PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 16535398-1 1996 Strain AT3: Evidence for Nortropine as an Intermediate in Tropine Breakdown and Reactions Leading to Succinate. Nortropine 25-35 ataxin 3 Homo sapiens 7-10 16535398-1 1996 Strain AT3: Evidence for Nortropine as an Intermediate in Tropine Breakdown and Reactions Leading to Succinate. tropine 58-65 ataxin 3 Homo sapiens 7-10 16535398-1 1996 Strain AT3: Evidence for Nortropine as an Intermediate in Tropine Breakdown and Reactions Leading to Succinate. Succinic Acid 101-110 ataxin 3 Homo sapiens 7-10 16535398-2 1996 Pseudomonas strain AT3, isolated by elective culture with atropine, hydrolyzed atropine and grew diauxically, first on the tropic acid and then on the tropine. Atropine 58-66 ataxin 3 Homo sapiens 19-22 16535398-2 1996 Pseudomonas strain AT3, isolated by elective culture with atropine, hydrolyzed atropine and grew diauxically, first on the tropic acid and then on the tropine. Atropine 79-87 ataxin 3 Homo sapiens 19-22 16535398-2 1996 Pseudomonas strain AT3, isolated by elective culture with atropine, hydrolyzed atropine and grew diauxically, first on the tropic acid and then on the tropine. tropic acid 123-134 ataxin 3 Homo sapiens 19-22 16535398-2 1996 Pseudomonas strain AT3, isolated by elective culture with atropine, hydrolyzed atropine and grew diauxically, first on the tropic acid and then on the tropine. tropine 59-66 ataxin 3 Homo sapiens 19-22 9109985-3 1996 Expansions of an unstable trinucleotide CAG repeat cause three of these disorders: SCA1, MJD/SCA3 and DRPLA. trinucleotide 26-39 ataxin 3 Homo sapiens 89-92 9109985-3 1996 Expansions of an unstable trinucleotide CAG repeat cause three of these disorders: SCA1, MJD/SCA3 and DRPLA. trinucleotide 26-39 ataxin 3 Homo sapiens 93-97 33822902-5 2021 RESULTS: Patients with MJD exhibited the highest proportion of atypical joints (80.3% in MJD vs 44.1% in axSpA and 37.5% in controls; p< 0.001). axspa 105-110 ataxin 3 Homo sapiens 23-26 8609925-2 1996 Five had an expanded trinucleotide (CAG) repeat sequence in the MJD1 gene on chromosome 14 indicating MJD, while 3 unaffected individuals had normal repeat lengths. trinucleotide 21-34 ataxin 3 Homo sapiens 64-68 8609925-2 1996 Five had an expanded trinucleotide (CAG) repeat sequence in the MJD1 gene on chromosome 14 indicating MJD, while 3 unaffected individuals had normal repeat lengths. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 36-39 ataxin 3 Homo sapiens 64-68 8800925-1 1996 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder associated with the expansion of a CAG trinucleotide repeat in the MJD1 gene located on 14q32.1. trinucleotide 120-133 ataxin 3 Homo sapiens 148-152 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. Alkaloids 33-41 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. Atropine 42-50 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. Carbon 73-79 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. Nitrogen 84-92 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. Nitrogen 96-104 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. tropic acid 148-159 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. tropine 43-50 ataxin 3 Homo sapiens 22-25 8328951-1 1993 Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. Nitrogen 96-104 ataxin 3 Homo sapiens 22-25 8659514-1 1996 Machado-Joseph disease (MJD) is a late-onset, progressive, neurodegenerative disorder caused by the expansion of an unstable trinucleotide (CAG) repeat sequence in a novel gene (MJD1) on chromosome 14. trinucleotide 125-138 ataxin 3 Homo sapiens 178-182 8659514-1 1996 Machado-Joseph disease (MJD) is a late-onset, progressive, neurodegenerative disorder caused by the expansion of an unstable trinucleotide (CAG) repeat sequence in a novel gene (MJD1) on chromosome 14. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 140-143 ataxin 3 Homo sapiens 178-182 7574470-2 1995 We have demonstrated expansion of the CAG trinucleotide repeat of the MJD1 gene located on chromosome 14q32.1 in 2 patients of Azorean descent who presented with levodopa-responsive atypical parkinsonism. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 38-41 ataxin 3 Homo sapiens 70-74 7574470-2 1995 We have demonstrated expansion of the CAG trinucleotide repeat of the MJD1 gene located on chromosome 14q32.1 in 2 patients of Azorean descent who presented with levodopa-responsive atypical parkinsonism. trinucleotide 42-55 ataxin 3 Homo sapiens 70-74 7574470-2 1995 We have demonstrated expansion of the CAG trinucleotide repeat of the MJD1 gene located on chromosome 14q32.1 in 2 patients of Azorean descent who presented with levodopa-responsive atypical parkinsonism. Levodopa 162-170 ataxin 3 Homo sapiens 70-74 7655453-0 1995 Trinucleotide expansion within the MJD1 gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients. trinucleotide 0-13 ataxin 3 Homo sapiens 35-39 7655453-3 1995 The MJD1 gene has recently been cloned and the disease causing mutation has been identified as an unstable and expanded (CAG)n trinucleotide repeat. trinucleotide 127-140 ataxin 3 Homo sapiens 4-8 28364102-0 2017 [Value of 1H-MRS on SCA3/MJD diagnosis and clinical course]. Hydrogen 10-12 ataxin 3 Homo sapiens 20-24 28364102-1 2017 OBJECTIVE: To investigate the value of proton magnetic resonance spectroscopy (1H-MRS) on the diagnosis of SCA3/MJD, and to calculate the correlation between 1H-MRS ratio and the clinical score. Hydrogen 79-81 ataxin 3 Homo sapiens 107-111 28364102-2 2017 : Methods: Sixteen patients with SCA3/MJD and 19 healthy volunteers were scanned with 1H-MRS. Hydrogen 87-89 ataxin 3 Homo sapiens 34-38 28364102-5 2017 : Results: The NAA/Cr in the pons and cerebellar dentate nucleus from the onset patients with SCA3/MJD was significantly reduced compared to that in the normal control group. N-acetylaspartate 16-19 ataxin 3 Homo sapiens 95-99 28364102-5 2017 : Results: The NAA/Cr in the pons and cerebellar dentate nucleus from the onset patients with SCA3/MJD was significantly reduced compared to that in the normal control group. Chromium 20-22 ataxin 3 Homo sapiens 95-99 28364102-6 2017 The NAA/Cr in the cerebellar dentate nucleus of onset patients with SCA3/MJD was obviously correlated with ICARS. N-acetylaspartate 4-7 ataxin 3 Homo sapiens 68-72 28364102-6 2017 The NAA/Cr in the cerebellar dentate nucleus of onset patients with SCA3/MJD was obviously correlated with ICARS. Chromium 8-10 ataxin 3 Homo sapiens 68-72 28364102-11 2017 1H-MRS is useful in the diagnosis of SCA3/MJD. Hydrogen 0-2 ataxin 3 Homo sapiens 37-41 34432315-5 2022 To investigate the optimal treatment regimen, a daily or intermittent CBZ administration was applied to MJD transgenic mice expressing a truncated human ATXN3 with 69 glutamine repeats. Glutamine 167-176 ataxin 3 Homo sapiens 153-158 8634230-0 1995 Open clinical trial of roxithromycin in patients of Plateau Hospitals, Jos in upper and lower respiratory tract infections. Roxithromycin 23-36 ataxin 3 Homo sapiens 71-74 8634230-1 1995 An open clinical study to assess the efficacy and tolerance of Roxithromycin 150 mg twice daily was carried out amongst Nigerian patients with upper and lower respiratory tract infections at Plateau Hospital Jos. Roxithromycin 63-76 ataxin 3 Homo sapiens 208-211 34783886-6 2022 The relationship between the cytosine-adenine-guanine (CAG) repeat length and brain microstructural alterations of preclinical MJD/SCA3 was identified. cytosine-adenine-guanine 29-53 ataxin 3 Homo sapiens 127-130 34628681-4 2021 In addition, antisense oligonucleotide therapy has provided encouraging proofs of concept in models of SCA1, SCA2, SCA3, and SCA7, but they have not yet progressed to clinical trials. Oligonucleotides 23-38 ataxin 3 Homo sapiens 115-119 34938609-0 2022 Allele-specific targeting of mutant ataxin-3 by antisense oligonucleotides in SCA3-iPSC-derived neurons. Oligonucleotides 58-74 ataxin 3 Homo sapiens 36-44 34938609-1 2022 Spinocerebellar ataxia type 3 (SCA3) is caused by an expanded polyglutamine stretch in ataxin-3. polyglutamine 62-75 ataxin 3 Homo sapiens 0-29 34938609-1 2022 Spinocerebellar ataxia type 3 (SCA3) is caused by an expanded polyglutamine stretch in ataxin-3. polyglutamine 62-75 ataxin 3 Homo sapiens 87-95 34938609-3 2022 We established a screening platform with human neurons of patients and controls derived from induced pluripotent stem cells to test antisense oligonucleotides (ASOs) for their effects on ataxin-3 expression. Oligonucleotides 142-158 ataxin 3 Homo sapiens 187-195 34938609-3 2022 We established a screening platform with human neurons of patients and controls derived from induced pluripotent stem cells to test antisense oligonucleotides (ASOs) for their effects on ataxin-3 expression. Oligonucleotides, Antisense 160-164 ataxin 3 Homo sapiens 187-195 34938609-8 2022 This study provides proof of principle that allele-specific lowering of poly(Q)-expanded ataxin-3 by selective ASOs is feasible and long lasting, with sparing of wild-type ataxin-3 expression in a human cell culture model that is genetically identical to SCA3 patients. polyglutamine 72-79 ataxin 3 Homo sapiens 89-97 34783886-6 2022 The relationship between the cytosine-adenine-guanine (CAG) repeat length and brain microstructural alterations of preclinical MJD/SCA3 was identified. