin-3. polyglutamine 100-113 ataxin 3 Mus musculus 169-177 20940148-1 2011 Machado-Joseph disease (MJD), the most common dominantly inherited ataxia worldwide, is caused by a polyglutamine (polyQ) expansion in the deubiquitinating (DUB) enzyme ataxin-3. polyglutamine 115-120 ataxin 3 Mus musculus 169-177 20940148-6 2011 Compared with wild-type ataxin-3, MJD-linked polyQ-expanded mutant ataxin-3 is more active, possibly owing to its greater efficiency at DUB K27- and K29-linked Ub conjugates on parkin. polyglutamine 45-50 ataxin 3 Mus musculus 24-32 20940148-6 2011 Compared with wild-type ataxin-3, MJD-linked polyQ-expanded mutant ataxin-3 is more active, possibly owing to its greater efficiency at DUB K27- and K29-linked Ub conjugates on parkin. polyglutamine 45-50 ataxin 3 Mus musculus 67-75 20510362-1 2010 Machado-Joseph disease (MJD) is a late-onset neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the ataxin-3 protein. polyglutamine 84-97 ataxin 3 Mus musculus 123-131 20510362-1 2010 Machado-Joseph disease (MJD) is a late-onset neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the ataxin-3 protein. polyglutamine 99-104 ataxin 3 Mus musculus 123-131 18668148-0 2008 PolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner. polyglutamine 0-5 ataxin 3 Mus musculus 15-23 19699305-1 2010 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is caused by the expansion of a polyglutamine repeat in the ataxin-3 protein. polyglutamine 103-116 ataxin 3 Mus musculus 0-29 19699305-1 2010 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is caused by the expansion of a polyglutamine repeat in the ataxin-3 protein. polyglutamine 103-116 ataxin 3 Mus musculus 31-35 19699305-1 2010 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is caused by the expansion of a polyglutamine repeat in the ataxin-3 protein. polyglutamine 103-116 ataxin 3 Mus musculus 131-139 19084066-3 2009 Genetic reduction or elimination of CHIP accelerates disease in transgenic mice expressing polyQ-expanded ataxin-3, the disease protein in Spinocerebellar Ataxia Type 3 (SCA3). polyglutamine 91-96 ataxin 3 Mus musculus 106-114 19084066-3 2009 Genetic reduction or elimination of CHIP accelerates disease in transgenic mice expressing polyQ-expanded ataxin-3, the disease protein in Spinocerebellar Ataxia Type 3 (SCA3). polyglutamine 91-96 ataxin 3 Mus musculus 139-168 19084066-3 2009 Genetic reduction or elimination of CHIP accelerates disease in transgenic mice expressing polyQ-expanded ataxin-3, the disease protein in Spinocerebellar Ataxia Type 3 (SCA3). polyglutamine 91-96 ataxin 3 Mus musculus 170-174 19084066-7 2009 Our results support an aggregation model of polyQ disease pathogenesis in which ataxin-3 microaggregates are a neurotoxic species, and suggest that enhancing CHIP activity is a possible route to therapy for SCA3 and other polyQ diseases. polyglutamine 44-49 ataxin 3 Mus musculus 80-88 20007218-1 2010 Spinocerebellar ataxia type 3 is a neurodegenerative disorder caused by the expansion of the polyglutamine repeat region within the ataxin-3 protein. polyglutamine 93-106 ataxin 3 Mus musculus 132-140 18668148-0 2008 PolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner. polyglutamine 0-5 ataxin 3 Mus musculus 51-59 18668148-0 2008 PolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner. polyglutamine 65-70 ataxin 3 Mus musculus 15-23 18668148-0 2008 PolyQ-expanded ataxin-3 interacts with full-length ataxin-3 in a polyQ length-dependent manner. polyglutamine 65-70 ataxin 3 Mus musculus 51-59 18668148-1 2008 OBJECTIVE: Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) tract in MJD-1 gene product, ataxin-3 (AT3). polyglutamine 164-177 ataxin 3 Mus musculus 55-84 18668148-1 2008 OBJECTIVE: Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) tract in MJD-1 gene product, ataxin-3 (AT3). polyglutamine 164-177 ataxin 3 Mus musculus 86-90 18668148-1 2008 OBJECTIVE: Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) tract in MJD-1 gene product, ataxin-3 (AT3). polyglutamine 164-177 ataxin 3 Mus musculus 195-200 18668148-1 2008 