PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25902068-9 2015 This interaction was impaired when ATXN2 harbored an expanded polyglutamine. polyglutamine 62-75 ataxin 2 Mus musculus 35-40 32932600-1 2020 Spinocerebellar ataxia type 2 (SCA2) is caused by polyglutamine expansion in Ataxin-2 (ATXN2). polyglutamine 50-63 ataxin 2 Mus musculus 0-29 32932600-1 2020 Spinocerebellar ataxia type 2 (SCA2) is caused by polyglutamine expansion in Ataxin-2 (ATXN2). polyglutamine 50-63 ataxin 2 Mus musculus 31-35 32932600-1 2020 Spinocerebellar ataxia type 2 (SCA2) is caused by polyglutamine expansion in Ataxin-2 (ATXN2). polyglutamine 50-63 ataxin 2 Mus musculus 77-85 32932600-1 2020 Spinocerebellar ataxia type 2 (SCA2) is caused by polyglutamine expansion in Ataxin-2 (ATXN2). polyglutamine 50-63 ataxin 2 Mus musculus 87-92 32307524-5 2020 SC transcriptomes were determined using an SCA2 bacterial artificial chromosome (BAC) mouse model expressing polyglutamine expanded ATXN2. polyglutamine 109-122 ataxin 2 Mus musculus 132-137 30194296-5 2018 Reduction of Stau1 in vivo improved motor behavior in an SCA2 mouse model, normalized the levels of several SCA2-related proteins, and reduced aggregation of polyglutamine-expanded ATXN2. polyglutamine 158-171 ataxin 2 Mus musculus 181-186 28525545-2 2017 The repeat resides in an encoded region of the gene resulting in polyglutamine (polyQ) expansion which has been assumed to result in gain of function, predominantly, for the ATXN2 protein. polyglutamine 65-78 ataxin 2 Mus musculus 174-179 28525545-2 2017 The repeat resides in an encoded region of the gene resulting in polyglutamine (polyQ) expansion which has been assumed to result in gain of function, predominantly, for the ATXN2 protein. polyglutamine 80-85 ataxin 2 Mus musculus 174-179 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 199-212 ataxin 2 Mus musculus 0-29 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 199-212 ataxin 2 Mus musculus 31-35 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 199-212 ataxin 2 Mus musculus 172-176 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 199-212 ataxin 2 Mus musculus 241-249 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 199-212 ataxin 2 Mus musculus 251-256 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 214-219 ataxin 2 Mus musculus 0-29 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 214-219 ataxin 2 Mus musculus 31-35 25721894-1 2015 Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). polyglutamine 214-219 ataxin 2 Mus musculus 172-176 33577922-1 2021 Large polyglutamine expansions in Ataxin-2 (ATXN2) cause multi-system nervous atrophy in Spinocerebellar Ataxia type 2 (SCA2). polyglutamine 6-19 ataxin 2 Mus musculus 34-42 33577922-1 2021 Large polyglutamine expansions in Ataxin-2 (ATXN2) cause multi-system nervous atrophy in Spinocerebellar Ataxia type 2 (SCA2). polyglutamine 6-19 ataxin 2 Mus musculus 44-49 33577922-1 2021 Large polyglutamine expansions in Ataxin-2 (ATXN2) cause multi-system nervous atrophy in Spinocerebellar Ataxia type 2 (SCA2). polyglutamine 6-19 ataxin 2 Mus musculus 120-124 31766565-3 2019 Conversely, the progressive ATXN2 gain of function due to the fact of polyglutamine (polyQ) expansions leads to a dominantly inherited neurodegenerative process named spinocerebellar ataxia type 2 (SCA2) with early adipose tissue loss and late muscle atrophy. polyglutamine 70-83 ataxin 2 Mus musculus 28-33 31766565-3 2019 Conversely, the progressive ATXN2 gain of function due to the fact of polyglutamine (polyQ) expansions leads to a dominantly inherited neurodegenerative process named spinocerebellar ataxia type 2 (SCA2) with early adipose tissue loss and late muscle atrophy. polyglutamine 70-83 ataxin 2 Mus musculus 167-196 31766565-3 2019 Conversely, the progressive ATXN2 gain of function due to the fact of polyglutamine (polyQ) expansions leads to a dominantly inherited neurodegenerative process named spinocerebellar