PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9801928-2 1998 Five genes (SCA1, 2, 3, 6, 7) have been cloned to date and show a single type of mutation, an unstable expansion of a CAG repeat coding for a polyglutamine stretch in the corresponding protein. polyglutamine 142-155 ataxin 1 Homo sapiens 12-16 32962458-1 2020 INTRODUCTION: Six of the most frequent dominantly inherited spinocerebellar ataxias (SCAs) worldwide - SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 - are caused by an expansion of a polyglutamine (polyQ) tract in the corresponding proteins. polyglutamine 177-190 ataxin 1 Homo sapiens 103-107 8872471-1 1996 Spinocerebellar ataxia type1 (SCA1) is one of several neurodegenerative disorders caused by expansions of translated CAG trinucleotide repeats which code for polyglutamine in the respective proteins. polyglutamine 158-171 ataxin 1 Homo sapiens 0-28 8872471-1 1996 Spinocerebellar ataxia type1 (SCA1) is one of several neurodegenerative disorders caused by expansions of translated CAG trinucleotide repeats which code for polyglutamine in the respective proteins. polyglutamine 158-171 ataxin 1 Homo sapiens 30-34 7614095-9 1995 A pathogenetic model is proposed based on the findings in SCA1 and other neurodegenerative diseases caused by expansion of polyglutamine tracts. polyglutamine 123-136 ataxin 1 Homo sapiens 58-62 8190020-1 1994 Three neurodegenerative diseases, Huntington"s disease (HD), Kennedy"s disease (hereditary spinobulbar muscular atrophy, SBMA), and type 1 spinocerebellar ataxia (SCA-1) have been found to share a common genetic defect: an unstable region of repeated CAG trinucleotides which are thought to be translated into a polyglutamine moiety. polyglutamine 312-325 ataxin 1 Homo sapiens 132-168 8190020-6 1994 These products, in part consisting of abnormally large polyglutamine moieties, act to disturb the cellular and mitochondrial milieu such that energy metabolism is impaired, rendering specific regions of the nervous system vulnerable, and resulting in the clinical phenotypes of HD, SBMA, and SCA-1. polyglutamine 55-68 ataxin 1 Homo sapiens 292-297 9353120-1 1997 Spinocerebellar ataxia type 1 (SCA1) is one of several neurodegenerative disorders caused by an expansion of a polyglutamine tract. polyglutamine 111-124 ataxin 1 Homo sapiens 0-29 9353120-1 1997 Spinocerebellar ataxia type 1 (SCA1) is one of several neurodegenerative disorders caused by an expansion of a polyglutamine tract. polyglutamine 111-124 ataxin 1 Homo sapiens 31-35 9353121-3 1997 Although the proteins containing these repeats are widely expressed, the neurodegeneration in SCA1 and other polyglutamine diseases selectively involves a few neuronal subtypes. polyglutamine 109-122 ataxin 1 Homo sapiens 94-98 9187671-5 1997 Patients with SCA1 have the CAG repeat sequence, which encodes a polyglutamine stretch in the ataxin-1 protein, expanded beyond the normal range. polyglutamine 65-78 ataxin 1 Homo sapiens 14-18 9187671-5 1997 Patients with SCA1 have the CAG repeat sequence, which encodes a polyglutamine stretch in the ataxin-1 protein, expanded beyond the normal range. polyglutamine 65-78 ataxin 1 Homo sapiens 94-102 9097953-1 1997 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine tract within the SCA1 gene product, ataxin-1. polyglutamine 118-131 ataxin 1 Homo sapiens 0-29 9097953-1 1997 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine tract within the SCA1 gene product, ataxin-1. polyglutamine 118-131 ataxin 1 Homo sapiens 31-35 9097953-1 1997 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine tract within the SCA1 gene product, ataxin-1. polyglutamine 118-131 ataxin 1 Homo sapiens 149-153 9097953-1 1997 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine tract within the SCA1 gene product, ataxin-1. polyglutamine 118-131 ataxin 1 Homo sapiens 168-176 7477379-4 1995 Here we report the characterization of a monoclonal antibody that selectively recognizes polyglutamine expansion in the proteins implicated in HD and in spinocerebellar ataxia (SCA) 1 and 3. polyglutamine 89-102 ataxin 1 Homo sapiens 153-189 35499073-0 2022 Cross-species genetic screens identify transglutaminase 5 as a regulator of polyglutamine-expanded ataxin-1. polyglutamine 76-89 ataxin 1 Homo sapiens 99-107 35499073-2 2022 In spinocerebellar ataxia type 1 (SCA1), accumulation of polyglutamine-expanded (polyQ-expanded) ataxin-1 (ATXN1) causes neuronal toxicity. polyglutamine 57-70 ataxin 1 Homo sapiens 3-32 35499073-2 2022 In spinocerebellar ataxia type 1 (SCA1), accumulation of polyglutamine-expanded (polyQ-expanded) ataxin-1 (ATXN1) causes neuronal toxicity. polyglutamine 57-70 ataxin 1 Homo sapiens 34-38 35499073-2 2022 In spinocerebellar ataxia type 1 (SCA1), accumulation of polyglutamine-expanded (polyQ-expanded) ataxin-1 (ATXN1) causes neuronal toxicity. polyglutamine 57-70 ataxin 1 Homo sapiens 97-105 35499073-2 2022 In spinocerebellar ataxia type 1 (SCA1), accumulation of polyglutamine-expanded (polyQ-expanded) ataxin-1 (ATXN1) causes neuronal toxicity. polyglutamine 57-70 ataxin 1 Homo sapiens 107-112 32962458-1 2020 INTRODUCTION: Six of the most frequent dominantly inherited spinocerebellar ataxias (SCAs) worldwide - SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 - are caused by an expansion of a polyglutamine (polyQ) tract in the corresponding proteins. polyglutamine 192-197 ataxin 1 Homo sapiens 103-107 32954321-5 2020 Subsequent functional experiments have shown that ATXN1 reduces the nucleocytoplasmic ratio of TDP-43 and enhances amyotrophic lateral sclerosis phenotypes in Drosophila, further emphasizing the role of polyglutamine repeat expansions in the pathophysiology of amyotrophic lateral sclerosis. polyglutamine 203-216 ataxin 1 Homo sapiens 50-55 32992839-0 2020 Dynamics of a Protein Interaction Network Associated to the Aggregation of polyQ-Expanded Ataxin-1. polyglutamine 75-80 ataxin 1 Homo sapiens 90-98 32873576-3 2020 Another striking example of this mutant and WT duality is spinocerebellar ataxia type 1 (SCA1) caused by an ATXN1 polyglutamine protein, although subtle variations in WT AXTN1 levels also lead to ataxia. polyglutamine 114-127 ataxin 1 Homo sapiens 108-113 32581696-1 2020 Polyglutamine spinocerebellar ataxias (polyQ SCAs) include SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 and constitute a group of adult onset neurodegenerative disorders caused by the expansion of a CAG repeat sequence located within the coding region of specific genes, which translates into polyglutamine tract in the corresponding proteins. polyglutamine 0-13 ataxin 1 Homo sapiens 59-63 32581673-2 2020 These polyQ SCAs (SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17) are inherited neurodegenerative diseases characterized by the progressive atrophy of the cerebellum and connected regions of the nervous system, which leads to loss of fine muscle movement coordination. polyglutamine 6-11 ataxin 1 Homo sapiens 18-22 32954321-3 2020 Together with previously published data, the identification of an amyotrophic lateral sclerosis patient with a family history of spinocerebellar ataxia type 1, caused by polyglutamine expansions in ATXN1, suggested a similar disease association for the repeat expansion in ATXN1. polyglutamine 170-183 ataxin 1 Homo sapiens 198-203 32954321-3 2020 Together with previously published