OBJECTIVE: Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) tract in MJD-1 gene product, ataxin-3 (AT3). polyglutamine 164-177 ataxin 3 Mus musculus 215-223 18668148-1 2008 OBJECTIVE: Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) tract in MJD-1 gene product, ataxin-3 (AT3). polyglutamine 179-184 ataxin 3 Mus musculus 55-84 18668148-1 2008 OBJECTIVE: Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) tract in MJD-1 gene product, ataxin-3 (AT3). polyglutamine 179-184 ataxin 3 Mus musculus 86-90 18502140-0 2008 Polyglutamine-expanded ataxin-3 causes cerebellar dysfunction of SCA3 transgenic mice by inducing transcriptional dysregulation. polyglutamine 0-13 ataxin 3 Mus musculus 23-31 18502140-1 2008 In the present study, we prepared a SCA3 animal model by generating transgenic mice expressing polyglutamine-expanded ataxin-3-Q79. polyglutamine 95-108 ataxin 3 Mus musculus 36-40 18502140-1 2008 In the present study, we prepared a SCA3 animal model by generating transgenic mice expressing polyglutamine-expanded ataxin-3-Q79. polyglutamine 95-108 ataxin 3 Mus musculus 118-126 18502140-9 2008 Our study suggests that polyglutamine-expanded ataxin-3 causes cerebellar dysfunction and ataxia by disrupting the normal pattern of gene transcriptions. polyglutamine 24-37 ataxin 3 Mus musculus 47-55 12127147-1 2002 Machado-Joseph disease/spinocerebellar ataxia-3 (MJD/SCA-3) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in the MJD gene-encoded protein ataxin-3. polyglutamine 130-143 ataxin 3 Mus musculus 49-52 17626202-1 2007 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominantly inherited neurodegenerative disorder caused by the expansion of a CAG repeat in the MJD1 gene resulting in an expanded polyglutamine repeat in the ataxin-3 protein. polyglutamine 183-196 ataxin 3 Mus musculus 0-29 17626202-1 2007 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominantly inherited neurodegenerative disorder caused by the expansion of a CAG repeat in the MJD1 gene resulting in an expanded polyglutamine repeat in the ataxin-3 protein. polyglutamine 183-196 ataxin 3 Mus musculus 148-152 17626202-1 2007 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominantly inherited neurodegenerative disorder caused by the expansion of a CAG repeat in the MJD1 gene resulting in an expanded polyglutamine repeat in the ataxin-3 protein. polyglutamine 183-196 ataxin 3 Mus musculus 211-219 17626202-4 2007 However, mice transgenic for ataxin-3 with expanded polyglutamine repeats were severely affected by a strong neurological phenotype with tremor, behavioral deficits, strongly reduced motor and exploratory activity, a hunchback, and premature death at 3 to 6 months of age. polyglutamine 52-65 ataxin 3 Mus musculus 29-37 17764659-1 2007 Spinocerebellar ataxia type 3 is a neurodegenerative disease caused by expansion of a polyglutamine domain in the protein ataxin-3 (ATXN3). polyglutamine 86-99 ataxin 3 Mus musculus 122-130 17764659-1 2007 Spinocerebellar ataxia type 3 is a neurodegenerative disease caused by expansion of a polyglutamine domain in the protein ataxin-3 (ATXN3). polyglutamine 86-99 ataxin 3 Mus musculus 132-137 16389311-1 2005 Machado-Joseph disease (MJD), also called spinocerebellar ataxia type 3, is caused by mutant ataxin-3 with a polyglutamine expansion. polyglutamine 109-122 ataxin 3 Mus musculus 24-27 16389311-1 2005 Machado-Joseph disease (MJD), also called spinocerebellar ataxia type 3, is caused by mutant ataxin-3 with a polyglutamine expansion. polyglutamine 109-122 ataxin 3 Mus musculus 93-101 15537899-1 2004 Machado-Joseph disease (MJD) is an inherited neurodegenerative disorder caused by ataxin-3 with a polyglutamine expansion. polyglutamine 98-111 ataxin 3 Mus musculus 82-90 15537899-7 2004 Reactivity of the Fragment with a panel of antibodies and comigration with truncations of mutant ataxin-3 revealed that it contained residues C terminal to amino acid 221 to include the polyglutamine expansion. polyglutamine 186-199 ataxin 3 Mus musculus 97-105 12127147-1 2002 Machado-Joseph disease/spinocerebellar ataxia-3 (MJD/SCA-3) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in