ataxia type 2 (SCA2) with early adipose tissue loss and late muscle atrophy. polyglutamine 70-83 ataxin 2 Mus musculus 198-202 31766565-3 2019 Conversely, the progressive ATXN2 gain of function due to the fact of polyglutamine (polyQ) expansions leads to a dominantly inherited neurodegenerative process named spinocerebellar ataxia type 2 (SCA2) with early adipose tissue loss and late muscle atrophy. polyglutamine 85-90 ataxin 2 Mus musculus 28-33 31766565-3 2019 Conversely, the progressive ATXN2 gain of function due to the fact of polyglutamine (polyQ) expansions leads to a dominantly inherited neurodegenerative process named spinocerebellar ataxia type 2 (SCA2) with early adipose tissue loss and late muscle atrophy. polyglutamine 85-90 ataxin 2 Mus musculus 167-196 31766565-3 2019 Conversely, the progressive ATXN2 gain of function due to the fact of polyglutamine (polyQ) expansions leads to a dominantly inherited neurodegenerative process named spinocerebellar ataxia type 2 (SCA2) with early adipose tissue loss and late muscle atrophy. polyglutamine 85-90 ataxin 2 Mus musculus 198-202 28405022-9 2017 A decrease in ataxin-2 suppresses TDP-43 toxicity in yeast and flies, and intermediate-length polyglutamine expansions in the ataxin-2 gene increase risk of ALS. polyglutamine 94-107 ataxin 2 Mus musculus 126-134 26868665-2 2017 The expansion of a polyglutamine (polyQ) domain in the RNA-binding protein ataxin-2 (ATXN2) is responsible for this disease, but the causal roles of deficient ATXN2 functions versus aggregation toxicity are still under debate. polyglutamine 19-32 ataxin 2 Mus musculus 75-83 26868665-2 2017 The expansion of a polyglutamine (polyQ) domain in the RNA-binding protein ataxin-2 (ATXN2) is responsible for this disease, but the causal roles of deficient ATXN2 functions versus aggregation toxicity are still under debate. polyglutamine 19-32 ataxin 2 Mus musculus 85-90 26868665-2 2017 The expansion of a polyglutamine (polyQ) domain in the RNA-binding protein ataxin-2 (ATXN2) is responsible for this disease, but the causal roles of deficient ATXN2 functions versus aggregation toxicity are still under debate. polyglutamine 34-39 ataxin 2 Mus musculus 75-83 26868665-2 2017 The expansion of a polyglutamine (polyQ) domain in the RNA-binding protein ataxin-2 (ATXN2) is responsible for this disease, but the causal roles of deficient ATXN2 functions versus aggregation toxicity are still under debate. polyglutamine 34-39 ataxin 2 Mus musculus 85-90 23102227-1 2012 Spinocerebellar ataxia type 2 (SCA2) is a neurodegenerative disorder caused by a polyglutamine expansion within the Ataxin-2 (Atxn2) protein. polyglutamine 81-94 ataxin 2 Mus musculus 0-29 23087021-1 2013 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited disorder, which is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the ATXN2 gene. polyglutamine 133-146 ataxin 2 Mus musculus 0-29 23087021-1 2013 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited disorder, which is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the ATXN2 gene. polyglutamine 133-146 ataxin 2 Mus musculus 31-35 23087021-1 2013 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited disorder, which is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the ATXN2 gene. polyglutamine 133-146 ataxin 2 Mus musculus 189-194 23087021-1 2013 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited disorder, which is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the ATXN2 gene. polyglutamine 148-153 ataxin 2 Mus musculus 0-29 23087021-1 2013 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited disorder, which is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the ATXN2 gene. polyglutamine 148-153 ataxin 2 Mus musculus 31-35 23087021-1 2013 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited disorder, which is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the ATXN2 gene. polyglutamine 148-153 ataxin 2 Mus musculus 189-194 22914732-5 