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 55-58 ataxin 3 Homo sapiens 127-130 34685571-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region. polyglutamine 212-225 ataxin 3 Homo sapiens 0-29 34713931-3 2022 METHODS: In a prospective cohort study, data on smoking, alcohol consumption, physical activity, physiotherapy, and body mass index (BMI) were collected from 243 patients with SCA3 and 119 controls and tested for associations with age of onset, disease severity, and progression. Alcohols 57-64 ataxin 3 Homo sapiens 176-180 34713931-4 2022 RESULTS: Compared with controls, patients with SCA3 were less active and consumed less alcohol. Alcohols 87-94 ataxin 3 Homo sapiens 47-51 34754867-0 2021 Spinocerebellar ataxia type 3 with dopamine-responsive dystonia: A case report. Dopamine 35-43 ataxin 3 Homo sapiens 0-29 34397117-0 2021 Polyglutamine-Expanded Ataxin-3: A Target Engagement Marker for Spinocerebellar Ataxia Type 3 in Peripheral Blood. polyglutamine 0-13 ataxin 3 Homo sapiens 23-31 34397117-6 2021 RESULTS: Statistical analyses revealed a correlation with clinical parameters and a stability of polyQ-expanded ataxin-3 during conversion from the pre-ataxic to the ataxic phases. polyglutamine 97-102 ataxin 3 Homo sapiens 112-120 34397117-7 2021 CONCLUSIONS: The novel immunoassay is able to quantify polyQ-expanded ataxin-3 in plasma and CSF, whereas ataxin-3 levels in plasma correlate with disease severity. polyglutamine 55-60 ataxin 3 Homo sapiens 70-78 34397117-8 2021 Longitudinal analyses demonstrated a high stability of polyQ-expanded ataxin-3 over a short period. polyglutamine 55-60 ataxin 3 Homo sapiens 70-78 34685571-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region. polyglutamine 212-225 ataxin 3 Homo sapiens 113-118 34685571-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region. polyglutamine 212-225 ataxin 3 Homo sapiens 183-191 34685571-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region. polyglutamine 227-232 ataxin 3 Homo sapiens 0-29 34685571-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region. polyglutamine 227-232 ataxin 3 Homo sapiens 113-118 34685571-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a hereditary ataxia caused by inheritance of a mutated form of the human ATXN3 gene containing an expanded CAG repeat region, encoding a human ataxin-3 protein with a long polyglutamine (polyQ) repeat region. polyglutamine 227-232 ataxin 3 Homo sapiens 183-191 34535635-2 2021 The accumulation of the mutant ataxin-3 proteins carrying expanded polyglutamine (polyQ) leads to selective degeneration of neurons. polyglutamine 67-80 ataxin 3 Homo sapiens 31-39 34535635-2 2021 The accumulation of the mutant ataxin-3 proteins carrying expanded polyglutamine (polyQ) leads to selective degeneration of neurons. polyglutamine 82-87 ataxin 3 Homo sapiens 31-39 34303201-7 2021 There was a significant statistical association between polyQ ATXN3 levels in urine samples and those in plasma. polyglutamine 56-61 ataxin 3 Homo sapiens 62-67 34416891-3 2021 We found that treatment with valproate improved the swimming of the MJD zebrafish, affected levels of acetylated histones 3 and 4, but also increased expression of polyglutamine expanded human ataxin-3. Valproic Acid 29-38 ataxin 3 Homo sapiens 193-201 34416891-3 2021 We found that treatment with valproate improved the swimming of the MJD zebrafish, affected levels of acetylated histones 3 and 4, but also increased expression of polyglutamine expanded human ataxin-3. polyglutamine 164-177 ataxin 3 Homo sapiens 193-201 34303201-8 2021 Further, the levels of polyQ ATXN3 urine associated with an earlier age of SCA3 disease onset. polyglutamine 23-28 ataxin 3 Homo sapiens 29-34 34303201-0 2021 Urine levels of the polyglutamine ataxin-3 protein are elevated in patients with spinocerebellar ataxia type 3. polyglutamine 20-33 ataxin 3 Homo sapiens 34-42 34303201-0 2021 Urine levels of the polyglutamine ataxin-3 protein are elevated in patients with spinocerebellar ataxia type 3. polyglutamine 20-33 ataxin 3 Homo sapiens 81-110 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 30-43 ataxin 3 Homo sapiens 52-60 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 30-43 ataxin 3 Homo sapiens 62-67 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 30-43 ataxin 3 Homo sapiens 104-133 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 45-50 ataxin 3 Homo sapiens 52-60 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 45-50 ataxin 3 Homo sapiens 62-67 34303201-1 2021 INTRODUCTION: Accumulation of polyglutamine (polyQ) ataxin-3 (ATXN3) contributes to the pathobiology of spinocerebellar ataxia type 3 (SCA3). polyglutamine 45-50 ataxin 3 Homo sapiens 104-133 34303201-2 2021 Recently, we showed that polyQ ATXN3 is elevated in the plasma and cerebrospinal fluid (CSF) of SCA3 patients, and has the potential to serve as a biological marker for this disease (1). polyglutamine 25-30 ataxin 3 Homo sapiens 31-36 34322387-0 2021 Downregulation of ATXN3 Enhances the Sensitivity to AKT Inhibitors (Perifosine or MK-2206), but Decreases the Sensitivity to Chemotherapeutic Drugs (Etoposide or Cisplatin) in Neuroblastoma Cells. perifosine 68-78 ataxin 3 Homo sapiens 18-23 34303201-3 2021 Based on these findings, we investigated whether polyQ ATXN3 can also be detected in urine samples from SCA3 patients. polyglutamine 49-54 ataxin 3 Homo sapiens 55-60 34303201-6 2021 RESULTS: PolyQ ATXN3 can be detected in the urine of SCA3 patients, but not in urine samples from healthy controls or other forms of ataxia. polyglutamine 9-14 ataxin 3 Homo sapiens 15-20 34322387-11 2021 Conclusion: Downregulation of ATXN3 enhanced AKT inhibitors (perifosine or MK-2206) induced cell death by BIM, but decreased the cell death induced by chemotherapeutic drugs (etoposide or cisplatin) via Bcl-xl. MK 2206 75-82 ataxin 3 Homo sapiens 30-35 34322387-0 2021 Downregulation of ATXN3 Enhances the Sensitivity to AKT Inhibitors (Perifosine or MK-2206), but Decreases the Sensitivity to Chemotherapeutic Drugs (Etoposide or Cisplatin) in Neuroblastoma Cells. MK 2206 82-89 ataxin 3 Homo sapiens 18-23 34322387-0 2021 Downregulation of ATXN3 Enhances the Sensitivity to AKT Inhibitors (Perifosine or MK-2206), but Decreases the Sensitivity to Chemotherapeutic Drugs (Etoposide or Cisplatin) in Neuroblastoma Cells. Etoposide 149-158 ataxin 3 Homo sapiens 18-23 34322387-0 2021 Downregulation of ATXN3 Enhances the Sensitivity to AKT Inhibitors (Perifosine or MK-2206), but Decreases the Sensitivity to Chemotherapeutic Drugs (Etoposide or Cisplatin) in Neuroblastoma Cells. Cisplatin 162-171 ataxin 3 Homo sapiens 18-23 34322387-3 2021 The aim of our study was to explore the role of ATXN3 in the cell death induced by AKT inhibitor (perifosine or MK-2206) or chemotherapy drugs (etoposide or cisplatin) in NB cells. perifosine 98-108 ataxin 3 Homo sapiens 48-53 34322387-11 2021 Conclusion: Downregulation of ATXN3 enhanced AKT inhibitors (perifosine or MK-2206) induced cell death by BIM, but decreased the cell death induced by chemotherapeutic drugs (etoposide or cisplatin) via Bcl-xl. bim 106-109 ataxin 3 Homo sapiens 30-35 34322387-3 2021 The aim of our study was to explore the role of ATXN3 in the cell death induced by AKT inhibitor (perifosine or MK-2206) or chemotherapy drugs (etoposide or cisplatin) in NB cells. MK 2206 112-119 ataxin 3 Homo sapiens 48-53 34322387-11 2021 Conclusion: Downregulation of ATXN3 enhanced AKT inhibitors (perifosine or MK-2206) induced cell death by BIM, but decreased the cell death induced by chemotherapeutic drugs (etoposide or cisplatin) via Bcl-xl. Etoposide 175-184 ataxin 3 Homo sapiens 30-35 34322387-11 2021 Conclusion: Downregulation of ATXN3 enhanced AKT inhibitors (perifosine or MK-2206) induced cell death by BIM, but decreased the cell death induced by chemotherapeutic drugs (etoposide or cisplatin) via Bcl-xl. Cisplatin 188-197 ataxin 3 Homo sapiens 30-35 34322387-3 2021 The aim of our study was to explore the role of ATXN3 in the cell death induced by AKT inhibitor (perifosine or MK-2206) or chemotherapy drugs (etoposide or cisplatin) in NB cells. Etoposide 144-153 ataxin 3 Homo sapiens 48-53 34322387-3 2021 The aim of our study was to explore the role of ATXN3 in the cell death induced by AKT inhibitor (perifosine or MK-2206) or chemotherapy drugs (etoposide or cisplatin) in NB cells. Cisplatin 157-166 ataxin 3 Homo sapiens 48-53 34322387-7 2021 Results: Downregulation of ATXN3 did not block, but significantly increased the perifosine/MK-2206-induced cell death. perifosine 80-90 ataxin 3 Homo sapiens 27-32 34322387-7 2021 Results: Downregulation of ATXN3 did not block, but significantly increased the perifosine/MK-2206-induced cell death. MK 2206 91-98 ataxin 3 Homo sapiens 27-32 34322387-10 2021 Downregulation of ATXN3 did not increase, but decrease the sensitivity of NB cells to etoposide/cisplatin, and knockdown of Bcl-xl attenuated this decrease in sensitivity. Etoposide 86-95 ataxin 3 Homo sapiens 18-23 34322387-10 2021 Downregulation