data, the identification of an amyotrophic lateral sclerosis patient with a family history of spinocerebellar ataxia type 1, caused by polyglutamine expansions in ATXN1, suggested a similar disease association for the repeat expansion in ATXN1. polyglutamine 170-183 ataxin 1 Homo sapiens 273-278 31381977-1 2020 Expression of mutant Ataxin-1 with an abnormally expanded polyglutamine domain is necessary for the onset and progression of spinocerebellar ataxia type 1 (SCA1). polyglutamine 58-71 ataxin 1 Homo sapiens 21-29 32145456-1 2020 Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. polyglutamine 73-86 ataxin 1 Homo sapiens 0-29 32145456-1 2020 Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. polyglutamine 73-86 ataxin 1 Homo sapiens 31-35 32145456-1 2020 Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. polyglutamine 73-86 ataxin 1 Homo sapiens 104-112 32145456-1 2020 Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. polyglutamine 88-93 ataxin 1 Homo sapiens 0-29 32145456-1 2020 Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. polyglutamine 88-93 ataxin 1 Homo sapiens 31-35 32145456-1 2020 Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. polyglutamine 88-93 ataxin 1 Homo sapiens 104-112 31381977-1 2020 Expression of mutant Ataxin-1 with an abnormally expanded polyglutamine domain is necessary for the onset and progression of spinocerebellar ataxia type 1 (SCA1). polyglutamine 58-71 ataxin 1 Homo sapiens 125-154 31381977-1 2020 Expression of mutant Ataxin-1 with an abnormally expanded polyglutamine domain is necessary for the onset and progression of spinocerebellar ataxia type 1 (SCA1). polyglutamine 58-71 ataxin 1 Homo sapiens 156-160 31655597-2 2019 Pathological polyQ expansion, such as that in human Ataxin-1 (ATXN1), that causes spinocerebellar ataxia type 1 (SCA1), results in abnormal PPI. polyglutamine 13-18 ataxin 1 Homo sapiens 52-60 32671744-3 2020 At least 9 kinds of polyglutamine diseases have been discovered, including Huntington disease (HD), dentatorubral pallidoluysian atrophy (DRPLA), spinobulbar muscular atrophy (SBMA) and six spinocerebellar ataxia (SCA) such as SCA1, 2, 3, 6, 7 and 17 subtypes (Table 9.1). polyglutamine 20-33 ataxin 1 Homo sapiens 227-231 32005838-1 2020 A mutant form of the ataxin-1 protein with an expanded polyglutamine (polyQ) tract is the underlying cause of the inherited neurodegenerative disease spinocerebellar ataxia 1 (SCA1). polyglutamine 55-68 ataxin 1 Homo sapiens 21-29 32005838-1 2020 A mutant form of the ataxin-1 protein with an expanded polyglutamine (polyQ) tract is the underlying cause of the inherited neurodegenerative disease spinocerebellar ataxia 1 (SCA1). polyglutamine 70-75 ataxin 1 Homo sapiens 21-29 31655597-2 2019 Pathological polyQ expansion, such as that in human Ataxin-1 (ATXN1), that causes spinocerebellar ataxia type 1 (SCA1), results in abnormal PPI. polyglutamine 13-18 ataxin 1 Homo sapiens 62-67 31655597-2 2019 Pathological polyQ expansion, such as that in human Ataxin-1 (ATXN1), that causes spinocerebellar ataxia type 1 (SCA1), results in abnormal PPI. polyglutamine 13-18 ataxin 1 Homo sapiens 82-111 31655597-2 2019 Pathological polyQ expansion, such as that in human Ataxin-1 (ATXN1), that causes spinocerebellar ataxia type 1 (SCA1), results in abnormal PPI. polyglutamine 13-18 ataxin 1 Homo sapiens 113-117 31655597-6 2019 RESULTS: Our data supports that the polyQ expansion alters the ATXN1 conformation and that it enhances the strength of interaction with ATXN1 partners. polyglutamine 36-41 ataxin 1 Homo sapiens 63-68 31655597-6 2019 RESULTS: Our data supports that the polyQ expansion alters the ATXN1 conformation and that it enhances the strength of interaction with ATXN1 partners. polyglutamine 36-41 ataxin 1 Homo sapiens 136-141 31655597-7 2019 For both ATXN1 variants, the number of residues at the predicted binding interface are greater after the polyQ, mainly due to the AXH domain. polyglutamine 105-110 ataxin 1 Homo sapiens 9-14 31655597-8 2019 Moreover, the difference in the interaction strength of the ATXN1 variants was due to an increase in the number of interactions at the N-terminal region, before the polyQ, for the expanded form. polyglutamine 165-170 ataxin 1 Homo sapiens 60-65 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 1 Homo sapiens 178-186 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 1 Homo sapiens 188-193 29212253-1 2017 Ataxin-1 (ATXN1) is a coregulator protein within which expansion of the polyglutamine tract causes spinocerebellar ataxia type 1, an autosomal dominant neurodegenerative disorder. polyglutamine 72-85 ataxin 1 Homo sapiens 0-8 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 1 Homo sapiens 43-48 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 1 Homo sapiens 49-53 29533923-1 2018 Spinocerebellar ataxia type 1 (SCA1) is an adult-onset neurodegenerative disease caused by a polyglutamine expansion in the protein ATXN1, which is involved in transcriptional regulation. polyglutamine 93-106 ataxin 1 Homo sapiens 0-29 29533923-1 2018 Spinocerebellar ataxia type 1 (SCA1) is an adult-onset neurodegenerative disease caused by a polyglutamine expansion in the protein ATXN1, which is involved in transcriptional regulation. polyglutamine 93-106 ataxin 1 Homo sapiens 31-35 29533923-1 2018 Spinocerebellar ataxia type 1 (SCA1) is an adult-onset neurodegenerative disease caused by a polyglutamine expansion in the protein ATXN1, which is involved in transcriptional regulation. polyglutamine 93-106 ataxin 1 Homo sapiens 132-137 30108484-0 2018 PolyQ Tract Toxicity in SCA1 is Length Dependent in the Absence of CAG Repeat Interruption. polyglutamine 0-5 ataxin 1 Homo sapiens 24-28 30108484-1 2018 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by an expansion of a polyglutamine tract within the ATXN1 gene. polyglutamine 117-130 ataxin 1 Homo sapiens 0-29 30108484-1 2018 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by an expansion of a polyglutamine tract within the ATXN1 gene. polyglutamine 117-130 ataxin 1 Homo sapiens 31-35 30108484-1 2018 Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative disorder caused by an expansion of a polyglutamine tract within the ATXN1 gene. polyglutamine 117-130 ataxin 1 Homo sapiens 148-153 30108484-6 2018 In addition, the threshold of toxicity shifts to a shorter polyQ length with the increase of the lifespan in SCA1. polyglutamine 59-64 ataxin 1 Homo sapiens 109-113 29274668-0 2018 ATXN1 intermediate-length polyglutamine expansions are associated with amyotrophic lateral sclerosis. polyglutamine 26-39 ataxin 1 Homo sapiens 0-5 29274668-2 2018 We detected ATXN1 alleles with >=33 polyglutamine repeats in 105 of 1146 patients (9.16%) and 29 of 529 controls (5.48%) (p = 0.003). polyglutamine 36-49 ataxin 1 Homo sapiens 12-17 29274668-3 2018 The frequency of ATXN1 alleles with >=33 polyglutamine repeats was particularly high in the group of ALS patients carrying the C9orf72 expansion (12/59, 20.3%). polyglutamine 41-54 ataxin 1 Homo sapiens 17-22 29212253-1 2017 Ataxin-1 (ATXN1) is a coregulator protein within which expansion of the polyglutamine tract causes spinocerebellar ataxia type 1, an autosomal dominant neurodegenerative disorder. polyglutamine 72-85 ataxin 1 Homo sapiens 10-15 27895927-2 2016 The genetic mutation is an expansion of CAG trinucleotide repeats