2012 As SCA2 is likely caused by a gain-of-toxic or gain-of-normal function like other polyglutamine disorders, targeting ATXN2 expression may represent a valid therapeutic approach. polyglutamine 82-95 ataxin 2 Mus musculus 3-7 25790475-0 2015 Both ubiquitin ligases FBXW8 and PARK2 are sequestrated into insolubility by ATXN2 PolyQ expansions, but only FBXW8 expression is dysregulated. polyglutamine 83-88 ataxin 2 Mus musculus 77-82 25790475-2 2015 The single RING finger type E3 ubiquitin-protein ligase PARK2 is mutated in a Parkinson"s disease (PD) variant and was found to interact with ATXN2, a protein where polyglutamine expansions cause Spinocerebellar ataxia type 2 (SCA2) or increase the risk for Levodopa-responsive PD and for the motor neuron disease Amyotrophic lateral sclerosis (ALS). polyglutamine 165-178 ataxin 2 Mus musculus 142-147 25790475-2 2015 The single RING finger type E3 ubiquitin-protein ligase PARK2 is mutated in a Parkinson"s disease (PD) variant and was found to interact with ATXN2, a protein where polyglutamine expansions cause Spinocerebellar ataxia type 2 (SCA2) or increase the risk for Levodopa-responsive PD and for the motor neuron disease Amyotrophic lateral sclerosis (ALS). polyglutamine 165-178 ataxin 2 Mus musculus 196-225 25790475-2 2015 The single RING finger type E3 ubiquitin-protein ligase PARK2 is mutated in a Parkinson"s disease (PD) variant and was found to interact with ATXN2, a protein where polyglutamine expansions cause Spinocerebellar ataxia type 2 (SCA2) or increase the risk for Levodopa-responsive PD and for the motor neuron disease Amyotrophic lateral sclerosis (ALS). polyglutamine 165-178 ataxin 2 Mus musculus 227-231 22914732-5 2012 As SCA2 is likely caused by a gain-of-toxic or gain-of-normal function like other polyglutamine disorders, targeting ATXN2 expression may represent a valid therapeutic approach. polyglutamine 82-95 ataxin 2 Mus musculus 117-122 23102227-1 2012 Spinocerebellar ataxia type 2 (SCA2) is a neurodegenerative disorder caused by a polyglutamine expansion within the Ataxin-2 (Atxn2) protein. polyglutamine 81-94 ataxin 2 Mus musculus 31-35 23102227-1 2012 Spinocerebellar ataxia type 2 (SCA2) is a neurodegenerative disorder caused by a polyglutamine expansion within the Ataxin-2 (Atxn2) protein. polyglutamine 81-94 ataxin 2 Mus musculus 116-124 23102227-1 2012 Spinocerebellar ataxia type 2 (SCA2) is a neurodegenerative disorder caused by a polyglutamine expansion within the Ataxin-2 (Atxn2) protein. polyglutamine 81-94 ataxin 2 Mus musculus 126-131 19625506-1 2009 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited, neurodegenerative disease caused by an expansion of polyglutamine tracts in the cytosolic protein ataxin-2 (Atx2). polyglutamine 127-140 ataxin 2 Mus musculus 0-29 22973002-2 2012 SCA2 results from a poly(Q) (polyglutamine) expansion in the cytosolic protein ataxin-2 (Atx2). polyglutamine 20-27 ataxin 2 Mus musculus 0-4 22973002-2 2012 SCA2 results from a poly(Q) (polyglutamine) expansion in the cytosolic protein ataxin-2 (Atx2). polyglutamine 20-27 ataxin 2 Mus musculus 79-87 22973002-2 2012 SCA2 results from a poly(Q) (polyglutamine) expansion in the cytosolic protein ataxin-2 (Atx2). polyglutamine 20-27 ataxin 2 Mus musculus 89-93 22973002-2 2012 SCA2 results from a poly(Q) (polyglutamine) expansion in the cytosolic protein ataxin-2 (Atx2). polyglutamine 29-42 ataxin 2 Mus musculus 0-4 22973002-2 2012 SCA2 results from a poly(Q) (polyglutamine) expansion in the cytosolic protein ataxin-2 (Atx2). polyglutamine 29-42 ataxin 2 Mus musculus 79-87 22973002-2 2012 SCA2 results from a poly(Q) (polyglutamine) expansion in the cytosolic protein ataxin-2 (Atx2). polyglutamine 29-42 ataxin 2 Mus musculus 89-93 21824437-5 2011 METHOD: Transgenic mice bearing poly-glutamine mutation in ataxin-2 gene (C57BL/6J SCA2 transgenic mice) were serially transplanted with hMSCs intravenously or intracranially before and after the onset of motor