of ATXN3 did not increase, but decrease the sensitivity of NB cells to etoposide/cisplatin, and knockdown of Bcl-xl attenuated this decrease in sensitivity. Cisplatin 96-105 ataxin 3 Homo sapiens 18-23 34322387-11 2021 Conclusion: Downregulation of ATXN3 enhanced AKT inhibitors (perifosine or MK-2206) induced cell death by BIM, but decreased the cell death induced by chemotherapeutic drugs (etoposide or cisplatin) via Bcl-xl. perifosine 61-71 ataxin 3 Homo sapiens 30-35 34345727-11 2021 Mutation in Ataxin3 polyQ repeats shows pathologically long CAG repeats, 72,10; 72,10; and 72,23 respectively in mutant and wild type allele. polyglutamine 20-25 ataxin 3 Homo sapiens 12-19 35587620-0 2022 Comment on: Polyglutamine-Expanded Ataxin-3: A Target Engagement Marker for Spinocerebellar Ataxia Type 3 in Peripheral Blood. polyglutamine 12-25 ataxin 3 Homo sapiens 35-43 34199295-0 2021 n-Butylidenephthalide Modulates Autophagy to Ameliorate Neuropathological Progress of Spinocerebellar Ataxia Type 3 through mTOR Pathway. butylidenephthalide 0-21 ataxin 3 Homo sapiens 86-115 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 148-161 ataxin 3 Homo sapiens 0-29 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 148-161 ataxin 3 Homo sapiens 199-207 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 148-161 ataxin 3 Homo sapiens 214-219 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 163-168 ataxin 3 Homo sapiens 0-29 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 163-168 ataxin 3 Homo sapiens 199-207 34199295-1 2021 Spinocerebellar ataxia type 3 (SCA3), a hereditary and lethal neurodegenerative disease, is attributed to the abnormal accumulation of undegradable polyglutamine (polyQ), which is encoded by mutated ataxin-3 gene (ATXN3). polyglutamine 163-168 ataxin 3 Homo sapiens 214-219 34795734-0 2021 Level of utilization and provider-related barriers to the use of hydroxyurea in the treatment of sickle cell disease patients in Jos, North-Central Nigeria. Hydroxyurea 65-76 ataxin 3 Homo sapiens 129-132 34795734-2 2021 Objectives: To assess the level of utilization and provider-related barriers to the use of hydroxyurea in SCD therapy in Jos, Nigeria. Hydroxyurea 91-102 ataxin 3 Homo sapiens 121-124 35635856-1 2022 BACKGROUND: The number of trinucleotide CAG repeats is inversely correlated with the age at onset (AAO) of motor symptoms in individuals with Spinocerebellar Ataxia type 3 (SCA 3) and may be responsible for 50%-60% of the variability in AAO. trinucleotide 26-39 ataxin 3 Homo sapiens 142-171 35635856-1 2022 BACKGROUND: The number of trinucleotide CAG repeats is inversely correlated with the age at onset (AAO) of motor symptoms in individuals with Spinocerebellar Ataxia type 3 (SCA 3) and may be responsible for 50%-60% of the variability in AAO. trinucleotide 26-39 ataxin 3 Homo sapiens 173-178 35587632-0 2022 Reply to: "Comment on: Polyglutamine-Expanded Ataxin-3: A Target Engagement Marker for Spinocerebellar Ataxia Type 3 in Peripheral Blood". polyglutamine 23-36 ataxin 3 Homo sapiens 46-54 35488942-2 2022 This disorder is caused by polyglutamine (polyQ)-containing mutant ataxin-3, which tends to misfold and aggregate in neuron cells. polyglutamine 27-40 ataxin 3 Homo sapiens 67-75 35488942-2 2022 This disorder is caused by polyglutamine (polyQ)-containing mutant ataxin-3, which tends to misfold and aggregate in neuron cells. polyglutamine 42-47 ataxin 3 Homo sapiens 67-75 35386195-0 2022 Plasma PolyQ-ATXN3 Levels Associate With Cerebellar Degeneration and Behavioral Abnormalities in a New AAV-Based SCA3 Mouse Model. polyglutamine 7-12 ataxin 3 Homo sapiens 13-18 35544632-2 2022 METHODOLOGY: Through a cross-sectional descriptive study, this study aims to determine the predictors of knowledge about TB among 261 mothers of children under 5 years of age attending Child Welfare Clinic, Bingham University Teaching Hospital, Jos, Plateau State, Nigeria. Terbium 121-123 ataxin 3 Homo sapiens 245-248 35386195-0 2022 Plasma PolyQ-ATXN3 Levels Associate With Cerebellar Degeneration and Behavioral Abnormalities in a New AAV-Based SCA3 Mouse Model. polyglutamine 7-12 ataxin 3 Homo sapiens 113-117 35065349-8 2022 Gamma-T3 exhibited the most potent effects in attenuating apoptosis, whereas alpha-T3 was most effective in preventing 6-OHDA-induced leakage of alpha-Synuclein. Oxidopamine 119-125 ataxin 3 Homo sapiens 77-85 35284767-7 2022 The carbon monoxide specific emissions were 2.78 g/MJd for pellets and 2.75 g/MJd for chips. Carbon Monoxide 4-19 ataxin 3 Homo sapiens 51-54 35284767-7 2022 The carbon monoxide specific emissions were 2.78 g/MJd for pellets and 2.75 g/MJd for chips. Carbon Monoxide 4-19 ataxin 3 Homo sapiens 78-81 35163312-12 2022 Such findings reveal that n-BP could not only inhibit the cleavage of ATXN3 but also protect the QA-induced excitotoxicity from the Purkinje progenitor loss. butylidenephthalide 26-30 ataxin 3 Homo sapiens 70-75 7398733-5 1980 The plasma level of propranolol and the reduction in an exercise tachycardia after L.A. propranolol increased slowly to reach a peak at 6 h and then declined gradually to 24 h. The maximum plasma concentration and effect after sotalol occurred at 3 h and then declined with an elimination half-life of 12.1 h. At 24 h the percentage reduction in an exercise tachycardia was 8.3 +/- 2.5 after oxprenolol, 10.0 +/- 2.3 after S.R. Propranolol 20-31 ataxin 3 Homo sapiens 244-248 35111747-0 2021 MicroRNA-409-3p Targeting at ATXN3 Reduces the Apoptosis of Dopamine Neurons Based on the Profile of miRNAs in the Cerebrospinal Fluid of Early Parkinson"s Disease. Dopamine 60-68 ataxin 3 Homo sapiens 29-34 35111747-9 2021 Moreover, miR-409-3p mimic reduced the aggregation of polyglutamine-expanded mutant of ATXN3 and apoptosis. polyglutamine 54-67 ataxin 3 Homo sapiens 87-92 7398733-5 1980 The plasma level of propranolol and the reduction in an exercise tachycardia after L.A. propranolol increased slowly to reach a peak at 6 h and then declined gradually to 24 h. The maximum plasma concentration and effect after sotalol occurred at 3 h and then declined with an elimination half-life of 12.1 h. At 24 h the percentage reduction in an exercise tachycardia was 8.3 +/- 2.5 after oxprenolol, 10.0 +/- 2.3 after S.R. Sotalol 227-234 ataxin 3 Homo sapiens 244-248 33408245-0 2021 Poly(ADP-ribosyl)ation temporally confines SUMO-dependent ataxin-3 recruitment to control DNA double-strand break repair. poly(adp-ribosyl) 0-17 ataxin 3 Homo sapiens 58-66 33837238-0 2021 PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates. polyglutamine 0-5 ataxin 3 Homo sapiens 56-64 33106888-0 2021 PolyQ-expanded ataxin-3 protein levels in peripheral blood mononuclear cells correlate with clinical parameters in SCA3: a pilot study. polyglutamine 0-5 ataxin 3 Homo sapiens 15-23 33106888-0 2021 PolyQ-expanded ataxin-3 protein levels in peripheral blood mononuclear cells correlate with clinical parameters in SCA3: a pilot study. polyglutamine 0-5 ataxin 3 Homo sapiens 115-119 33106888-5 2021 Additionally, polyQ-expanded ataxin-3 protein levels correlated with disease progression and clinical severity as assessed by the Scale for the Assessment and Rating of Ataxia. polyglutamine 14-19 ataxin 3 Homo sapiens 29-37 33106888-10 2021 In conclusion, the polyQ-expanded ataxin-3 protein is a promising candidate as a molecular target engagement marker in SCA3 in future clinical trials, determinable even in-easily accessible-peripheral blood biomaterials. polyglutamine 19-24 ataxin 3 Homo sapiens 34-42 33106888-10 2021 In conclusion, the polyQ-expanded ataxin-3 protein is a promising candidate as a molecular target engagement marker in SCA3 in future clinical trials, determinable even in-easily accessible-peripheral blood biomaterials. polyglutamine 19-24 ataxin 3 Homo sapiens 119-123 33741019-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a rare neurodegenerative disorder resulting from an aberrant expansion of a polyglutamine stretch in the ataxin-3 protein and subsequent neuronal death. polyglutamine 116-129 ataxin 3 Homo sapiens 0-29 33741019-1 2021 Spinocerebellar ataxia type 3 (SCA3) is a rare neurodegenerative disorder resulting from an aberrant expansion of a polyglutamine stretch in the ataxin-3 protein and subsequent neuronal death. polyglutamine 116-129 ataxin 3 Homo sapiens 145-153 33629274-1 2021 Spinocerebellar ataxia type 3 (SCA3) is the most common type of SCA worldwide caused by abnormal polyglutamine expansion in the coding region of the ataxin-3 gene. polyglutamine 97-110 ataxin 3 Homo sapiens 0-29 33629274-1 2021 Spinocerebellar ataxia type 3 (SCA3) is the most common type of SCA worldwide caused by abnormal polyglutamine expansion in the coding region of the ataxin-3 gene. polyglutamine 97-110 ataxin 3 Homo sapiens 31-35 33629274-1 2021 Spinocerebellar ataxia type 3 (SCA3) is the most common type of SCA worldwide caused by abnormal polyglutamine expansion in the coding region of the ataxin-3 gene. polyglutamine 97-110 ataxin 3 Homo sapiens 149-157 33408245-3 2021 The co-dependence of ataxin-3 recruitment on PARylation and SUMOylation temporally confines its presence at DSBs to a short time window directly