within the coding region of the ataxin-1 gene, characterizing SCA1 as a polyglutamine expansion disease like Huntington"s. polyglutamine 138-151 ataxin 1 Homo sapiens 128-132 27306906-1 2017 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (Q) repeat tract in the protein ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 0-29 27306906-1 2017 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (Q) repeat tract in the protein ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 31-35 27306906-1 2017 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (Q) repeat tract in the protein ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 164-172 27306906-1 2017 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (Q) repeat tract in the protein ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 174-179 27895927-2 2016 The genetic mutation is an expansion of CAG trinucleotide repeats within the coding region of the ataxin-1 gene, characterizing SCA1 as a polyglutamine expansion disease like Huntington"s. polyglutamine 138-151 ataxin 1 Homo sapiens 98-106 27895927-3 2016 As with most polyglutamine expansion diseases, SCA1 follows the rules of genetic anticipation: the larger the expansion, the earlier and more rapid the symptoms. polyglutamine 13-26 ataxin 1 Homo sapiens 47-51 27895927-4 2016 Unlike the majority of polyglutamine expansion diseases, the presence of histidine interruptions within the polyglutamine tract of ataxin-1 protein can prevent or mitigate disease. polyglutamine 23-36 ataxin 1 Homo sapiens 131-139 27895927-4 2016 Unlike the majority of polyglutamine expansion diseases, the presence of histidine interruptions within the polyglutamine tract of ataxin-1 protein can prevent or mitigate disease. polyglutamine 108-121 ataxin 1 Homo sapiens 131-139 27895927-5 2016 The present review aims to synthesize three decades of research on the ataxin-1 polyglutamine expansion mutation that causes SCA1. polyglutamine 80-93 ataxin 1 Homo sapiens 71-79 27895927-5 2016 The present review aims to synthesize three decades of research on the ataxin-1 polyglutamine expansion mutation that causes SCA1. polyglutamine 80-93 ataxin 1 Homo sapiens 125-129 27686464-1 2016 OBJECTIVE: Spinocerebellar ataxia type 1 is an autosomal dominant fatal neurodegenerative disease caused by a polyglutamine expansion in the coding region of ATXN1. polyglutamine 110-123 ataxin 1 Homo sapiens 158-163 27658206-0 2016 Polyglutamine Tract Expansion Increases S-Nitrosylation of Huntingtin and Ataxin-1. polyglutamine 0-13 ataxin 1 Homo sapiens 74-82 27168726-2 2015 The neurodegenerative disease spinocerebellar ataxia type 1 (SCA1) is caused by a coding polyglutamine expansion in the Ataxin-1 gene (ATXN1), which gives rise to the aggregation-prone mutant form of ATXN1 protein. polyglutamine 89-102 ataxin 1 Homo sapiens 30-59 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 0-29 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 31-35 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 149-157 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 159-164 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 133-138 ataxin 1 Homo sapiens 0-29 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 133-138 ataxin 1 Homo sapiens 31-35 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 133-138 ataxin 1 Homo sapiens 149-157 27058144-1 2016 Spinocerebellar ataxia type 1 (SCA1) is a dominantly inherited neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract in ataxin-1 (ATXN1). polyglutamine 133-138 ataxin 1 Homo sapiens 159-164 27058144-2 2016 The pathological hallmarks of SCA1 are the loss of cerebellar Purkinje cells and neurons in the brainstem and the presence of nuclear aggregates containing the polyQ-expanded ATXN1 protein. polyglutamine 160-165 ataxin 1 Homo sapiens 30-34 27058144-2 2016 The pathological hallmarks of SCA1 are the loss of cerebellar Purkinje cells and neurons in the brainstem and the presence of nuclear aggregates containing the polyQ-expanded ATXN1 protein. polyglutamine 160-165 ataxin 1 Homo sapiens 175-180 27058144-4 2016 This study was designed to examine the therapeutic effects of BIIB021, a purine-scaffold Hsp90 inhibitor, on the protein homeostasis of polyQ-expanded mutant ATXN1 in a cell culture model of SCA1. polyglutamine 136-141 ataxin 1 Homo sapiens 158-163 27058144-7 2016 These findings indicate that HSF1 is a key molecule in the regulation of the protein homeostasis of the polyQ-expanded mutant ATXN1 and that Hsp90 has potential as a novel therapeutic target in patients with SCA1. polyglutamine 104-109 ataxin 1 Homo sapiens 126-131 27168726-2 2015 The neurodegenerative disease spinocerebellar ataxia type 1 (SCA1) is caused by a coding polyglutamine expansion in the Ataxin-1 gene (ATXN1), which gives rise to the aggregation-prone mutant form of ATXN1 protein. polyglutamine 89-102 ataxin 1 Homo sapiens 61-65 27168726-2 2015 The neurodegenerative disease spinocerebellar ataxia type 1 (SCA1) is caused by a coding polyglutamine expansion in the Ataxin-1 gene (ATXN1), which gives rise to the aggregation-prone mutant form of ATXN1 protein. polyglutamine 89-102 ataxin 1 Homo sapiens 120-128 27168726-2 2015 The neurodegenerative disease spinocerebellar ataxia type 1 (SCA1) is caused by a coding polyglutamine expansion in the Ataxin-1 gene (ATXN1), which gives rise to the aggregation-prone mutant form of ATXN1 protein. polyglutamine 89-102 ataxin 1 Homo sapiens 135-140 27168726-2 2015 The neurodegenerative disease spinocerebellar ataxia type 1 (SCA1) is caused by a coding polyglutamine expansion in the Ataxin-1 gene (ATXN1), which gives rise to the aggregation-prone mutant form of ATXN1 protein. polyglutamine 89-102 ataxin 1 Homo sapiens 200-205 26879337-1 2016 Ataxin-1 is the protein responsible for the Spinocerebellar ataxia type 1, an incurable neurodegenerative disease caused by polyglutamine expansion. polyglutamine 124-137 ataxin 1 Homo sapiens 0-8 26748090-1 2016 Spinocerebellar ataxia type 1 (SCA1), due to the expansion of a polyglutamine repeat within the ubiquitously expressed Ataxin-1 protein, leads to the premature degeneration of Purkinje cells (PCs), the cause of which is poorly understood. polyglutamine 64-77 ataxin 1 Homo sapiens 119-127 24858692-1 2014 Spinocerebellar Ataxia Type1 (SCA1) is a dominantly inherited neurodegenerative disease and belongs to polyglutamine expansion disorders. polyglutamine 103-116 ataxin 1 Homo sapiens 0-28 25641559-1 2015 Spinocerebellar ataxia type 1 (SCA1), an autosomal-dominant neurodegenerative disorder, is caused by expansion of the polyglutamine tract within ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 0-29 25641559-1 2015 Spinocerebellar ataxia type 1 (SCA1), an autosomal-dominant neurodegenerative disorder, is caused by expansion of the polyglutamine tract within ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 31-35 25641559-1 2015 Spinocerebellar ataxia type 1 (SCA1), an autosomal-dominant neurodegenerative disorder, is caused by expansion of the polyglutamine tract within ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 145-153 25641559-1 2015 Spinocerebellar ataxia type 1 (SCA1), an autosomal-dominant neurodegenerative disorder, is caused by expansion of the polyglutamine tract within ataxin-1 (ATXN1). polyglutamine 118-131 ataxin 1 Homo sapiens 155-160 23853075-1 