the MJD gene-encoded protein ataxin-3. polyglutamine 130-143 ataxin 3 Mus musculus 53-58 12127147-1 2002 Machado-Joseph disease/spinocerebellar ataxia-3 (MJD/SCA-3) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in the MJD gene-encoded protein ataxin-3. polyglutamine 130-143 ataxin 3 Mus musculus 159-162 12127147-1 2002 Machado-Joseph disease/spinocerebellar ataxia-3 (MJD/SCA-3) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in the MJD gene-encoded protein ataxin-3. polyglutamine 130-143 ataxin 3 Mus musculus 184-192 12127147-4 2002 To test this hypothesis, we transfected BHK-21 and Neuro2a cells transiently with N-terminal truncated ataxin-3 with an expanded polyglutamine stretch. polyglutamine 129-142 ataxin 3 Mus musculus 103-111 11394998-3 2001 We generated transgenic mice in which orexin-containing neurons are ablated by orexinergic-specific expression of a truncated Machado-Joseph disease gene product (ataxin-3) with an expanded polyglutamine stretch. polyglutamine 190-203 ataxin 3 Mus musculus 163-171 11978767-1 2002 Machado-Joseph disease (MJD; MIM 109150) is a late-onset neurodegenerative disorder caused by the expansion of a polyglutamine tract within the MJD1 gene. polyglutamine 113-126 ataxin 3 Mus musculus 144-148 34273111-2 2022 Expansion of a CAG trinucleotide in the MJD1 gene translates into a polyglutamine tract within ataxin-3, which upon proteolysis may lead to MJD. polyglutamine 68-81 ataxin 3 Mus musculus 40-44 9020849-1 1997 Six inherited neurodegenerative diseases are caused by a CAG/polyglutamine expansion, including spinal and bulbar muscular atrophy (SBMA), Huntington"s disease (HD), spinocerebellar ataxia type 1 (SCA1), dentatorubral pallidoluysian atrophy (DRPLA) Machado-Joseph disease (MJD or SCA3) and SCA2. polyglutamine 61-74 ataxin 3 Mus musculus 273-276 9020849-1 1997 Six inherited neurodegenerative diseases are caused by a CAG/polyglutamine expansion, including spinal and bulbar muscular atrophy (SBMA), Huntington"s disease (HD), spinocerebellar ataxia type 1 (SCA1), dentatorubral pallidoluysian atrophy (DRPLA) Machado-Joseph disease (MJD or SCA3) and SCA2. polyglutamine 61-74 ataxin 3 Mus musculus 280-284 34273111-2 2022 Expansion of a CAG trinucleotide in the MJD1 gene translates into a polyglutamine tract within ataxin-3, which upon proteolysis may lead to MJD. polyglutamine 68-81 ataxin 3 Mus musculus 95-103 34220448-1 2021 Spinocerebellar ataxia type 3 (SCA3/MJD) is caused by CAG expansion mutation resulting in a long polyQ domain in mutant ataxin-3. polyglutamine 97-102 ataxin 3 Mus musculus 31-35 34298131-2 2022 It is caused by an expansion of a CAG trinucleotide in the ATXN3 gene, translating into an expanded polyglutamine (polyQ) tract in the ATXN3 protein, that becomes prone to misfolding and aggregation. polyglutamine 100-113 ataxin 3 Mus musculus 59-64 34298131-2 2022 It is caused by an expansion of a CAG trinucleotide in the ATXN3 gene, translating into an expanded polyglutamine (polyQ) tract in the ATXN3 protein, that becomes prone to misfolding and aggregation. polyglutamine 100-113 ataxin 3 Mus musculus 135-140 34298131-2 2022 It is caused by an expansion of a CAG trinucleotide in the ATXN3 gene, translating into an expanded polyglutamine (polyQ) tract in the ATXN3 protein, that becomes prone to misfolding and aggregation. polyglutamine 115-120 ataxin 3 Mus musculus 59-64 34298131-2 2022 It is caused by an expansion of a CAG trinucleotide in the ATXN3 gene, translating into an expanded polyglutamine (polyQ) tract in the ATXN3 protein, that becomes prone to misfolding and aggregation. polyglutamine 115-120 ataxin 3 Mus musculus 135-140 34716557-1 2022 Spinocerebellar ataxia type 3 is the most common autosomal dominant inherited ataxia worldwide, caused by a CAG repeat expansion in the Ataxin-3 gene resulting in a polyglutamine (polyQ)-expansion in the corresponding protein. polyglutamine 165-178 ataxin 3 Mus musculus 136-144 34716557-1 2022 Spinocerebellar ataxia type 3 is the most common autosomal dominant inherited ataxia worldwide, caused by a CAG repeat expansion in the