following detection of the DNA damage. dsbs 108-112 ataxin 3 Homo sapiens 21-29 33408245-5 2021 Thus, our data show that PARylation differentially regulates SUMO-dependent recruitment of ataxin-3 and RNF4 to DSBs, explaining how both proteins can play a stimulatory role at DSBs despite their opposing activities. dsbs 112-116 ataxin 3 Homo sapiens 91-99 33408245-5 2021 Thus, our data show that PARylation differentially regulates SUMO-dependent recruitment of ataxin-3 and RNF4 to DSBs, explaining how both proteins can play a stimulatory role at DSBs despite their opposing activities. dsbs 178-182 ataxin 3 Homo sapiens 91-99 32978817-1 2021 OBJECTIVE: In spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD), the expanded cytosine adenine guanine (CAG) repeat in ATXN3 is the causal mutation, and its length is the main factor in determining the age at onset (AO) of clinical symptoms. cytosine adenine guanine 92-116 ataxin 3 Homo sapiens 73-76 33065068-0 2021 Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. polyglutamine 58-71 ataxin 3 Homo sapiens 80-88 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Homo sapiens 119-148 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Homo sapiens 150-154 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 15-20 ataxin 3 Homo sapiens 119-148 33542212-1 2021 Polyglutamine (polyQ) diseases comprise Huntington"s disease and several subtypes of spinocerebellar ataxia, including spinocerebellar ataxia type 3 (SCA3). polyglutamine 15-20 ataxin 3 Homo sapiens 150-154 33542212-10 2021 Our data suggest that Exoc7/exo70 exerts its ATXN3-polyQ-modifying effect through regulating the E3 ligase function of Prpf19/prp19. polyglutamine 51-56 ataxin 3 Homo sapiens 45-50 32978817-1 2021 OBJECTIVE: In spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD), the expanded cytosine adenine guanine (CAG) repeat in ATXN3 is the causal mutation, and its length is the main factor in determining the age at onset (AO) of clinical symptoms. cytosine adenine guanine 92-116 ataxin 3 Homo sapiens 133-138 32978817-1 2021 OBJECTIVE: In spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD), the expanded cytosine adenine guanine (CAG) repeat in ATXN3 is the causal mutation, and its length is the main factor in determining the age at onset (AO) of clinical symptoms. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 118-121 ataxin 3 Homo sapiens 73-76 32978817-1 2021 OBJECTIVE: In spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD), the expanded cytosine adenine guanine (CAG) repeat in ATXN3 is the causal mutation, and its length is the main factor in determining the age at onset (AO) of clinical symptoms. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 118-121 ataxin 3 Homo sapiens 133-138 20301375-2 1993 DIAGNOSIS/TESTING: The diagnosis of SCA3 rests on the use of molecular genetic testing to detect an abnormal CAG trinucleotide repeat expansion in ATXN3. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 109-112 ataxin 3 Homo sapiens 36-40 33425926-1 2020 DNA damage response (DDR) and apoptosis are reported to be involved in the pathogenesis of many neurodegenerative diseases including polyglutamine (polyQ) disorders, such as Spinocerebellar ataxia type 3 (SCA3) and Huntington"s disease (HD). polyglutamine 133-146 ataxin 3 Homo sapiens 174-203 33425926-1 2020 DNA damage response (DDR) and apoptosis are reported to be involved in the pathogenesis of many neurodegenerative diseases including polyglutamine (polyQ) disorders, such as Spinocerebellar ataxia type 3 (SCA3) and Huntington"s disease (HD). polyglutamine 148-153 ataxin 3 Homo sapiens 174-203 33425926-2 2020 Consistently, an increasing body of studies provide compelling evidence for the crucial roles of ATX3, whose polyQ expansion is defined as the cause of SCA3, in the maintenance of genome integrity and regulation of apoptosis. polyglutamine 109-114 ataxin 3 Homo sapiens 97-101 33425926-3 2020 The polyQ expansion in ATX3 seems to affect its physiological functions in these distinct pathways. polyglutamine 4-9 ataxin 3 Homo sapiens 23-27 32817181-6 2020 RESULTS: sNfL concentrations were elevated in asymptomatic, preclinical, and ataxic ATXN3 mutation carriers compared to controls (12.18 [10.20-13.92], 21.84 [18.37-23.45], 36.06 [30.04-45.90] and 8.24 [5.92-10.84] pg/mL, median [interquartile range], respectively, p < 0 001). snfl 9-13 ataxin 3 Homo sapiens 84-89 33196459-7 2020 In retinoic acid-differentiated ATXN3/Q75-GFP SH-SY5Y cells inflamed with IFN-gamma-primed HMC3 conditioned medium, treatment with the tested compounds mitigated the increased caspase 1 activity and lactate dehydrogenase release, reduced polyQ aggregation and ROS and/or promoted neurite outgrowth. Tretinoin 3-16 ataxin 3 Homo sapiens 32-37 33102457-8 2020 We further demonstrated a pronounced capability of LCC-L-CR in inhibiting the aggregation of expanded Ataxin-3, disease protein of SCA type 3, in human neuronal cells. lcc-l-cr 51-59 ataxin 3 Homo sapiens 102-110 32643267-1 2020 BACKGROUND: Homozygous spinocerebellar ataxia type 3 (SCA3) patients, which have an expanded cytosine-adenine-guanine (CAG) repeat mutation in both alleles of ATXN3, are extremely rare. cytosine-adenine-guanine 93-117 ataxin 3 Homo sapiens 23-52 32643267-1 2020 BACKGROUND: Homozygous spinocerebellar ataxia type 3 (SCA3) patients, which have an expanded cytosine-adenine-guanine (CAG) repeat mutation in both alleles of ATXN3, are extremely rare. cytosine-adenine-guanine 93-117 ataxin 3 Homo sapiens 159-164 32643267-1 2020 BACKGROUND: Homozygous spinocerebellar ataxia type 3 (SCA3) patients, which have an expanded cytosine-adenine-guanine (CAG) repeat mutation in both alleles of ATXN3, are extremely rare. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 119-122 ataxin 3 Homo sapiens 23-52 33613103-0 2021 Involvement of miR-619-5p in resistance to cisplatin by regulating ATXN3 in oral squamous cell carcinoma. Cisplatin 43-52 ataxin 3 Homo sapiens 67-72 33613103-9 2021 Importantly, ATXN3 was responsible for the regulatory effects of miR-619-5p on biological behaviors of cisplatin-resistant OSCC cells. Cisplatin 103-112 ataxin 3 Homo sapiens 13-18 33413777-9 2020 Aspect of vitamin E forms in sea fish, detection rates alpha-T3, gamma-T and gamma-T3 were 28. Vitamin E 10-19 ataxin 3 Homo sapiens 55-63 33413777-18 2020 With respect to correlation analysis, there was a strong correlation between gamma-T and alpha-T3 in sea fish, while weak correlation of isomers in aquatic fish and certain correlations of isomers in shrimp and crab. gamma-t 77-84 ataxin 3 Homo sapiens 89-97 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 0-29 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 78-86 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 93-98 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 130-143 ataxin 3 Homo sapiens 152-157 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 0-29 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 78-86 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 93-98 33087504-1 2020 Spinocerebellar ataxia type 3 (SCA3), caused by a CAG repeat expansion in the ataxin-3 gene (ATXN3), is characterized by neuronal polyglutamine (polyQ) ATXN3 protein aggregates. polyglutamine 145-150 ataxin 3 Homo sapiens 152-157 33087504-2 2020 Although there is no cure for SCA3, gene-silencing approaches to reduce toxic polyQ ATXN3 showed promise in preclinical models. polyglutamine 78-83 ataxin 3 Homo sapiens 84-89 33087504-5 2020 We show that polyQ ATXN3 serves as a marker of target engagement in human fibroblasts, which may bode well for its use in clinical trials. polyglutamine 13-18 ataxin 3 Homo sapiens 19-24 32643791-2 2020 Mutations in ataxin-3 cause spinocerebellar ataxia type 3 (SCA3), a neurodegenerative disorder that is a member of the polyglutamine family of diseases. polyglutamine 119-132 ataxin 3 Homo sapiens 13-21 32643791-2 2020 Mutations in ataxin-3 cause spinocerebellar ataxia type 3 (SCA3), a neurodegenerative disorder that is a member of the polyglutamine family of diseases. polyglutamine 119-132 ataxin 3 Homo sapiens 28-57 20301375-2 1993 DIAGNOSIS/TESTING: The diagnosis of SCA3 rests on the use of molecular genetic testing to detect an abnormal CAG trinucleotide repeat expansion in ATXN3. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 109-112 ataxin 3 Homo sapiens 147-152 20301375-2 1993 DIAGNOSIS/TESTING: The diagnosis of SCA3 rests on the use of molecular genetic testing to detect an abnormal CAG trinucleotide repeat expansion in ATXN3. trinucleotide 113-126 ataxin 3 Homo sapiens 36-40 20301375-2 1993 DIAGNOSIS/TESTING: The diagnosis of SCA3 rests on the use of molecular genetic testing to detect an abnormal CAG trinucleotide repeat expansion in ATXN3. trinucleotide 113-126 ataxin 3 Homo sapiens 147-152 20301375-12 1993 Offspring of affected individuals have a 50% chance of inheriting the abnormal CAG trinucleotide repeat expansion in ATXN3. trinucleotide 83-96 ataxin 3 Homo sapiens 117-122 31970864-1 2020 Expansion above a certain threshold in the polyglutamine (polyQ) tract of ataxin-3 is the main cause of neurodegeneration in Machado-Joseph disease. polyglutamine 43-56 ataxin 3 Homo sapiens 74-82 31970864-1 2020 Expansion above a certain threshold in the polyglutamine (polyQ) tract of ataxin-3 is the main cause of neurodegeneration in Machado-Joseph disease. polyglutamine 58-63 ataxin 3 Homo sapiens 74-82 31970864-2 2020 Ataxin-3 contains an N-terminal catalytic domain, called Josephin domain, and a highly aggregation-prone C-terminal domain containing the polyQ tract. polyglutamine 138-143 ataxin 3 Homo sapiens 0-8 31970864-5 2020 We hypothesize that the expansion of the polyQ tract in ataxin-3 could impact CME. polyglutamine 41-46 ataxin 3 Homo sapiens 56-64 32340608-3 2020 Moreover, the difference in frequency and timing of appearance of an HCB between MSA-C and spinocerebellar ataxia type 3 (SCA3) has not been fully investigated. Hexachlorobenzene 69-72 ataxin 3 Homo sapiens 91-120 32361312-1 2020 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is autosomal-dominant neurodegenerative disease caused by an expansion of polyglutamine-encoding CAG repeats in the ATXN3 gene. polyglutamine 156-169 ataxin 3 Homo sapiens 0-29 32361312-1 2020 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is autosomal-dominant neurodegenerative disease caused by an expansion of polyglutamine-encoding CAG repeats in the ATXN3 gene. polyglutamine 156-169 ataxin 3 Homo sapiens 31-35 32361312-1 2020 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is autosomal-dominant neurodegenerative disease caused by an expansion of polyglutamine-encoding CAG repeats in the ATXN3 gene. polyglutamine 156-169 ataxin 3 Homo sapiens 198-203 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 168-181 ataxin 3 Homo sapiens 0-29 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 183-188 ataxin 3 Homo sapiens 0-29 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 183-188 ataxin 3 Homo sapiens 220-228 31783119-1 2020 Spinocerebellar Ataxia type 3 (SCA3, also known as Machado-Joseph disease) is a neurodegenerative disorder caused by a CAG repeat expansion encoding an abnormally long polyglutamine (polyQ) tract in the disease protein, ataxin-3 (ATXN3). polyglutamine 183-188 ataxin 3 Homo sapiens 230-235 31783119-5 2020 We screened a collection of siRNAs targeting 2742 druggable human genes using a cell-based assay based on luminescence readout of polyQ-expanded ATXN3. polyglutamine 130-135 ataxin 3 Homo sapiens 145-150 31669734-0 2020 Pathogenesis of SCA3 and implications for other polyglutamine diseases. polyglutamine 48-61 ataxin 3 Homo sapiens 16-20 31927329-4 2020 Here we show that repeat-targeting short hairpin RNAs preferentially reduce the levels of mutant huntingtin, atrophin-1, ataxin-3, and ataxin-7 proteins in patient-derived fibroblasts and may serve as universal allele-selective reagents for polyglutamine (polyQ) diseases. polyglutamine 241-254 ataxin 3 Homo sapiens 121-129 31927329-4 2020 Here we show that repeat-targeting short hairpin RNAs preferentially reduce the levels of mutant huntingtin, atrophin-1, ataxin-3, and ataxin-7 proteins in patient-derived fibroblasts and may serve as universal allele-selective reagents for polyglutamine (polyQ) diseases. polyglutamine 256-261 ataxin 3 Homo sapiens 121-129 31310802-1 2019 The most commonly inherited dominant ataxia, Spinocerebellar Ataxia Type 3 (SCA3), is caused by a CAG repeat expansion that encodes an abnormally long polyglutamine (polyQ) repeat in the disease protein ataxin-3, a deubiquitinase. polyglutamine 151-164 ataxin 3 Homo sapiens 76-80 31625269-1 2020 The pathology of spinocerebellar ataxia type 3, also known as Machado-Joseph disease, is triggered by aggregation of toxic ataxin-3 (ATXN3) variants containing expanded polyglutamine repeats. polyglutamine 169-182 ataxin 3 Homo sapiens 123-131 31625269-1 2020 The pathology of spinocerebellar ataxia type 3, also known as Machado-Joseph disease, is triggered by aggregation of toxic ataxin-3 (ATXN3) variants containing expanded polyglutamine repeats. polyglutamine 169-182 ataxin 3 Homo sapiens 133-138 31767406-3 2020 Here, we demonstrate that the same agents also deplete other polyglutamine disease-related proteins: mutant ataxin-3 and ataxin-7 in cells from spino-cerebellar ataxia patients, and mutant atrophin-1 in cells from dentatorubral-pallidoluysian atrophy patients. polyglutamine 61-74 ataxin 3 Homo sapiens 108-116 32274760-4 2020 The genetic cause of MJD is a polyglutamine (polyQ) repeat expansion in the gene that encodes ataxin-3. polyglutamine 30-43 ataxin 3 Homo sapiens 94-102 32274760-4 2020 The genetic cause of MJD is a polyglutamine (polyQ) repeat expansion in the gene that encodes ataxin-3. polyglutamine 45-50 ataxin 3 Homo sapiens 94-102 32274760-5 2020 This polyQ-containing protein displays a well-defined catalytic activity as ataxin-3 is a deubiquitylating enzyme that removes and disassembles ubiquitin chains from specific substrates. polyglutamine 5-10 ataxin 3 Homo sapiens 76-84 32274760-6 2020 While mutant ataxin-3 with an expanded polyQ repeat induces cellular stress due to its propensity to aggregate, the native functions of wild-type ataxin-3 are linked to the cellular countermeasures against the very same stress conditions inflicted by polyQ-containing and other aggregation-prone proteins. polyglutamine 39-44 ataxin 3 Homo sapiens 13-21 32274760-6 2020 While mutant ataxin-3 with an expanded polyQ repeat induces cellular stress due to its propensity to aggregate, the native functions of wild-type ataxin-3 are linked to the cellular countermeasures against the very same stress conditions inflicted by polyQ-containing and other aggregation-prone proteins. polyglutamine 251-256 ataxin 3 Homo sapiens 13-21 32274760-6 2020 While mutant ataxin-3 with an expanded polyQ repeat induces cellular stress due to its propensity to aggregate, the native functions of wild-type ataxin-3 are linked to the cellular countermeasures against the very same stress conditions inflicted by polyQ-containing and other aggregation-prone proteins. polyglutamine 251-256 ataxin 3 Homo sapiens 146-154 31310802-1 2019 The most commonly inherited dominant ataxia, Spinocerebellar Ataxia Type 3 (SCA3), is caused by a CAG repeat expansion that encodes an abnormally long polyglutamine (polyQ) repeat in the disease protein ataxin-3, a deubiquitinase. polyglutamine 166-171 ataxin 3 Homo sapiens 76-80 31639609-1 2019 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant disorder that is caused by the abnormal amplification of cytosine-adenine-guanine (CAG) trinucleotide repeats in the ATXN3 gene. cytosine-adenine-guanine 119-143 ataxin 3 Homo sapiens 0-29 31639609-1 2019 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant disorder that is caused by the abnormal amplification of cytosine-adenine-guanine (CAG) trinucleotide repeats in the ATXN3 gene. cytosine-adenine-guanine 119-143 ataxin 3 Homo sapiens 179-184 31639609-1 2019 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant disorder that is caused by the abnormal amplification of cytosine-adenine-guanine (CAG) trinucleotide repeats in the ATXN3 gene. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 145-148 ataxin 3 Homo sapiens 0-29 31639609-1 2019 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant disorder that is caused by the abnormal amplification of cytosine-adenine-guanine (CAG) trinucleotide repeats in the ATXN3 gene. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 145-148 ataxin 3 Homo sapiens 179-184 31639609-1 2019 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant disorder that is caused by the abnormal amplification of cytosine-adenine-guanine (CAG) trinucleotide repeats in the ATXN3 gene. trinucleotide 150-163 ataxin 3 Homo sapiens 0-29 31639609-1 2019 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant disorder that is caused by the abnormal amplification of cytosine-adenine-guanine (CAG) trinucleotide repeats in the ATXN3 gene. trinucleotide 150-163 ataxin 3 Homo sapiens 179-184 31683630-6 2019 Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2"-O-methyl modified bases on a phosphorothioate backbone. 2"-o-methyl 210-221 ataxin 3 Homo sapiens 89-97 31197505-4 2019 We show that cholesterol 24-hydroxylase (CYP46A1), the key enzyme allowing efflux of brain cholesterol and activating brain cholesterol turnover, is decreased in cerebellar extracts from SCA3 patients and SCA3 mice. Cholesterol 13-24 ataxin 3 Homo sapiens 187-191 31197505-4 2019 We show that cholesterol 24-hydroxylase (CYP46A1), the key enzyme allowing efflux of brain cholesterol and activating brain cholesterol turnover, is decreased in cerebellar extracts from SCA3 patients and SCA3 mice. Cholesterol 13-24 ataxin 3 Homo sapiens 205-209 31683630-0 2019 Removal of the Polyglutamine Repeat of Ataxin-3 by Redirecting pre-mRNA Processing. polyglutamine 15-28 ataxin 3 Homo sapiens 39-47 31683630-2 2019 One of nine polyglutamine disorders known to date, SCA3 is clinically heterogeneous and the main feature is progressive ataxia, which in turn affects speech, balance and gait of the affected individual. polyglutamine 12-25 ataxin 3 Homo sapiens 51-55 31683630-3 2019 SCA3 is caused by an expanded polyglutamine tract in the ataxin-3 protein, resulting in conformational changes that lead to toxic gain of function. polyglutamine 30-43 ataxin 3 Homo sapiens 0-4 31197505-4 2019 We show that cholesterol 24-hydroxylase (CYP46A1), the key enzyme allowing efflux of brain cholesterol and activating brain cholesterol turnover, is decreased in cerebellar extracts from SCA3 patients and SCA3 mice. Cholesterol 91-102 ataxin 3 Homo sapiens 187-191 31683630-6 2019 Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2"-O-methyl modified bases on a phosphorothioate backbone. 