2014 Ataxin-1 is the protein responsible for the genetically-inherited neurodegenerative disease spinocerebellar ataxia type-1 linked to the expansion of a polyglutamine tract within the protein sequence. polyglutamine 151-164 ataxin 1 Homo sapiens 0-8 24858692-1 2014 Spinocerebellar Ataxia Type1 (SCA1) is a dominantly inherited neurodegenerative disease and belongs to polyglutamine expansion disorders. polyglutamine 103-116 ataxin 1 Homo sapiens 30-34 24858692-2 2014 The polyglutamine expansion in Ataxin-1 (ATXN1) is responsible for SCA1 pathology. polyglutamine 4-17 ataxin 1 Homo sapiens 31-39 24858692-2 2014 The polyglutamine expansion in Ataxin-1 (ATXN1) is responsible for SCA1 pathology. polyglutamine 4-17 ataxin 1 Homo sapiens 41-46 24858692-2 2014 The polyglutamine expansion in Ataxin-1 (ATXN1) is responsible for SCA1 pathology. polyglutamine 4-17 ataxin 1 Homo sapiens 67-71 24858692-4 2014 The wild-type ATXN1 dominantly forms a complex with CIC and the polyglutamine expanded form of ATXN1 favors to form a complex with RBM17. polyglutamine 64-77 ataxin 1 Homo sapiens 14-19 24858692-4 2014 The wild-type ATXN1 dominantly forms a complex with CIC and the polyglutamine expanded form of ATXN1 favors to form a complex with RBM17. polyglutamine 64-77 ataxin 1 Homo sapiens 95-100 24225362-2 2013 SCA1, 2, 3 and 6 are the four most common SCAs, all caused by expanded polyglutamine-coding CAG repeats. polyglutamine 71-84 ataxin 1 Homo sapiens 0-4 25309920-1 2014 The history of polyglutamine diseases dates back approximately 20 years to the discovery of a polyglutamine repeat in the androgen receptor of SBMA followed by the identification of similar expansion mutations in Huntington"s disease, SCA1, DRPLA, and the other spinocerebellar ataxias. polyglutamine 15-28 ataxin 1 Homo sapiens 235-239 24741770-2 2014 Studies have revealed that mutant huntingtin, polyglutamine-expanded ataxin-1 and ataxin-3 can cause elevated levels of reactive oxygen species in neuronal cells. polyglutamine 46-59 ataxin 1 Homo sapiens 69-77 24711972-4 2014 Identification of aggregation-prone regions other than polyglutamine could greatly help the development of SCA1 treatment more specific than that based on targeting the low complexity polyglutamine region. polyglutamine 184-197 ataxin 1 Homo sapiens 107-111 25131594-1 2014 PolyQ (polyglutamine) diseases such as HD (Huntington"s disease) or SCA1 (spinocerebellar ataxia type 1) are neurodegenerative disorders caused by abnormally elongated polyQ tracts in human proteins. polyglutamine 0-5 ataxin 1 Homo sapiens 68-72 25131594-1 2014 PolyQ (polyglutamine) diseases such as HD (Huntington"s disease) or SCA1 (spinocerebellar ataxia type 1) are neurodegenerative disorders caused by abnormally elongated polyQ tracts in human proteins. polyglutamine 0-5 ataxin 1 Homo sapiens 74-103 25131594-1 2014 PolyQ (polyglutamine) diseases such as HD (Huntington"s disease) or SCA1 (spinocerebellar ataxia type 1) are neurodegenerative disorders caused by abnormally elongated polyQ tracts in human proteins. polyglutamine 7-20 ataxin 1 Homo sapiens 68-72 25131594-1 2014 PolyQ (polyglutamine) diseases such as HD (Huntington"s disease) or SCA1 (spinocerebellar ataxia type 1) are neurodegenerative disorders caused by abnormally elongated polyQ tracts in human proteins. polyglutamine 7-20 ataxin 1 Homo sapiens 74-103 25131594-1 2014 PolyQ (polyglutamine) diseases such as HD (Huntington"s disease) or SCA1 (spinocerebellar ataxia type 1) are neurodegenerative disorders caused by abnormally elongated polyQ tracts in human proteins. polyglutamine 168-173 ataxin 1 Homo sapiens 68-72 25131594-1 2014 PolyQ (polyglutamine) diseases such as HD (Huntington"s disease) or SCA1 (spinocerebellar ataxia type 1) are neurodegenerative disorders caused by abnormally elongated polyQ tracts in human proteins. polyglutamine 168-173 ataxin 1 Homo sapiens 74-103 23760502-1 2013 Spinocerebellar ataxia type 1 is an autosomal dominant cerebellar ataxia associated with the expansion of a polyglutamine tract within the ataxin-1 (ATXN1) protein. polyglutamine 108-121 ataxin 1 Homo sapiens 139-147 23877406-3 2013 recently identified RAS-MAPK-MSK1 as a cellular pathway that modulates levels of the polyglutamine-containing protein ATXN1 and its subsequent toxicity in SCA1. polyglutamine 85-98 ataxin 1 Homo sapiens 118-123 23877406-3 2013 recently identified RAS-MAPK-MSK1 as a cellular pathway that modulates levels of the polyglutamine-containing protein ATXN1 and its subsequent toxicity in SCA1. polyglutamine 85-98 ataxin 1 Homo sapiens 155-159 23760502-1 2013 Spinocerebellar ataxia type 1 is an autosomal dominant cerebellar ataxia associated with the expansion of a polyglutamine tract within the ataxin-1 (ATXN1) protein. polyglutamine 108-121 ataxin 1 Homo sapiens 149-154 23754227-4 2013 In this chapter, we present a model of neurodegeneration in SCA1 initiated through phosphorylation at S776 by cAMP-dependent protein kinase (PKA) and enhanced by the presence of the polyglutamine expansion. polyglutamine 182-195 ataxin 1 Homo sapiens 60-64 23528090-2 2013 Essential for ataxin-1 aggregation is the anomalous expansion of a polyglutamine tract near the protein N-terminus, but the sequence-wise distant AXH domain modulates and contributes to the process. polyglutamine 67-80 ataxin 1 Homo sapiens 14-22 22309224-1 2012 AIMS: Spinocerebellar ataxia type 1 (SCA1) represents the first molecular genetically characterized autosomal dominantly inherited cerebellar ataxia and is assigned to the CAG-repeat or polyglutamine diseases. polyglutamine 186-199 ataxin 1 Homo sapiens 6-35 23935513-0 2013 The role of interruptions in polyQ in the pathology of SCA1. polyglutamine 29-34 ataxin 1 Homo sapiens 55-59 23935513-10 2013 Our study contributes to the understanding of the role of polyQ interruption in the SCA1 phenotype with regards to age at disease onset, prognosis and transmission. polyglutamine 58-63 ataxin 1 Homo sapiens 84-88 23022625-9 2012 We investigated 3 polyQ-containing proteins known to interact with PQBP-1: BRN-2, Huntingtin, and ATAXIN-1, and showed a diverse nature of protein-protein interaction in Vertebrata. polyglutamine 18-23 ataxin 1 Homo sapiens 98-106 23197749-3 2012 METHODS: We assessed the PolyQ lengths of ATXN-1 and ATXN-2 in 405 patients with sALS, 13 patients with fALS, and 296 unrelated controls without history of neurodegenerative disorders. polyglutamine 25-30 ataxin 1 Homo sapiens 42-48 23197749-4 2012 RESULTS: We found significantly higher intermediate PolyQ expansions >= 32 for ATXN-1 alleles and >= 28 for ATXN-2 alleles in the sALS cohort (ATXN-1: ALS, 7.07% vs controls, 2.38%; p = 0.0001; ATXN-2: ALS, 2.72% vs controls, 0.5%; p = 0.001). polyglutamine 52-57 ataxin 1 Homo sapiens 79-85 23197749-4 2012 RESULTS: We found significantly higher intermediate PolyQ expansions >= 32 for ATXN-1 alleles and >= 28 for ATXN-2 alleles in the sALS cohort (ATXN-1: ALS, 7.07% vs controls, 2.38%; p = 0.0001; ATXN-2: ALS, 2.72% vs controls, 0.5%; p = 0.001). polyglutamine 52-57 ataxin 1 Homo sapiens 143-149 22309224-1 2012 AIMS: Spinocerebellar ataxia type 1 (SCA1) represents the first molecular genetically characterized autosomal dominantly inherited cerebellar ataxia and is assigned to the CAG-repeat or polyglutamine diseases. polyglutamine 186-199 ataxin 1 Homo sapiens 37-41 