Ataxin-3 gene resulting in a polyglutamine (polyQ)-expansion in the corresponding protein. polyglutamine 180-185 ataxin 3 Mus musculus 136-144 34716557-7 2022 The novel knock-in mouse is characterized by the expression of a polyQ-expansion in the murine Ataxin-3 protein, leading to aggregate formation, especially in brain regions known to be vulnerable in SCA3 patients, and impairment of Purkinje cells. polyglutamine 65-70 ataxin 3 Mus musculus 95-103 34220448-1 2021 Spinocerebellar ataxia type 3 (SCA3/MJD) is caused by CAG expansion mutation resulting in a long polyQ domain in mutant ataxin-3. polyglutamine 97-102 ataxin 3 Mus musculus 36-39 34220448-1 2021 Spinocerebellar ataxia type 3 (SCA3/MJD) is caused by CAG expansion mutation resulting in a long polyQ domain in mutant ataxin-3. polyglutamine 97-102 ataxin 3 Mus musculus 120-128 31960910-1 2020 Proteolytic fragmentation of polyglutamine-expanded ataxin-3 is a concomitant and modifier of the molecular pathogenesis of Machado-Joseph disease (MJD), the most common autosomal dominant cerebellar ataxia. polyglutamine 29-42 ataxin 3 Mus musculus 52-60 35605759-1 2022 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine (polyQ)-encoding CAG repeat in the ATXN3 gene. polyglutamine 114-127 ataxin 3 Mus musculus 0-29 35605759-1 2022 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine (polyQ)-encoding CAG repeat in the ATXN3 gene. polyglutamine 114-127 ataxin 3 Mus musculus 31-35 35605759-1 2022 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine (polyQ)-encoding CAG repeat in the ATXN3 gene. polyglutamine 114-127 ataxin 3 Mus musculus 163-168 35605759-1 2022 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine (polyQ)-encoding CAG repeat in the ATXN3 gene. polyglutamine 129-134 ataxin 3 Mus musculus 0-29 35605759-1 2022 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine (polyQ)-encoding CAG repeat in the ATXN3 gene. polyglutamine 129-134 ataxin 3 Mus musculus 31-35 35605759-1 2022 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine (polyQ)-encoding CAG repeat in the ATXN3 gene. polyglutamine 129-134 ataxin 3 Mus musculus 163-168 35386195-1 2022 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3. polyglutamine 110-123 ataxin 3 Mus musculus 0-29 35386195-1 2022 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3. polyglutamine 110-123 ataxin 3 Mus musculus 31-35 35386195-1 2022 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3. polyglutamine 110-123 ataxin 3 Mus musculus 160-165 35386195-1 2022 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3. polyglutamine 125-130 ataxin 3 Mus musculus 0-29 35386195-1 2022 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3. polyglutamine 125-130 ataxin 3 Mus musculus 31-35 35386195-1 2022 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3. polyglutamine 125-130 ataxin 3 Mus musculus 160-165 35386195-3 2022 We used adeno-associated virus (AAV) technology to develop a new mouse model of SCA3 that recapitulates several features of the human disease, including locomotor defects, cerebellar-specific neuronal loss, polyQ-expanded ATXN3 inclusions, and TDP-43 pathology. polyglutamine 207-212 ataxin 3 Mus musculus 80-84 35386195-5 2022 Interestingly, the levels of polyQ-ATXN3 in plasma correlated with measures of cerebellar degeneration and locomotor deficits in 6-month-old SCA3 mice, supporting the hypothesis that this factor could act as a biomarker for SCA3. polyglutamine 29-34 ataxin 3 Mus musculus 35-40 35386195-5 2022 Interestingly, the levels of polyQ-ATXN3 in plasma correlated with measures of cerebellar degeneration and locomotor deficits in 6-month-old SCA3 mice, supporting the hypothesis that this factor could act as a biomarker for SCA3. polyglutamine 29-34 ataxin 3 Mus musculus 141-145 35386195-5 2022 Interestingly, the levels of polyQ-ATXN3 in plasma correlated with measures of cerebellar degeneration and locomotor deficits in 6-month-old SCA3 mice, supporting the hypothesis that this factor could act as a biomarker for SCA3. polyglutamine 29-34 ataxin 3 Mus musculus 224-228 34199295-6 2021 n-BP treatment led to