4-nitrophenyl phosphorothioate 242-258 ataxin 3 Homo sapiens 89-97 31683630-3 2019 SCA3 is caused by an expanded polyglutamine tract in the ataxin-3 protein, resulting in conformational changes that lead to toxic gain of function. polyglutamine 30-43 ataxin 3 Homo sapiens 57-65 31683630-6 2019 Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2"-O-methyl modified bases on a phosphorothioate backbone. polyglutamine 66-79 ataxin 3 Homo sapiens 89-97 31683630-7 2019 Significant downregulation of both the expanded and non-expanded protein was induced by the morpholino antisense oligomer, with a greater proportion of ataxin-3 protein missing the polyglutamine tract. polyglutamine 181-194 ataxin 3 Homo sapiens 152-160 31683630-6 2019 Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2"-O-methyl modified bases on a phosphorothioate backbone. DIAMIDOPHOSPHATE 113-131 ataxin 3 Homo sapiens 89-97 31683630-9 2019 These results suggest that morpholino oligomers may provide greater therapeutic benefit for the treatment of spinocerebellar ataxia type 3, without toxic effects. Morpholinos 27-37 ataxin 3 Homo sapiens 109-138 31683630-6 2019 Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2"-O-methyl modified bases on a phosphorothioate backbone. Morpholinos 132-142 ataxin 3 Homo sapiens 89-97 31374463-0 2019 Antisense oligonucleotide therapy rescues aggresome formation in a novel spinocerebellar ataxia type 3 human embryonic stem cell line. Oligonucleotides 10-25 ataxin 3 Homo sapiens 73-102 31749756-0 2019 Carboxyl Terminus of Hsp70-Interacting Protein Is Increased in Serum and Cerebrospinal Fluid of Patients With Spinocerebellar Ataxia Type 3. carboxyl radical 0-8 ataxin 3 Homo sapiens 110-139 31691128-1 2019 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is a neurodegenerative disorder caused by a polyglutamine expansion in the ATXN3 gene. polyglutamine 126-139 ataxin 3 Homo sapiens 0-29 31691128-1 2019 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is a neurodegenerative disorder caused by a polyglutamine expansion in the ATXN3 gene. polyglutamine 126-139 ataxin 3 Homo sapiens 31-35 31691128-1 2019 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is a neurodegenerative disorder caused by a polyglutamine expansion in the ATXN3 gene. polyglutamine 126-139 ataxin 3 Homo sapiens 157-162 31107713-0 2019 Divalproex sodium regulates ataxin-3 translocation likely by an importin alpha1-dependent pathway. Valproic Acid 0-17 ataxin 3 Homo sapiens 28-36 31107713-3 2019 In our previous study, we found that divalproex sodium (DVS) reduced heat shock-induced nuclear localization of ataxin-3. Valproic Acid 37-54 ataxin 3 Homo sapiens 112-120 31107713-3 2019 In our previous study, we found that divalproex sodium (DVS) reduced heat shock-induced nuclear localization of ataxin-3. Valproic Acid 56-59 ataxin 3 Homo sapiens 112-120 31828177-2 2019 The expanded CAG repeat is translated into a prolonged polyglutamine repeat in the ataxin-3 protein and accumulates within inclusions, acquiring toxic properties, which results in degeneration of the cerebellum and brain stem. polyglutamine 55-68 ataxin 3 Homo sapiens 83-91 31687087-2 2019 The expanded CAG repeats encode a polyglutamine (polyQ) tract at the C-terminus of the ATXN3 protein. polyglutamine 49-54 ataxin 3 Homo sapiens 87-92 31687087-3 2019 ATXN3 containing expanded polyQ forms aggregates, leading to subsequent cellular dysfunctions including an impaired ubiquitin-proteasome system (UPS). polyglutamine 26-31 ataxin 3 Homo sapiens 0-5 31157458-4 2019 Previously, we have shown a significant increase in the expression of carbonic anhydrase VIII (CA8) in SK-N-SH-MJD78 cells, which are human neuroblastoma cells overexpressing mutant ataxin-3 with 78 glutamine repeats. Glutamine 199-208 ataxin 3 Homo sapiens 182-190 31374463-3 2019 Referred to as SCA3-hESC, this line is heterozygous for the mutant polyglutamine-encoding CAG repeat expansion in the ATXN3 gene. polyglutamine 67-80 ataxin 3 Homo sapiens 118-123 31374463-6 2019 Finally, antisense oligonucleotide-mediated reduction of ATXN3 markedly suppressed aggresome formation. Oligonucleotides 19-34 ataxin 3 Homo sapiens 57-62 30707359-7 2019 We show its usefulness by performing a comparative study of the interactome of the nine polyglutamine (polyQ) disease proteins, namely androgen receptor (AR), atrophin-1 (ATN1), ataxin 1 (ATXN1), ataxin 2 (ATXN2), ataxin 3 (ATXN3), ataxin 7 (ATXN7), calcium voltage-gated channel subunit alpha1 A (CACNA1A), Huntingtin (HTT), and TATA-binding protein (TBP). polyglutamine 88-101 ataxin 3 Homo sapiens 214-222 31316347-7 2019 Our study demonstrates that symptomatic SCA3 patients present distinct metabolic profiles with perturbed AA metabolism and fatty acid metabolism, and FFA 16:1, FFA 18:3, L-Proline and L-Tryptophan are identified as potential disease biomarkers. Fatty Acids 123-133 ataxin 3 Homo sapiens 40-44 31379806-4 2019 Depletion of ataxin-3 leads to impaired induction of mitochondrial reactive oxygen species (mROS) and defective bacterial killing. Reactive Oxygen Species 67-90 ataxin 3 Homo sapiens 13-21 30707359-7 2019 We show its usefulness by performing a comparative study of the interactome of the nine polyglutamine (polyQ) disease proteins, namely androgen receptor (AR), atrophin-1 (ATN1), ataxin 1 (ATXN1), ataxin 2 (ATXN2), ataxin 3 (ATXN3), ataxin 7 (ATXN7), calcium voltage-gated channel subunit alpha1 A (CACNA1A), Huntingtin (HTT), and TATA-binding protein (TBP). polyglutamine 88-101 ataxin 3 Homo sapiens 224-229 30455355-6 2019 At the pathological level, we found that the expansion of the polyglutamine repeat leads to a stabilization of ataxin-3 and that ataxin-3 isoforms differ in their aggregation properties. polyglutamine 62-75 ataxin 3 Homo sapiens 111-119 30455355-7 2019 Interestingly, we observed a functional interaction between normal and polyglutamine-expanded ATXN3 allelic variants. polyglutamine 71-84 ataxin 3 Homo sapiens 94-99 31619607-6 2019 A calculation of the most stable structure of Asx in the presence of alpha-T or T3, suggested that only T3 was able to hydrogen bond with Asx, and the Asx polyene chain partially interacting with the alpha-T3 triene chain, which could explain the synergistic effect between Asx and T3, but not Asx and alpha-T. astaxanthine 46-49 ataxin 3 Homo sapiens 200-208 31188927-2 2019 Due to an expanded polyglutamine at ataxin-3, SCA3/MJD presents a relentless course with no current disease modifying treatment. polyglutamine 19-32 ataxin 3 Homo sapiens 36-44 31188927-2 2019 Due to an expanded polyglutamine at ataxin-3, SCA3/MJD presents a relentless course with no current disease modifying treatment. polyglutamine 19-32 ataxin 3 Homo sapiens 51-54 31619607-6 2019 A calculation of the most stable structure of Asx in the presence of alpha-T or T3, suggested that only T3 was able to hydrogen bond with Asx, and the Asx polyene chain partially interacting with the alpha-T3 triene chain, which could explain the synergistic effect between Asx and T3, but not Asx and alpha-T. alpha-Tocopherol 69-76 ataxin 3 Homo sapiens 200-208 31619607-6 2019 A calculation of the most stable structure of Asx in the presence of alpha-T or T3, suggested that only T3 was able to hydrogen bond with Asx, and the Asx polyene chain partially interacting with the alpha-T3 triene chain, which could explain the synergistic effect between Asx and T3, but not Asx and alpha-T. asx polyene 151-162 ataxin 3 Homo sapiens 200-208 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 105-118 ataxin 3 Homo sapiens 12-41 31378764-0 2019 Disulfiram facilitates ataxin-3 nuclear translocation and potentiates the cytotoxicity in a cell model of SCA3. Disulfiram 0-10 ataxin 3 Homo sapiens 23-31 31378764-1 2019 Spinocerebellar ataxia type 3 (SCA3) is caused by the expansion of a glutamine-encoding CAG repeat in the ATXN3 gene encoding the protein ataxin-3. Glutamine 69-78 ataxin 3 Homo sapiens 0-29 31378764-1 2019 Spinocerebellar ataxia type 3 (SCA3) is caused by the expansion of a glutamine-encoding CAG repeat in the ATXN3 gene encoding the protein ataxin-3. Glutamine 69-78 ataxin 3 Homo sapiens 106-111 31378764-1 2019 Spinocerebellar ataxia type 3 (SCA3) is caused by the expansion of a glutamine-encoding CAG repeat in the ATXN3 gene encoding the protein ataxin-3. Glutamine 69-78 ataxin 3 Homo sapiens 138-146 31378764-2 2019 The nuclear presence of polyglutamine-expanded ataxin-3 is of critical importance for the pathogenesis of SCA3. polyglutamine 24-37 ataxin 3 Homo sapiens 47-55 31378764-5 2019 Bearing this in mind, we treated cells expressing ataxin-3 with disulfiram to measure several pathogenic cascades of SCA3, including