22531670-1 2012 Spinocerebellar ataxia type 1 (SCA1) is one an intriguing set of nine neurodegenerative diseases caused by the expansion of a unstable trinucleotide CAG repeat where the repeat is located within the coding of the affected gene, i.e. the polyglutamine (polyQ) diseases. polyglutamine 237-250 ataxin 1 Homo sapiens 0-29 22531670-1 2012 Spinocerebellar ataxia type 1 (SCA1) is one an intriguing set of nine neurodegenerative diseases caused by the expansion of a unstable trinucleotide CAG repeat where the repeat is located within the coding of the affected gene, i.e. the polyglutamine (polyQ) diseases. polyglutamine 237-250 ataxin 1 Homo sapiens 31-35 22531670-1 2012 Spinocerebellar ataxia type 1 (SCA1) is one an intriguing set of nine neurodegenerative diseases caused by the expansion of a unstable trinucleotide CAG repeat where the repeat is located within the coding of the affected gene, i.e. the polyglutamine (polyQ) diseases. polyglutamine 252-257 ataxin 1 Homo sapiens 0-29 22531670-1 2012 Spinocerebellar ataxia type 1 (SCA1) is one an intriguing set of nine neurodegenerative diseases caused by the expansion of a unstable trinucleotide CAG repeat where the repeat is located within the coding of the affected gene, i.e. the polyglutamine (polyQ) diseases. polyglutamine 252-257 ataxin 1 Homo sapiens 31-35 22531670-5 2012 For SCA1 considerable evidence is accumulating that pathology is mediated by a polyQ-induced exaggeration of a native function of the host protein Ataxin-1 (ATXN1) and that phosphorylation of S776 regulates its interaction with other cellular protein and thereby function. polyglutamine 79-84 ataxin 1 Homo sapiens 4-8 22531670-5 2012 For SCA1 considerable evidence is accumulating that pathology is mediated by a polyQ-induced exaggeration of a native function of the host protein Ataxin-1 (ATXN1) and that phosphorylation of S776 regulates its interaction with other cellular protein and thereby function. polyglutamine 79-84 ataxin 1 Homo sapiens 147-155 22531670-5 2012 For SCA1 considerable evidence is accumulating that pathology is mediated by a polyQ-induced exaggeration of a native function of the host protein Ataxin-1 (ATXN1) and that phosphorylation of S776 regulates its interaction with other cellular protein and thereby function. polyglutamine 79-84 ataxin 1 Homo sapiens 157-162 22531670-6 2012 In addition, this posttranslational modification modulates toxicity of ATXN1 with an expanded polyglutamine. polyglutamine 94-107 ataxin 1 Homo sapiens 71-76 21964520-0 2012 Comparative genetics of the poly-Q tract of ataxin-1 and its binding protein PQBP-1. polyglutamine 28-34 ataxin 1 Homo sapiens 44-52 22511762-0 2012 Ataxin-1 poly(Q)-induced proteotoxic stress and apoptosis are attenuated in neural cells by docosahexaenoic acid-derived neuroprotectin D1. polyglutamine 9-16 ataxin 1 Homo sapiens 0-8 22491195-10 2012 CONCLUSIONS: Disease progressed faster in SCA s with polyglutamine expansions in SCA1, 2, and 3 than the other groups. polyglutamine 53-66 ataxin 1 Homo sapiens 81-85 22831947-3 2012 RESULTS: SCA1 and 7 are the most frequent types of polyglutamine SCA in the SA patient population, followed by SCA2, 3 and 6. polyglutamine 51-64 ataxin 1 Homo sapiens 9-13 21958864-2 2011 SCA1 is a trinucleotide repeat disorder in which the expanded polyglutamine mutation in the protein ataxin-1 primarily targets Purkinje cells of the cerebellum. polyglutamine 62-75 ataxin 1 Homo sapiens 0-4 22916034-2 2012 Here, we have identified 21 human proteins that influence polyQ-induced ataxin-1 misfolding and proteotoxicity in cell model systems. polyglutamine 58-63 ataxin 1 Homo sapiens 72-80 20451302-8 2011 Thus, the activation of miRNA expression in the aging brain may serve to reduce the cytotoxic effect of polyglutamine expanded ATXN1 and the deregulation of miRNA expression may be a risk factor for disease development. polyglutamine 104-117 ataxin 1 Homo sapiens 127-132 21827903-2 2012 SCA1, the first autosomal dominant cerebellar ataxia (ADCA) to be genetically characterized, is caused by the expansion of a CAG triplet repeat located in the N-terminal coding region of the disease-causing gene ATX1 located on chromosome 6p23: the mutation results in the production of a mutant protein, dubbed ataxin-1, with a longer-than-normal polyglutamine stretch. polyglutamine 348-361 ataxin 1 Homo sapiens 0-4 21827903-2 2012 SCA1, the first autosomal dominant cerebellar ataxia (ADCA) to be genetically characterized, is caused by the expansion of a CAG triplet repeat located in the N-terminal coding region of the disease-causing gene ATX1 located on chromosome 6p23: the mutation results in the production of a mutant protein, dubbed ataxin-1, with a longer-than-normal polyglutamine stretch. polyglutamine 348-361 ataxin 1 Homo sapiens 212-216 21958864-2 2011 SCA1 is a trinucleotide repeat disorder in which the expanded polyglutamine mutation in the protein ataxin-1 primarily targets Purkinje cells of the cerebellum. polyglutamine 62-75 ataxin 1 Homo sapiens 100-108 21835928-1 2011 Spinocerebellar ataxia type 1 (SCA1) is a lethal neurodegenerative disorder caused by expansion of a polyglutamine tract in ATXN1. polyglutamine 101-114 ataxin 1 Homo sapiens 0-29 22277448-5 2011 DNA damage repair is significantly impaired by interaction of mutant polyglutamine proteins with HMGB or Ku70, and the functional rescue of these molecules alleviated symptoms and pathologies of HD and SCA1. polyglutamine 69-82 ataxin 1 Homo sapiens 202-206 21835928-1 2011 Spinocerebellar ataxia type 1 (SCA1) is a lethal neurodegenerative disorder caused by expansion of a polyglutamine tract in ATXN1. polyglutamine 101-114 ataxin 1 Homo sapiens 31-35 21835928-1 2011 Spinocerebellar ataxia type 1 (SCA1) is a lethal neurodegenerative disorder caused by expansion of a polyglutamine tract in ATXN1. polyglutamine 101-114 ataxin 1 Homo sapiens 124-129 20155408-7 2010 This targeted binding of 14-3-3 protein to phosphorylated ataxin-1 to stabilize ataxin-1 in cellular models was corroborated by our double-labeling study for expanded polyglutamine and 14-3-3 proteins which demonstrated colocalization of these two epitopes in the neuronal nuclei in human autopsied brains with SCA1. polyglutamine 167-180 ataxin 1 Homo sapiens 58-66 21893199-1 2011 Ataxin-1 is part of a larger family of polyglutamine-containing proteins that is linked to nine distinct neurodegenerative disorders. polyglutamine 39-52 ataxin 1 Homo sapiens 0-8 20155408-7 2010 This targeted binding of 14-3-3 protein to phosphorylated ataxin-1 to stabilize ataxin-1 in cellular models was corroborated by our double-labeling study for expanded polyglutamine and 14-3-3 proteins which demonstrated colocalization of these two epitopes in the neuronal nuclei in human autopsied brains with SCA1. polyglutamine 167-180 ataxin 1 Homo sapiens 80-88 18461158-4 2008 We provide evidence that two unrelated proteins with expanded polyglutamine repeats induce p38MAPK in cultured cells, and demonstrate induction of p38MAPK in an in vivo model of neurodegeneration (spinocerebellar ataxia 1, or SCA-1). polyglutamine 62-75 ataxin 1 Homo sapiens 226-231 20304006-1 2010 Ataxin-1 is part of a larger family of polyglutamine-containing proteins that is linked to nine distinct neurodegenerative disorders. polyglutamine 39-52 ataxin 1 Homo sapiens 0-8 20030245-3 