function loss. polyglutamine 32-46 ataxin 2 Mus musculus 59-67 19625506-1 2009 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited, neurodegenerative disease caused by an expansion of polyglutamine tracts in the cytosolic protein ataxin-2 (Atx2). polyglutamine 127-140 ataxin 2 Mus musculus 31-35 19625506-1 2009 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited, neurodegenerative disease caused by an expansion of polyglutamine tracts in the cytosolic protein ataxin-2 (Atx2). polyglutamine 127-140 ataxin 2 Mus musculus 173-181 19625506-1 2009 Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominantly inherited, neurodegenerative disease caused by an expansion of polyglutamine tracts in the cytosolic protein ataxin-2 (Atx2). polyglutamine 127-140 ataxin 2 Mus musculus 183-187 18250099-2 2008 Expansion of the normal polyglutamine tract in the protein leads to the neurodegenerative disorder Spino-Cerebellar Ataxia type 2 (SCA2). polyglutamine 24-37 ataxin 2 Mus musculus 131-135 18602463-1 2008 Ataxin-2 is a novel protein, where the unstable expansion of an internal polyglutamine domain can cause the neurodegenerative disease Spinocerebellar Ataxia type 2 (SCA2). polyglutamine 73-86 ataxin 2 Mus musculus 0-8 18602463-1 2008 Ataxin-2 is a novel protein, where the unstable expansion of an internal polyglutamine domain can cause the neurodegenerative disease Spinocerebellar Ataxia type 2 (SCA2). polyglutamine 73-86 ataxin 2 Mus musculus 165-169 17949716-0 2007 Ataxin-2 mediated cell death is dependent on domains downstream of the polyQ repeat. polyglutamine 71-76 ataxin 2 Mus musculus 0-8 17949716-1 2007 Spinocerebellar ataxia 2 (SCA2) belongs to the group of neurodegenerative diseases caused by expansion of a polyglutamine (polyQ) domain. polyglutamine 108-121 ataxin 2 Mus musculus 0-24 17949716-1 2007 Spinocerebellar ataxia 2 (SCA2) belongs to the group of neurodegenerative diseases caused by expansion of a polyglutamine (polyQ) domain. polyglutamine 108-121 ataxin 2 Mus musculus 26-30 17949716-1 2007 Spinocerebellar ataxia 2 (SCA2) belongs to the group of neurodegenerative diseases caused by expansion of a polyglutamine (polyQ) domain. polyglutamine 123-128 ataxin 2 Mus musculus 0-24 17949716-1 2007 Spinocerebellar ataxia 2 (SCA2) belongs to the group of neurodegenerative diseases caused by expansion of a polyglutamine (polyQ) domain. polyglutamine 123-128 ataxin 2 Mus musculus 26-30 17949716-4 2007 N-terminal truncated ataxin-2(N) with expanded polyQ repeats did not form intranuclear inclusion and was less cytotoxic than the corresponding full-length ataxin-2. polyglutamine 47-52 ataxin 2 Mus musculus 21-29 17949716-7 2007 These observations confirm that ataxin-2 cytotoxicity increases with increasing polyQ expansion and Golgi dispersion and indicate that, in contrast to other polyQ diseases, N-terminal fragments containing the polyQ repeat are less toxic than full-length ataxin-2. polyglutamine 80-85 ataxin 2 Mus musculus 32-40 17949716-7 2007 These observations confirm that ataxin-2 cytotoxicity increases with increasing polyQ expansion and Golgi dispersion and indicate that, in contrast to other polyQ diseases, N-terminal fragments containing the polyQ repeat are less toxic than full-length ataxin-2. polyglutamine 157-162 ataxin 2 Mus musculus 32-40 17949716-7 2007 These observations confirm that ataxin-2 cytotoxicity increases with increasing polyQ expansion and Golgi dispersion and indicate that, in contrast to other polyQ diseases, N-terminal fragments containing the polyQ repeat are less toxic than full-length ataxin-2. polyglutamine 157-162 ataxin 2 Mus musculus 32-40 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 2 Mus musculus 290-294 34978024-3 2022 The ataxin-2 protein is involved in RNA metabolism; the polyQ expansion may interrupt ataxin-2 interaction with its molecular targets, thus representing a loss-of-function mutation. polyglutamine 56-61 ataxin 2 Mus musculus 86-94