the depletion of mutant ATXN3 with the expanded polyQ chain and the toxic fragments resulting in increased metabolic activity and alleviated atrophy of SCA3 murine cerebellum. polyglutamine 70-75 ataxin 3 Mus musculus 46-51 35042771-2 2022 The polyglutamine-encoding CAG repeat expansion in the ATXN3 gene results in expression of a mutant form of the ATXN3 protein, a deubiquitinase that causes selective neurodegeneration despite being widely expressed. polyglutamine 4-17 ataxin 3 Mus musculus 55-60 35042771-2 2022 The polyglutamine-encoding CAG repeat expansion in the ATXN3 gene results in expression of a mutant form of the ATXN3 protein, a deubiquitinase that causes selective neurodegeneration despite being widely expressed. polyglutamine 4-17 ataxin 3 Mus musculus 112-117 33741019-5 2021 Expanded ataxin-3 strongly interfered (by stimulation or suppression) with normal ataxin-3 signaling consistent with the pathogenic role of the polyglutamine expansion. polyglutamine 144-157 ataxin 3 Mus musculus 9-17 33411688-0 2020 Polyglutamine-expanded ataxin3 alter specific gene expressions through changing DNA methylation status in SCA3/MJD. polyglutamine 0-13 ataxin 3 Mus musculus 23-30 33411688-0 2020 Polyglutamine-expanded ataxin3 alter specific gene expressions through changing DNA methylation status in SCA3/MJD. polyglutamine 0-13 ataxin 3 Mus musculus 111-114 32867861-2 2020 However, BBB integrity has not been assessed in spinocerebellar ataxias (SCAs) such as Machado-Joseph disease/SCA type 3 (MJD/SCA3), a genetic disorder, triggered by polyglutamine-expanded ataxin-3. polyglutamine 166-179 ataxin 3 Mus musculus 122-125 32867861-2 2020 However, BBB integrity has not been assessed in spinocerebellar ataxias (SCAs) such as Machado-Joseph disease/SCA type 3 (MJD/SCA3), a genetic disorder, triggered by polyglutamine-expanded ataxin-3. polyglutamine 166-179 ataxin 3 Mus musculus 126-130 32867861-2 2020 However, BBB integrity has not been assessed in spinocerebellar ataxias (SCAs) such as Machado-Joseph disease/SCA type 3 (MJD/SCA3), a genetic disorder, triggered by polyglutamine-expanded ataxin-3. polyglutamine 166-179 ataxin 3 Mus musculus 189-197 30760052-2 2019 This expansion translates into a long polyglutamine tract, leading to the misfolding of the mutant protein ataxin-3, which abnormally accumulates in the nucleus, thus leading to neurodegeneration in specific brain regions. polyglutamine 38-51 ataxin 3 Mus musculus 107-115 31157458-2 2019 It is known that expansion of CAG repeats encodes abnormally long polyQ in mutant ataxin-3, the disease protein. polyglutamine 66-71 ataxin 3 Mus musculus 82-90 31394429-2 2019 Both diseases are caused by a CAG-repeat expansion in exon 10 of the Ataxin-3 and exon 8 of the Ataxin-1 gene, respectively, encoding an elongated polyglutamine tract that confers toxic properties to the resulting proteins. polyglutamine 147-160 ataxin 3 Mus musculus 69-77 31666698-6 2019 We further show that these compounds interact with the expanded polyQ stretch and could lower the level of mutant ataxin-3 (ATXN3), another disease-causing protein with an expanded polyQ tract3. polyglutamine 64-69 ataxin 3 Mus musculus 114-122 31666698-6 2019 We further show that these compounds interact with the expanded polyQ stretch and could lower the level of mutant ataxin-3 (ATXN3), another disease-causing protein with an expanded polyQ tract3. polyglutamine 64-69 ataxin 3 Mus musculus 124-129 31666698-6 2019 We further show that these compounds interact with the expanded polyQ stretch and could lower the level of mutant ataxin-3 (ATXN3), another disease-causing protein with an expanded polyQ tract3. polyglutamine 181-186 ataxin 3 Mus musculus 114-122 31666698-6 2019 We further show that these compounds interact with the expanded polyQ stretch and could lower the level of mutant ataxin-3 (ATXN3), another disease-causing protein with an expanded polyQ tract3. polyglutamine 181-186 ataxin 3 Mus musculus 124-129 30343032-2 2019 Spinocerebellar ataxia type 3 (SCA3, also known as Machado-Joseph disease), a hereditary neurodegenerative disease, is caused