aggregate formation, soluble ataxin-3 expression and nuclear localization of ataxin-3 and the cytotoxicity, which assess the direct effect of disulfiram on SCA3 cell models. Disulfiram 64-74 ataxin 3 Homo sapiens 50-58 31378764-6 2019 To our knowledge, this is direct evidence that disulfiram elevated the nuclear localization of polyglutamine-expanded ataxin-3 and enhanced the cytotoxicity in a cell model of SCA3. Disulfiram 47-57 ataxin 3 Homo sapiens 118-126 31378764-6 2019 To our knowledge, this is direct evidence that disulfiram elevated the nuclear localization of polyglutamine-expanded ataxin-3 and enhanced the cytotoxicity in a cell model of SCA3. polyglutamine 95-108 ataxin 3 Homo sapiens 118-126 31378764-8 2019 Our findings repurpose disulfiram as a modulator of ataxin-3 nuclear transport that aggravates the pathology of SCA3, which is a new target for disulfiram. Disulfiram 23-33 ataxin 3 Homo sapiens 52-60 31378764-8 2019 Our findings repurpose disulfiram as a modulator of ataxin-3 nuclear transport that aggravates the pathology of SCA3, which is a new target for disulfiram. Disulfiram 144-154 ataxin 3 Homo sapiens 52-60 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 105-118 ataxin 3 Homo sapiens 152-160 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 105-118 ataxin 3 Homo sapiens 162-167 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 120-125 ataxin 3 Homo sapiens 12-41 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 120-125 ataxin 3 Homo sapiens 152-160 30147021-1 2019 BACKGROUND: Spinocerebellar ataxia type 3 (SCA3), the most common spinocerebellar ataxia, is caused by a polyglutamine (polyQ) expansion in the protein ataxin-3 (ATXN3). polyglutamine 120-125 ataxin 3 Homo sapiens 162-167 30147021-2 2019 Silencing the expression of polyQ-expanded ATXN3 rescues the cellular disease phenotype. polyglutamine 28-33 ataxin 3 Homo sapiens 43-48 30287796-6 2018 Aggregation curves measured by the standard thioflavin-T (ThT) fluorescence assay are shown to reflect the relative composition of protein monomers and soluble oligomers measured by nuclear magnetic resonance (NMR) for human insulin, and by dynamic light scattering (DLS) for ataxin-3. thioflavin T 58-61 ataxin 3 Homo sapiens 276-284 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 3 Homo sapiens 67-72 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 3 Homo sapiens 73-77 30190267-5 2018 In contrast, neurons cultured from zebrafish expressing human ataxin-3 with disease-associated expanded polyQ repeats did not accumulate within nuclei in a manner often reported to occur in SCA3. polyglutamine 104-109 ataxin 3 Homo sapiens 62-70 30036587-1 2018 An expansion of the polyglutamine (polyQ) tract within the deubiquitinase ataxin-3 protein is believed to play a role in a neurodegenerative disorder. polyglutamine 20-33 ataxin 3 Homo sapiens 74-82 30036587-1 2018 An expansion of the polyglutamine (polyQ) tract within the deubiquitinase ataxin-3 protein is believed to play a role in a neurodegenerative disorder. polyglutamine 35-40 ataxin 3 Homo sapiens 74-82 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 3-32 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 34-38 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 229-237 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 199-212 ataxin 3 Homo sapiens 239-244 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 3-32 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 34-38 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 229-237 30086154-2 2018 In spinocerebellar ataxia type 3 (SCA3), the co-chaperone DnaJ homology subfamily B member 1 (DNAJB1 or heat shock protein 40) is recruited to protein aggregates formed by the disease-causing mutant polyglutamine (polyQ) protein ataxin-3 (ATXN3). polyglutamine 214-219 ataxin 3 Homo sapiens 239-244 30042316-1 2018 The protein ataxin-3 contains a polyglutamine stretch that triggers amyloid aggregation when it is expanded beyond a critical threshold. polyglutamine 32-45 ataxin 3 Homo sapiens 12-20 30042316-0 2018 Protein Environment: A Crucial Triggering Factor in Josephin Domain Aggregation: The Role of 2,2,2-Trifluoroethanol. Trifluoroethanol 93-115 ataxin 3 Homo sapiens 52-60 29972812-6 2018 Ataxin-3 is a 42-kDa protein containing a globular N-terminal Josephin domain and a C-terminal tail that comprises 13 polyglutamine repeats within a low complexity region. polyglutamine 118-131 ataxin 3 Homo sapiens 0-8 29936336-1 2018 A skin biopsy of a patient with spinocerebellar ataxia type 3 (SCA3, also known as Machado-Joseph disease (MJD)) caused by a CAG trinucleotide repeat expansion in the ATXN3 gene, was used to generate an induced pluripotent stem cell line, HIHCNi002-A (iPSC-SCA3). trinucleotide 129-142 ataxin 3 Homo sapiens 32-61 29936336-1 2018 A skin biopsy of a patient with spinocerebellar ataxia type 3 (SCA3, also known as Machado-Joseph disease (MJD)) caused by a CAG trinucleotide repeat expansion in the ATXN3 gene, was used to generate an induced pluripotent stem cell line, HIHCNi002-A (iPSC-SCA3). trinucleotide 129-142 ataxin 3 Homo sapiens 63-67 29936336-1 2018 A skin biopsy of a patient with spinocerebellar ataxia type 3 (SCA3, also known as Machado-Joseph disease (MJD)) caused by a CAG trinucleotide repeat expansion in the ATXN3 gene, was used to generate an induced pluripotent stem cell line, HIHCNi002-A (iPSC-SCA3). trinucleotide 129-142 ataxin 3 Homo sapiens 167-172 29661116-0 2018 CRISPR/Cas9-Targeted Deletion of Polyglutamine in Spinocerebellar Ataxia Type 3-Derived Induced Pluripotent Stem Cells. polyglutamine 33-46 ataxin 3 Homo sapiens 50-79 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. cytosine-adenine-guanine 79-103 ataxin 3 Homo sapiens 0-29 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. cytosine-adenine-guanine 79-103 ataxin 3 Homo sapiens 121-126 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. cytosine-adenine-guanine 79-103 ataxin 3 Homo sapiens 187-195 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. cytosine-adenine-guanine 79-103 ataxin 3 Homo sapiens 197-202 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 105-108 ataxin 3 Homo sapiens 0-29 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 105-108 ataxin 3 Homo sapiens 121-126 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 105-108 ataxin 3 Homo sapiens 187-195 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 105-108 ataxin 3 Homo sapiens 197-202 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 0-29 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 121-126 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 187-195 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 152-165 ataxin 3 Homo sapiens 197-202 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 0-29 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 121-126 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 187-195 29661116-1 2018 Spinocerebellar ataxia type 3 (SCA3) is caused by an abnormal expansion of the cytosine-adenine-guanine (CAG) triplet in ATXN3, which translates into a polyglutamine (polyQ) tract within ataxin-3 (ATXN3) protein. polyglutamine 167-172 ataxin 3 Homo sapiens 197-202 29111377-0 2018 Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. polyglutamine 41-54 ataxin 3 Homo sapiens 64-72 30035006-2 2018 Methods: 17 genetically-confirmed SCA3 patients and 16 controls underwent structural MRI and static resting-state [18F]-Fluoro-deoxyglucose Positron Emission Tomography (FDG-PET) imaging. Fluorodeoxyglucose F18 114-139 ataxin 3 Homo sapiens 34-38 29229556-1 2018 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine (polyQ) tract in the ataxin-3 protein. polyglutamine 152-165 ataxin 3 Homo sapiens 0-29 29229556-1 2018 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine (polyQ) tract in the ataxin-3 protein. polyglutamine 167-172 ataxin 3 Homo sapiens 0-29 29229556-1 2018 Spinocerebellar ataxia type 3 (SCA3), or Machado-Joseph disease (MJD), is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine (polyQ) tract in the ataxin-3 protein. polyglutamine 167-172 ataxin 3 Homo sapiens 187-195 29427106-12 2018 While misfolding of ataxin-3 due to overly long polyglutamine stretches is a critical contributor to the pathogenesis of SCA-3/MJD, the great neuropathological complexity of the disorder remains largely unexplained. polyglutamine 48-61 ataxin 3 Homo sapiens 20-28 29427106-12 2018 While misfolding of ataxin-3 due to overly long polyglutamine stretches is a critical contributor to the pathogenesis of SCA-3/MJD, the great neuropathological complexity of the disorder remains largely unexplained. polyglutamine 48-61 ataxin 3 Homo sapiens 121-130 29427109-0 2018 Polyglutamine-Independent Features in Ataxin-3 Aggregation and Pathogenesis of Machado-Joseph Disease. polyglutamine 0-13 ataxin 3 Homo sapiens 38-46 29318784-0 2018 Divalproex sodium modulates nuclear localization of ataxin-3 and prevents cellular toxicity caused by expanded ataxin-3. Valproic Acid 0-17 ataxin 3 Homo sapiens 52-60 29318784-0 2018 Divalproex sodium modulates nuclear localization of ataxin-3 and prevents cellular toxicity caused by expanded ataxin-3. Valproic