2009 These "polyglutamine disorders" are, SCA1, SCA2, Machado-Joseph disease, SCA6, SCA7, SCA17 and DRPLA. polyglutamine 7-20 ataxin 1 Homo sapiens 37-41 19541676-1 2009 Spinocerebellar ataxia type 1 (SCA1) is one of a group of nine expanded CAG repeat diseases, in which polyglutamine (polyQ) expansion above a threshold is associated with increased disease risk and aggregation. polyglutamine 102-115 ataxin 1 Homo sapiens 0-29 19541676-1 2009 Spinocerebellar ataxia type 1 (SCA1) is one of a group of nine expanded CAG repeat diseases, in which polyglutamine (polyQ) expansion above a threshold is associated with increased disease risk and aggregation. polyglutamine 102-115 ataxin 1 Homo sapiens 31-35 19541676-1 2009 Spinocerebellar ataxia type 1 (SCA1) is one of a group of nine expanded CAG repeat diseases, in which polyglutamine (polyQ) expansion above a threshold is associated with increased disease risk and aggregation. polyglutamine 117-122 ataxin 1 Homo sapiens 0-29 19541676-1 2009 Spinocerebellar ataxia type 1 (SCA1) is one of a group of nine expanded CAG repeat diseases, in which polyglutamine (polyQ) expansion above a threshold is associated with increased disease risk and aggregation. polyglutamine 117-122 ataxin 1 Homo sapiens 31-35 19541676-2 2009 SCA1 is unique in which the polyQ in the disease protein, ataxin1, often contains a few His residues that appear to block toxicity. polyglutamine 28-33 ataxin 1 Homo sapiens 0-4 19541676-2 2009 SCA1 is unique in which the polyQ in the disease protein, ataxin1, often contains a few His residues that appear to block toxicity. polyglutamine 28-33 ataxin 1 Homo sapiens 58-65 19572115-6 2009 Additional proteins have been identified, whose conformational alterations occurring through interactions with the polyglutamine tract itself or non-polyglutamine regions in ataxin-1 are the cause of SCA-1 cytotoxicity. polyglutamine 115-128 ataxin 1 Homo sapiens 174-182 19572115-6 2009 Additional proteins have been identified, whose conformational alterations occurring through interactions with the polyglutamine tract itself or non-polyglutamine regions in ataxin-1 are the cause of SCA-1 cytotoxicity. polyglutamine 149-162 ataxin 1 Homo sapiens 174-182 19208651-0 2009 The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1. polyglutamine 77-90 ataxin 1 Homo sapiens 100-108 19208651-11 2009 We therefore investigated the effects of siRNA-mediated sacsin knockdown on polyglutamine-expanded ataxin-1. polyglutamine 76-89 ataxin 1 Homo sapiens 99-107 18957430-0 2009 Pathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1. polyglutamine 27-40 ataxin 1 Homo sapiens 77-106 18957430-1 2009 Spinocerebellar ataxia type 1 (SCA1) is one of nine inherited neurodegenerative diseases caused by the expansion of a CAG trinucleotide repeat encoding a polyglutamine tract. polyglutamine 154-167 ataxin 1 Homo sapiens 0-29 18957430-1 2009 Spinocerebellar ataxia type 1 (SCA1) is one of nine inherited neurodegenerative diseases caused by the expansion of a CAG trinucleotide repeat encoding a polyglutamine tract. polyglutamine 154-167 ataxin 1 Homo sapiens 31-35 18957430-7 2009 Moreover, the finding that other ATXN1 interactions are decreased in disease suggests that the polyglutamine expansion contributes to disease by both a gain-of-function mechanism and partial loss of function. polyglutamine 95-108 ataxin 1 Homo sapiens 33-38 18758459-3 2008 Here we found that miR-19, miR-101 and miR-130 co-regulate ataxin1 levels and that their inhibition enhanced the cytotoxicity of polyglutamine-expanded ATXN1 in human cells. polyglutamine 129-142 ataxin 1 Homo sapiens 59-66 18758459-3 2008 Here we found that miR-19, miR-101 and miR-130 co-regulate ataxin1 levels and that their inhibition enhanced the cytotoxicity of polyglutamine-expanded ATXN1 in human cells. polyglutamine 129-142 ataxin 1 Homo sapiens 152-157 18519031-2 2008 SCA1 is caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 35-48 ataxin 1 Homo sapiens 0-4 18519031-2 2008 SCA1 is caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 35-48 ataxin 1 Homo sapiens 62-66 18519031-2 2008 SCA1 is caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 35-48 ataxin 1 Homo sapiens 81-89 20037628-1 2009 Ataxin-1 (Atx1), a member of the polyglutamine (polyQ) expanded protein family, is responsible for spinocerebellar ataxia type 1. polyglutamine 33-46 ataxin 1 Homo sapiens 0-8 20037628-1 2009 Ataxin-1 (Atx1), a member of the polyglutamine (polyQ) expanded protein family, is responsible for spinocerebellar ataxia type 1. polyglutamine 33-46 ataxin 1 Homo sapiens 10-14 20037628-1 2009 Ataxin-1 (Atx1), a member of the polyglutamine (polyQ) expanded protein family, is responsible for spinocerebellar ataxia type 1. polyglutamine 48-53 ataxin 1 Homo sapiens 0-8 20037628-1 2009 Ataxin-1 (Atx1), a member of the polyglutamine (polyQ) expanded protein family, is responsible for spinocerebellar ataxia type 1. polyglutamine 48-53 ataxin 1 Homo sapiens 10-14 19085187-2 2009 Expansion of the polyglutamine tract in ATXN1 causes the neurodegenerative disease, spinocerebellar ataxia type 1 (SCA1) with prominent cerebellar pathology. polyglutamine 17-30 ataxin 1 Homo sapiens 115-119 18337722-0 2008 Opposing effects of polyglutamine expansion on native protein complexes contribute to SCA1. polyglutamine 20-33 ataxin 1 Homo sapiens 86-90 18337722-5 2008 Concomitantly, polyglutamine expansion attenuates the formation and function of another protein complex containing ATXN1 and capicua, contributing to SCA1 through a partial loss-of-function mechanism. polyglutamine 15-28 ataxin 1 Homo sapiens 150-154 18337722-6 2008 This model provides mechanistic insight into the molecular pathogenesis of SCA1 as well as other polyglutamine diseases. polyglutamine 97-110 ataxin 1 Homo sapiens 75-79 18337722-4 2008 Polyglutamine expansion in ATXN1 favours the formation of a particular protein complex containing RBM17, contributing to SCA1 neuropathology by means of a gain-of-function mechanism. polyglutamine 0-13 ataxin 1 Homo sapiens 27-32 18337722-5 2008 Concomitantly, polyglutamine expansion attenuates the formation and function of another protein complex containing ATXN1 and capicua, contributing to SCA1 through a partial loss-of-function mechanism. polyglutamine 15-28 ataxin 1 Homo sapiens 115-120 18231590-0 2008 Polyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation. polyglutamine 0-13 ataxin 1 Homo sapiens 52-60 18231590-5 2008 Instead of being static, insoluble aggregates, nuclear accumulations formed by the polyQ-expanded ataxin-1 showed enhanced intracellular kinetics as compared to wild-type ataxin-1. polyglutamine 83-88 ataxin 1 Homo sapiens 98-106 18231590-5 2008 Instead of being static, insoluble aggregates, nuclear accumulations formed by the polyQ-expanded ataxin-1 showed enhanced intracellular kinetics as compared to wild-type ataxin-1. polyglutamine 83-88 ataxin 1 Homo sapiens 171-179 18231590-8 2008 CONCLUSIONS/SIGNIFICANCE: These results indicate that polyQ expansion does not necessarily lead to aggregate formation, and that the enhanced kinetics may affect the nuclear function of ataxin-1. polyglutamine 54-59 ataxin 1 Homo sapiens 186-194 18231590-9 2008 The unexpected findings for a polyQ-expanded protein and their consequences for ongoing SCA1 research are discussed. polyglutamine 30-35 ataxin 1 Homo