by an abnormal expansion of the polyglutamine tract in the causative ATXN3 protein. polyglutamine 158-171 ataxin 3 Mus musculus 0-29 30343032-2 2019 Spinocerebellar ataxia type 3 (SCA3, also known as Machado-Joseph disease), a hereditary neurodegenerative disease, is caused by an abnormal expansion of the polyglutamine tract in the causative ATXN3 protein. polyglutamine 158-171 ataxin 3 Mus musculus 195-200 29908063-7 2018 RESULTS: The ATXN3-targeting ASO achieved sustained reduction of polyglutamine-expanded ATXN3 up to 8 weeks after treatment and prevented oligomeric and nuclear accumulation of ATXN3 up to at least 14 weeks after treatment. polyglutamine 65-78 ataxin 3 Mus musculus 13-18 30231063-1 2018 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene which encodes the deubiquitinating enzyme, ATXN3. polyglutamine 102-115 ataxin 3 Mus musculus 0-29 30231063-1 2018 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene which encodes the deubiquitinating enzyme, ATXN3. polyglutamine 102-115 ataxin 3 Mus musculus 31-35 30231063-1 2018 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene which encodes the deubiquitinating enzyme, ATXN3. polyglutamine 102-115 ataxin 3 Mus musculus 153-158 30231063-1 2018 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene which encodes the deubiquitinating enzyme, ATXN3. polyglutamine 102-115 ataxin 3 Mus musculus 207-212 30231063-2 2018 Several mechanisms have been proposed to explain the pathogenic role of mutant, polyQ-expanded ATXN3 in SCA3 including disease protein aggregation, impairment of ubiquitin-proteasomal degradation and transcriptional dysregulation. polyglutamine 80-85 ataxin 3 Mus musculus 95-100 30231063-2 2018 Several mechanisms have been proposed to explain the pathogenic role of mutant, polyQ-expanded ATXN3 in SCA3 including disease protein aggregation, impairment of ubiquitin-proteasomal degradation and transcriptional dysregulation. polyglutamine 80-85 ataxin 3 Mus musculus 104-108 29908063-7 2018 RESULTS: The ATXN3-targeting ASO achieved sustained reduction of polyglutamine-expanded ATXN3 up to 8 weeks after treatment and prevented oligomeric and nuclear accumulation of ATXN3 up to at least 14 weeks after treatment. polyglutamine 65-78 ataxin 3 Mus musculus 88-93 29908063-7 2018 RESULTS: The ATXN3-targeting ASO achieved sustained reduction of polyglutamine-expanded ATXN3 up to 8 weeks after treatment and prevented oligomeric and nuclear accumulation of ATXN3 up to at least 14 weeks after treatment. polyglutamine 65-78 ataxin 3 Mus musculus 88-93 29929540-1 2018 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3) is a progressive neurodegenerative disorder caused by expansion of the polyglutamine repeat in the ataxin-3 protein. polyglutamine 120-133 ataxin 3 Mus musculus 12-41 29929540-1 2018 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3) is a progressive neurodegenerative disorder caused by expansion of the polyglutamine repeat in the ataxin-3 protein. polyglutamine 120-133 ataxin 3 Mus musculus 43-47 29929540-1 2018 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3) is a progressive neurodegenerative disorder caused by expansion of the polyglutamine repeat in the ataxin-3 protein. polyglutamine 120-133 ataxin 3 Mus musculus 148-156 28918024-0 2017 Antisense Oligonucleotide-Mediated Removal of the Polyglutamine Repeat in Spinocerebellar Ataxia Type 3 Mice. polyglutamine 50-63 ataxin 3 Mus musculus 74-103 29476013-1 2018 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder caused by a CAG expansion in the ATXN3 gene leading to a polyglutamine expansion in the ataxin-3 protein. polyglutamine 126-139 ataxin 3 Mus musculus 157-165 28918024-2 2017 The resultant expanded polyglutamine stretch in the mutant ataxin-3 protein causes a gain of toxic function, which eventually leads to neurodegeneration. polyglutamine 23-36 ataxin 3 Mus musculus 59-67 28918024-5 2017 This led to formation of a truncated ataxin-3 protein lacking the toxic polyglutamine expansion, but retaining its ubiquitin binding and cleavage function. polyglutamine 72-85 ataxin 3 Mus musculus 37-45 