sapiens 88-92 18231590-3 2008 The polyQ disorder SpinoCerebellar Ataxia 1 (SCA1) is caused by a polyQ-expansion in the ataxin-1 protein, which is thought to lead to nuclear aggregates. polyglutamine 4-9 ataxin 1 Homo sapiens 89-97 18231590-4 2008 METHODOLOGY/PRINCIPAL FINDINGS: Using advanced live cell fluorescence microscopy and a filter retardation assay we show that nuclear accumulations formed by polyQ-expanded ataxin-1 do not resemble aggregates of other polyQ-expanded proteins. polyglutamine 157-162 ataxin 1 Homo sapiens 172-180 18301861-1 2008 Spinocerebellar ataxia type 1 (SCA1; OMIM: #164400) is an autosomal dominant cerebellar ataxia caused by an expansion of CAG repeat, which encodes polyglutamine, in the ataxin-1 (ATXN1) gene. polyglutamine 147-160 ataxin 1 Homo sapiens 0-29 18418661-2 2008 SCA1 is caused by the toxic effects triggered by an expanded polyglutamine (polyQ) within the protein ataxin 1 (Atxn1) resulting in variable degrees of neurodegeneration in the cerebellum, brainstem, and spinocerebellar tracts. polyglutamine 61-74 ataxin 1 Homo sapiens 0-4 18418661-2 2008 SCA1 is caused by the toxic effects triggered by an expanded polyglutamine (polyQ) within the protein ataxin 1 (Atxn1) resulting in variable degrees of neurodegeneration in the cerebellum, brainstem, and spinocerebellar tracts. polyglutamine 61-74 ataxin 1 Homo sapiens 102-110 18418661-2 2008 SCA1 is caused by the toxic effects triggered by an expanded polyglutamine (polyQ) within the protein ataxin 1 (Atxn1) resulting in variable degrees of neurodegeneration in the cerebellum, brainstem, and spinocerebellar tracts. polyglutamine 61-74 ataxin 1 Homo sapiens 112-117 18418661-2 2008 SCA1 is caused by the toxic effects triggered by an expanded polyglutamine (polyQ) within the protein ataxin 1 (Atxn1) resulting in variable degrees of neurodegeneration in the cerebellum, brainstem, and spinocerebellar tracts. polyglutamine 76-81 ataxin 1 Homo sapiens 0-4 18418661-2 2008 SCA1 is caused by the toxic effects triggered by an expanded polyglutamine (polyQ) within the protein ataxin 1 (Atxn1) resulting in variable degrees of neurodegeneration in the cerebellum, brainstem, and spinocerebellar tracts. polyglutamine 76-81 ataxin 1 Homo sapiens 102-110 18418661-2 2008 SCA1 is caused by the toxic effects triggered by an expanded polyglutamine (polyQ) within the protein ataxin 1 (Atxn1) resulting in variable degrees of neurodegeneration in the cerebellum, brainstem, and spinocerebellar tracts. polyglutamine 76-81 ataxin 1 Homo sapiens 112-117 18418679-4 2008 The more common SCAs, SCA1, 2, 3 and 6 are due to translated CAG repeat expansions that code for an elongated polyglutamine tract within the respective proteins. polyglutamine 110-123 ataxin 1 Homo sapiens 22-26 19044200-1 2008 Spinocerebellar ataxia type 1 (SCA1) is a dominant inherited disease caused by expanded trinucleotide repeats resulting in an increased polyglutamine tract in the gene product. polyglutamine 136-149 ataxin 1 Homo sapiens 0-29 19044200-1 2008 Spinocerebellar ataxia type 1 (SCA1) is a dominant inherited disease caused by expanded trinucleotide repeats resulting in an increased polyglutamine tract in the gene product. polyglutamine 136-149 ataxin 1 Homo sapiens 31-35 18301861-1 2008 Spinocerebellar ataxia type 1 (SCA1; OMIM: #164400) is an autosomal dominant cerebellar ataxia caused by an expansion of CAG repeat, which encodes polyglutamine, in the ataxin-1 (ATXN1) gene. polyglutamine 147-160 ataxin 1 Homo sapiens 31-35 18301861-1 2008 Spinocerebellar ataxia type 1 (SCA1; OMIM: #164400) is an autosomal dominant cerebellar ataxia caused by an expansion of CAG repeat, which encodes polyglutamine, in the ataxin-1 (ATXN1) gene. polyglutamine 147-160 ataxin 1 Homo sapiens 169-177 18301861-1 2008 Spinocerebellar ataxia type 1 (SCA1; OMIM: #164400) is an autosomal dominant cerebellar ataxia caused by an expansion of CAG repeat, which encodes polyglutamine, in the ataxin-1 (ATXN1) gene. polyglutamine 147-160 ataxin 1 Homo sapiens 179-184 18301861-2 2008 Length of polyglutamine in the ATXN1 protein is the critical determinant of pathogenesis of this disease. polyglutamine 10-23 ataxin 1 Homo sapiens 31-36 17190592-2 2006 In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion. polyglutamine 44-57 ataxin 1 Homo sapiens 66-74 17127076-3 2007 Interestingly CHIP associates not only with the polyQ-expanded ataxin-1 but also with the normal ataxin-1. polyglutamine 48-53 ataxin 1 Homo sapiens 63-71 17127076-4 2007 Moreover, by enhancing ataxin-1 ubiquitylation, CHIP over-expression leads to a reduction in the solubility of ataxin-1 and thus increases the aggregate formation, especially that of polyQ-expanded ataxin-1. polyglutamine 183-188 ataxin 1 Homo sapiens 23-31 17540008-2 2007 The mutation causing SCA1 is an expansion in the polyglutamine tract of the ATXN1 protein. polyglutamine 49-62 ataxin 1 Homo sapiens 21-25 17540008-2 2007 The mutation causing SCA1 is an expansion in the polyglutamine tract of the ATXN1 protein. polyglutamine 49-62 ataxin 1 Homo sapiens 76-81 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 1 Homo sapiens 66-74 17442486-1 2007 Spinocerebellar ataxia-1 (SCA1) is caused by the expansion of a polyglutamine repeats within the disease protein, ataxin-1. polyglutamine 64-77 ataxin 1 Homo sapiens 0-24 17442486-1 2007 Spinocerebellar ataxia-1 (SCA1) is caused by the expansion of a polyglutamine repeats within the disease protein, ataxin-1. polyglutamine 64-77 ataxin 1 Homo sapiens 26-30 17442486-1 2007 Spinocerebellar ataxia-1 (SCA1) is caused by the expansion of a polyglutamine repeats within the disease protein, ataxin-1. polyglutamine 64-77 ataxin 1 Homo sapiens 114-122 16277991-0 2005 Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein. polyglutamine 0-13 ataxin 1 Homo sapiens 71-79 15824120-7 2005 There was a decrease in ataxin-1 SUMOylation in the presence of the expanded polyglutamine tract, ataxin-1[82Q]. polyglutamine 77-90 ataxin 1 Homo sapiens 24-32 16122429-4 2005 Overexpression of hAtx-1 in fruit flies produces phenotypes similar to those of dAtx-1 but different from the polyglutamine peptide alone. polyglutamine 110-123 ataxin 1 Homo sapiens 18-24 15824120-7 2005 There was a decrease in ataxin-1 SUMOylation in the presence of the expanded polyglutamine tract, ataxin-1[82Q]. polyglutamine 77-90 ataxin 1 Homo sapiens 98-106 15615787-1 2005 Spinocerebellar ataxia type 1 (SCA1) is a dominant neurodegenerative disease caused by the expression of mutant ataxin-1 containing an expanded polyglutamine tract. polyglutamine 144-157 ataxin 1 Homo sapiens 0-29 15750336-0 2005 Proteasome function is inhibited by polyglutamine-expanded ataxin-1, the SCA1 gene product. polyglutamine 36-49 ataxin 1 Homo sapiens 59-67 15750336-0 2005 Proteasome function is inhibited by polyglutamine-expanded ataxin-1, the SCA1 gene product. polyglutamine 36-49 ataxin 1 Homo sapiens 73-77 15750336-1 2005 Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 116-129 ataxin 1 Homo sapiens 0-29 15750336-1 2005 Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 116-129 ataxin 1 Homo sapiens 31-35 15750336-1 2005 Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 116-129 ataxin 1 Homo sapiens 143-147 15750336-1 2005 Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder caused by expansion of the polyglutamine