28624196-1 2017 The most common dominantly inherited ataxia, spinocerebellar ataxia type 3 (SCA3), is an incurable neurodegenerative disorder caused by a CAG repeat expansion in the ATXN3 gene that encodes an abnormally long polyglutamine tract in the disease protein, ATXN3. polyglutamine 209-222 ataxin 3 Mus musculus 45-74 28854700-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene. polyglutamine 81-94 ataxin 3 Mus musculus 0-29 28854700-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene. polyglutamine 81-94 ataxin 3 Mus musculus 31-35 28854700-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3 gene. polyglutamine 81-94 ataxin 3 Mus musculus 132-137 28624196-1 2017 The most common dominantly inherited ataxia, spinocerebellar ataxia type 3 (SCA3), is an incurable neurodegenerative disorder caused by a CAG repeat expansion in the ATXN3 gene that encodes an abnormally long polyglutamine tract in the disease protein, ATXN3. polyglutamine 209-222 ataxin 3 Mus musculus 76-80 28624196-1 2017 The most common dominantly inherited ataxia, spinocerebellar ataxia type 3 (SCA3), is an incurable neurodegenerative disorder caused by a CAG repeat expansion in the ATXN3 gene that encodes an abnormally long polyglutamine tract in the disease protein, ATXN3. polyglutamine 209-222 ataxin 3 Mus musculus 166-171 27165717-1 2016 Machado-Joseph disease (MJD) is a neurodegenerative disorder characterized by an abnormal expansion of the CAG triplet in the ATXN3 gene, translating into a polyglutamine tract within the ataxin-3 protein. polyglutamine 157-170 ataxin 3 Mus musculus 126-131 28445460-1 2017 Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3). polyglutamine 55-68 ataxin 3 Mus musculus 154-162 28445460-1 2017 Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3). polyglutamine 55-68 ataxin 3 Mus musculus 166-195 28445460-1 2017 Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3). polyglutamine 55-68 ataxin 3 Mus musculus 197-201 28445460-1 2017 Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3). polyglutamine 70-75 ataxin 3 Mus musculus 154-162 28445460-1 2017 Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3). polyglutamine 70-75 ataxin 3 Mus musculus 166-195 28445460-1 2017 Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3). polyglutamine 70-75 ataxin 3 Mus musculus 197-201 28445460-7 2017 Here we show that the polyQ domain enables wild-type ataxin 3 to interact with beclin 1, a key initiator of autophagy. polyglutamine 22-27 ataxin 3 Mus musculus 53-61 28445460-10 2017 This activity of ataxin 3 and its polyQ-mediated interaction with beclin 1 was competed for by other soluble proteins with polyQ tracts in a length-dependent fashion. polyglutamine 34-39 ataxin 3 Mus musculus 17-25 28445460-10 2017 This activity of ataxin 3 and its polyQ-mediated interaction with beclin 1 was competed for by other soluble proteins with polyQ tracts in a length-dependent fashion. polyglutamine 123-128 ataxin 3 Mus musculus 17-25 28032667-3 2017 Here we investigated the ability of caffeine to alleviate behavioral deficits and cerebellar neuropathology in transgenic mice with a severe ataxia resulting from expression of a truncated fragment of polyglutamine-expanded ataxin-3 in Purkinje cells. polyglutamine 201-214 ataxin 3 Mus musculus 224-232 27851749-5 2016 Furthermore, the polyglutamine (polyQ)-expanded ATX-3 retains enhanced interaction and deubiquitination catalytic activity to p53 and causes more severe p53-dependent neurodegeneration in zebrafish brains and in the substantia nigra pars compacta (SNpc) or striatum of a transgenic SCA3 mouse model. polyglutamine 17-30 ataxin 3 Mus musculus 282-286 27851749-5 2016 Furthermore, the polyglutamine (polyQ)-expanded ATX-3 retains enhanced interaction and deubiquitination catalytic activity to p53 and causes more severe p53-dependent neurodegeneration in zebrafish brains and in the substantia nigra pars compacta (SNpc) or striatum of a transgenic SCA3 mouse model. polyglutamine 32-37 ataxin 3 Mus musculus 282-286 26990650-2 2016 The cause of this disease is the expansion of a CAG repeat in the