tract in the SCA1 gene product, ataxin-1. polyglutamine 116-129 ataxin 1 Homo sapiens 162-170 15750336-2 2005 Using d2EGFP, a short-lived enhanced green fluorescent protein, we investigated whether polyglutamine-expanded ataxin-1 affects the function of the proteasome, a cellular multicatalytic protease that degrades most misfolded proteins and regulatory proteins. polyglutamine 88-101 ataxin 1 Homo sapiens 111-119 15750336-6 2005 Furthermore, d2EGFP localization experiments showed that polyglutamine-expanded ataxin-1 inhibited the general function of the proteasome activity. polyglutamine 57-70 ataxin 1 Homo sapiens 80-88 15750336-7 2005 Taken together, these results demonstrate that polyglutamine-expanded ataxin-1 decreases the activity of the proteasome, implying that a disturbance in the ubiquitin-proteasome pathway is directly involved in the development of spinocerebellar ataxia type1. polyglutamine 47-60 ataxin 1 Homo sapiens 70-78 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 1 Homo sapiens 77-82 17132942-2 2005 The majority of these diseases result from expanded polyglutamine tracts in the encoded protein as seen in SCA1, SCA2, SCA3, SCA6, SCA7 and Dentatorubral-Pallidoluysian Atrophy (DRPLA). polyglutamine 52-65 ataxin 1 Homo sapiens 107-111 15615787-1 2005 Spinocerebellar ataxia type 1 (SCA1) is a dominant neurodegenerative disease caused by the expression of mutant ataxin-1 containing an expanded polyglutamine tract. polyglutamine 144-157 ataxin 1 Homo sapiens 112-120 15615787-2 2005 Ataxin-1 is a nuclear protein that localizes to punctate inclusions similar to neuronal nuclear inclusions seen in many polyglutamine expansion disease proteins. polyglutamine 120-133 ataxin 1 Homo sapiens 0-8 14583607-2 2004 This results in the lengthening of a polyglutamine tract in the gene product ataxin-1. polyglutamine 37-50 ataxin 1 Homo sapiens 77-85 12717018-0 2003 Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: A molecular approach. polyglutamine 78-91 ataxin 1 Homo sapiens 105-109 12893274-0 2003 Polyglutamine-expanded ataxin-1 recruits Cu/Zn-superoxide dismutase into the nucleus of HeLa cells. polyglutamine 0-13 ataxin 1 Homo sapiens 23-31 12893274-1 2003 Spinocerebellar ataxia 1 (SCA1) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in ataxin-1, the SCA1 gene product. polyglutamine 102-115 ataxin 1 Homo sapiens 0-24 12893274-1 2003 Spinocerebellar ataxia 1 (SCA1) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in ataxin-1, the SCA1 gene product. polyglutamine 102-115 ataxin 1 Homo sapiens 26-30 12893274-1 2003 Spinocerebellar ataxia 1 (SCA1) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in ataxin-1, the SCA1 gene product. polyglutamine 102-115 ataxin 1 Homo sapiens 127-135 12893274-1 2003 Spinocerebellar ataxia 1 (SCA1) is an inherited neurodegenerative disorder caused by expansion of the polyglutamine stretch in ataxin-1, the SCA1 gene product. polyglutamine 102-115 ataxin 1 Homo sapiens 141-145 12893274-2 2003 Polyglutamine expansion leads to the aggregation of ataxin-1 proteins. polyglutamine 0-13 ataxin 1 Homo sapiens 52-60 12893274-7 2003 Our results suggest that polyglutamine-expanded ataxin-1 increases the levels of reactive oxygen species in HeLa cells. polyglutamine 25-38 ataxin 1 Homo sapiens 48-56 12717018-3 2003 In one such disorder, spinocerebellar ataxia (SCA1), it has been reported that certain individuals with expanded polyglutamine repeats in the disease range (Q(12)HQHQ(12)HQHQ(14/15)) but with histidine interruptions were found to be phenotypically normal. polyglutamine 113-126 ataxin 1 Homo sapiens 46-50 12717018-7 2003 The study strengthens our earlier hypothesis of the importance of histidine interruptions in mitigating the pathogenicity of expanded polyglutamine tract at the SCA1 locus. polyglutamine 134-147 ataxin 1 Homo sapiens 161-165 12360291-4 2002 Here, we used fluorescence recovery after photobleaching (FRAP) to examine the intranuclear dynamics of polyglutamine-expanded ataxin1 and inclusion-associated proteins. polyglutamine 104-117 ataxin 1 Homo sapiens 127-134 12062018-2 2002 In this study, using in vitro and in vivo assays, we show that the association between ataxin-1 and PQBP-1 is positively influenced by expanded polyglutamine sequences. polyglutamine 144-157 ataxin 1 Homo sapiens 87-95 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 1 Homo sapiens 346-351 10624951-1 1999 Mutant ataxin-1, the expanded polyglutamine protein causing spinocerebellar ataxia type 1 (SCA1), aggregates in ubiquitin-positive nuclear inclusions (NI) that alter proteasome distribution in affected SCA1 patient neurons. polyglutamine 30-43 ataxin 1 Homo sapiens 7-15 11001934-1 2000 Expansion of a polyglutamine tract within ataxin-1 causes spinocerebellar ataxia type 1 (SCA1). polyglutamine 15-28 ataxin 1 Homo sapiens 42-50 11001934-1 2000 Expansion of a polyglutamine tract within ataxin-1 causes spinocerebellar ataxia type 1 (SCA1). polyglutamine 15-28 ataxin 1 Homo sapiens 58-87 11001934-1 2000 Expansion of a polyglutamine tract within ataxin-1 causes spinocerebellar ataxia type 1 (SCA1). polyglutamine 15-28 ataxin 1 Homo sapiens 89-93 10970064-5 2000 The mutations that cause SCA1, SCA2, SCA3, SCA6 and SCA7 share the common feature of an expanded CAG sequence, encoding an abnormally long polyglutamine tract within the respective gene products. polyglutamine 139-152 ataxin 1 Homo sapiens 25-29 10928291-2 2000 At least nine disorders result from a CAG trinucleotide repeat expansion which is translated into a polyglutamine stretch in the respective proteins: Huntington"s disease (HD), dentatorubral pallidolysian atrophy (DRPLA), spinal bulbar muscular atrophy (SBMA), and several of the spinocerebellar ataxias (SCA1, 2, 3, 6, 7 and 12). polyglutamine 100-113 ataxin 1 Homo sapiens 305-309 11081516-2 2000 Spinocerebellar ataxia type 1 (SCA1) is one such disease-caused by expansion of a polyglutamine tract in the protein ataxin-1. polyglutamine 82-95 ataxin 1 Homo sapiens 0-29 11081516-2 2000 Spinocerebellar ataxia type 1 (SCA1) is one such disease-caused by expansion of a polyglutamine tract in the protein ataxin-1. polyglutamine 82-95 ataxin 1 Homo sapiens 31-35 11081516-2 2000 Spinocerebellar ataxia type 1 (SCA1) is one such disease-caused by expansion of a polyglutamine tract in the protein ataxin-1. polyglutamine 82-95 ataxin 1 Homo sapiens 117-125 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 1 Homo sapiens 38-42 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 1 Homo sapiens 66-70 10649571-0 2000 Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1. polyglutamine 0-13 ataxin 1 Homo sapiens 92-96 10624951-1 1999 Mutant ataxin-1, the expanded polyglutamine protein causing spinocerebellar ataxia type 1 (SCA1), aggregates in ubiquitin-positive nuclear inclusions (NI) that alter proteasome distribution in affected SCA1 patient neurons. polyglutamine 30-43 ataxin 1 Homo sapiens 60-89 10624951-1 1999 Mutant ataxin-1, the expanded polyglutamine protein causing spinocerebellar ataxia type 1 (SCA1), aggregates in ubiquitin-positive nuclear inclusions (NI) that alter proteasome distribution in affected SCA1 patient neurons. polyglutamine 30-43 ataxin 1 Homo sapiens 91-95 10066385-0 1999 Pathogenesis of polyglutamine-induced disease: A model for SCA1. polyglutamine 16-29 ataxin 1 Homo sapiens 59-63