so-called ATXN3 gene leading to an expanded polyglutamine stretch in the ataxin-3 protein. polyglutamine 110-123 ataxin 3 Mus musculus 76-81 26990650-2 2016 The cause of this disease is the expansion of a CAG repeat in the so-called ATXN3 gene leading to an expanded polyglutamine stretch in the ataxin-3 protein. polyglutamine 110-123 ataxin 3 Mus musculus 139-147 27165717-1 2016 Machado-Joseph disease (MJD) is a neurodegenerative disorder characterized by an abnormal expansion of the CAG triplet in the ATXN3 gene, translating into a polyglutamine tract within the ataxin-3 protein. polyglutamine 157-170 ataxin 3 Mus musculus 188-196 24817574-2 2014 It is caused by an expanded CAG repeat in the ATXN3 gene, which translates into a polyglutamine tract within the ataxin-3 protein. polyglutamine 82-95 ataxin 3 Mus musculus 46-51 25143392-0 2015 Dominant negative effect of polyglutamine expansion perturbs normal function of ataxin-3 in neuronal cells. polyglutamine 28-41 ataxin 3 Mus musculus 80-88 25139423-0 2014 Polyglutamine-expanded ataxin-3 impairs long-term depression in Purkinje neurons of SCA3 transgenic mouse by inhibiting HAT and impairing histone acetylation. polyglutamine 0-13 ataxin 3 Mus musculus 23-31 25139423-0 2014 Polyglutamine-expanded ataxin-3 impairs long-term depression in Purkinje neurons of SCA3 transgenic mouse by inhibiting HAT and impairing histone acetylation. polyglutamine 0-13 ataxin 3 Mus musculus 84-88 25139423-8 2014 Our results suggest that polyglutamine-expanded ataxin-3-Q79 impairs HAT activity, leading to histone hypoacetylation, downregulated expression of cerebellar genes required for LTD induction and impaired induction of cerebellar LTD in the SCA3 transgenic mouse. polyglutamine 25-38 ataxin 3 Mus musculus 48-56 25139423-8 2014 Our results suggest that polyglutamine-expanded ataxin-3-Q79 impairs HAT activity, leading to histone hypoacetylation, downregulated expression of cerebellar genes required for LTD induction and impaired induction of cerebellar LTD in the SCA3 transgenic mouse. polyglutamine 25-38 ataxin 3 Mus musculus 239-243 26254860-0 2015 T1-11 and JMF1907 ameliorate polyglutamine-expanded ataxin-3-induced neurodegeneration, transcriptional dysregulation and ataxic symptom in the SCA3 transgenic mouse. polyglutamine 29-42 ataxin 3 Mus musculus 52-60 26254860-0 2015 T1-11 and JMF1907 ameliorate polyglutamine-expanded ataxin-3-induced neurodegeneration, transcriptional dysregulation and ataxic symptom in the SCA3 transgenic mouse. polyglutamine 29-42 ataxin 3 Mus musculus 144-148 26254860-1 2015 More studies are required to develop therapeutic agents for treating spinocerebellar ataxia type 3 (SCA3), which is caused by mutant polyglutamine-expanded ataxin-3 and is the most prevalent subtype of spinocerebellar ataxias. polyglutamine 133-146 ataxin 3 Mus musculus 69-98 26254860-1 2015 More studies are required to develop therapeutic agents for treating spinocerebellar ataxia type 3 (SCA3), which is caused by mutant polyglutamine-expanded ataxin-3 and is the most prevalent subtype of spinocerebellar ataxias. polyglutamine 133-146 ataxin 3 Mus musculus 100-104 26254860-1 2015 More studies are required to develop therapeutic agents for treating spinocerebellar ataxia type 3 (SCA3), which is caused by mutant polyglutamine-expanded ataxin-3 and is the most prevalent subtype of spinocerebellar ataxias. polyglutamine 133-146 ataxin 3 Mus musculus 156-164 25320121-1 2015 Polyglutamine diseases, including spinocerebellar ataxia type 3 (SCA3), are caused by CAG repeat expansions that encode abnormally long glutamine repeats in the respective disease proteins. polyglutamine 0-13 ataxin 3 Mus musculus 34-63 24817574-2 2014 It is caused by an expanded CAG repeat in the ATXN3 gene, which translates into a polyglutamine tract within the ataxin-3 protein. polyglutamine 82-95 ataxin 3 Mus musculus 113-121 25144231-1 2014 Machado-Joseph disease or Spinocerebellar ataxia type 3 is a progressive fatal neurodegenerative disorder caused by the polyglutamine-expanded protein ataxin-3. polyglutamine 120-133 ataxin 3 Mus musculus 151-159