Acid 0-17 ataxin 3 Homo sapiens 111-119 29318784-1 2018 BACKGROUND & AIMS: Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal dominantly inherited neurodegenerative disorder and the most common form of SCA worldwide. Adenosine Monophosphate 12-15 ataxin 3 Homo sapiens 23-52 29318784-1 2018 BACKGROUND & AIMS: Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal dominantly inherited neurodegenerative disorder and the most common form of SCA worldwide. Adenosine Monophosphate 12-15 ataxin 3 Homo sapiens 54-58 29318784-5 2018 METHODS: In this study, we explored the effect of divalproex sodium as an HDACi in SCA3 cell models and explored how divalproex sodium interferes with pathogenetic processes causing SCA3. Valproic Acid 50-67 ataxin 3 Homo sapiens 83-87 29318784-6 2018 RESULTS: We found that divalproex sodium rescues the hypoacetylation levels of histone H3 and attenuates cellular cytotoxicity induced by expanded ataxin-3 partly via preventing nuclear transport of ataxin-3 (particularly heat shock-dependent). Valproic Acid 23-40 ataxin 3 Homo sapiens 147-155 29318784-6 2018 RESULTS: We found that divalproex sodium rescues the hypoacetylation levels of histone H3 and attenuates cellular cytotoxicity induced by expanded ataxin-3 partly via preventing nuclear transport of ataxin-3 (particularly heat shock-dependent). Valproic Acid 23-40 ataxin 3 Homo sapiens 199-207 29318784-7 2018 CONCLUSION: Our study provides novel insights into the mechanisms of action of divalproex sodium as a possible treatment for SCA3, beyond the known regulation of transcription. Valproic Acid 79-96 ataxin 3 Homo sapiens 125-129 29534440-5 2018 Additionally, all of them except ATx 3 (+), caused similar results when the accumulation of the P-gp fluorescent substrate was evaluated after pre-incubating cells with the test compounds for 24 h, significantly reducing the rhodamine 123 intracellular accumulation as a result of a significant increase in P-gp activity. Rhodamines 225-234 ataxin 3 Homo sapiens 33-38 29937988-0 2018 Genetic polymorphisms in ataxin-3 and liver cirrhosis risk related to aflatoxin B1. Aflatoxin B1 70-82 ataxin 3 Homo sapiens 25-33 29334808-0 2018 Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1. polyglutamine 101-114 ataxin 3 Homo sapiens 54-62 29334808-4 2018 Ataxin-3 consists of a globular N-terminal Josephin domain, which can aggregate into curvilinear protofibrils, and an unstructured, dynamically disordered C-terminal domain containing three ubiquitin interacting motifs separated by a polyglutamine stretch. polyglutamine 234-247 ataxin 3 Homo sapiens 0-8 29334808-5 2018 Upon expansion of the polyglutamine region above 50 residues, ataxin-3 undergoes a second stage of aggregation in which long, straight amyloid fibrils form. polyglutamine 22-35 ataxin 3 Homo sapiens 62-70 29334808-6 2018 A peptide inhibitor of polyglutamine aggregation, known as polyQ binding peptide 1, has been shown previously to prevent the maturation of ataxin-3 fibrils. polyglutamine 23-36 ataxin 3 Homo sapiens 139-147 29334808-8 2018 Using nanoelectrospray ionisation-mass spectrometry, we demonstrate that polyQ binding peptide 1 binds to monomeric ataxin-3. polyglutamine 73-78 ataxin 3 Homo sapiens 116-124 29334808-9 2018 By investigating the ability of polyQ binding peptide 1 to bind to truncated ataxin-3 constructs lacking one or more domains, we localise the site of this interaction to a 39-residue sequence immediately C-terminal to the Josephin domain. polyglutamine 32-37 ataxin 3 Homo sapiens 77-85 29244944-4 2018 Emission factors of CO2, CO, THC, CH4, and NOx on the basis of useful energy delivered (MJd) were 142 +- 17, 0.77 +- 0.55, 130 +- 196, 5.6 +- 8.2, and 46 +- 9 mg/MJd, respectively. Carbon Monoxide 20-22 ataxin 3 Homo sapiens 88-91 29244944-4 2018 Emission factors of CO2, CO, THC, CH4, and NOx on the basis of useful energy delivered (MJd) were 142 +- 17, 0.77 +- 0.55, 130 +- 196, 5.6 +- 8.2, and 46 +- 9 mg/MJd, respectively. nicotine 1-N-oxide 43-46 ataxin 3 Homo sapiens 88-91 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 101-114 ataxin 3 Homo sapiens 64-68 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 101-114 ataxin 3 Homo sapiens 71-79 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 116-121 ataxin 3 Homo sapiens 64-68 29111377-3 2018 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine 116-121 ataxin 3 Homo sapiens 71-79 29111377-5 2018 Hence, we analyzed the repertoire of proteins interacting with normal and polyQ expanded ataxin-3 by mass spectrometry. polyglutamine 74-79 ataxin 3 Homo sapiens 89-97 29111377-6 2018 This showed that both normal and polyQ expanded ataxin-3 interacted with components of the protein quality control system and mitochondria. polyglutamine 33-38 ataxin 3 Homo sapiens 48-56 29111377-7 2018 Five proteins showed increased interaction with polyQ expanded ataxin-3 relative to normal and three of these were mitochondrial proteins. polyglutamine 48-53 ataxin 3 Homo sapiens 63-71 29045563-8 2017 In conclusion, we established a novel transgenic marmoset line carrying the mutant human ataxin 3 gene controlled by the tet-on system. tetramethylenedisulfotetramine 121-124 ataxin 3 Homo sapiens 89-97 29061563-6 2017 We tested three neuroprotective compounds (Methylene Blue, guanabenz and salubrinal) believed to modulate ER stress and observed that these molecules rescued ATXN3-CAG89 phenotypes. Methylene Blue 43-57 ataxin 3 Homo sapiens 158-163 29061563-6 2017 We tested three neuroprotective compounds (Methylene Blue, guanabenz and salubrinal) believed to modulate ER stress and observed that these molecules rescued ATXN3-CAG89 phenotypes. Guanabenz 59-68 ataxin 3 Homo sapiens 158-163 29061563-6 2017 We tested three neuroprotective compounds (Methylene Blue, guanabenz and salubrinal) believed to modulate ER stress and observed that these molecules rescued ATXN3-CAG89 phenotypes. salubrinal 73-83 ataxin 3 Homo sapiens 158-163 29045563-4 2017 The mutant human ataxin 3 gene controlled by the tet-on system was introduced into marmoset embryos via lentiviral transduction, and 34 transgene-introduced embryos were transferred into the uteri of surrogate mothers. tetramethylenedisulfotetramine 49-52 ataxin 3 Homo sapiens 17-25 28939772-6 2017 We also probed the nucleotide dependence of this interaction, confirming that ataxin3 and p97 associate in the presence of ATP and in the absence of nucleotide, but not in the presence of ADP. Adenosine Triphosphate 123-126 ataxin 3 Homo sapiens 78-85 28939772-7 2017 Our experiments suggest that an ADP-driven downward movement of the p97 N-terminal domain dislodges ataxin3 by inducing a steric clash between the D1-domain and ataxin3"s C terminus. Adenosine Diphosphate 32-35 ataxin 3 Homo sapiens 100-107 28939772-7 2017 Our experiments suggest that an ADP-driven downward movement of the p97 N-terminal domain dislodges ataxin3 by inducing a steric clash between the D1-domain and ataxin3"s C terminus. Adenosine Diphosphate 32-35 ataxin 3 Homo sapiens 161-168 28687604-2 2017 We have successfully established the first transgenic zebrafish (Danio rerio) model of MJD by expressing human ataxin-3 protein containing either 23 glutamines (23Q, wild-type) or 84Q (MJD-causing) within neurons. Glutamine 149-159 ataxin 3 Homo sapiens 111-119 28900413-14 2017 Both patients with PD and SCA3 showed impairment of such plasticity, suggesting significant functional perturbation of the CDTC circuit. cdtc 123-127 ataxin 3 Homo sapiens 26-30 29042637-1 2017 The protein ataxin-3 carries a polyglutamine stretch close to the C-terminus that triggers a neurodegenerative disease in humans when its length exceeds a critical threshold. polyglutamine 31-44 ataxin 3 Homo sapiens 12-20 28979235-2 2017 Conformational changes in mutant ataxin-3 trigger different pathogenic cascades, including reactive oxygen species (ROS) generation; however, the clinical relevance of oxidative stress elements as peripheral biomarkers of SCA3/MJD remains unknown. Reactive Oxygen Species 91-114 ataxin 3 Homo sapiens 33-41 28979235-2 2017 Conformational changes in mutant ataxin-3 trigger different pathogenic cascades, including reactive oxygen species (ROS) generation; however, the clinical relevance of oxidative stress elements as peripheral biomarkers of SCA3/MJD remains unknown. Reactive Oxygen Species 116-119 ataxin 3 Homo sapiens 33-41 28722507-6 2017 Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. polyglutamine 24-29 ataxin 3 Homo sapiens 102-107 28722507-6 2017 Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. polyglutamine 24-29 ataxin 3 Homo sapiens 145-150 28722507-6 2017 Interestingly, expanded polyQ tracts in other polyglutamine disease proteins compete with the shorter ATXN3 polyQ stretch and interfere with the ATXN3-BECN1 interaction. polyglutamine 108-113 ataxin 3 Homo sapiens 102-107 28687604-8 2017 Cotreatment with the autophagy inhibitor chloroquine blocked the decrease in human ataxin-3 levels and the improved movement produced by calpeptin treatment. Chloroquine 41-52 ataxin 3 Homo sapiens 83-91 28687604-11 2017 We have found that treating the MJD zebrafish with the calpain inhibitor compound calpeptin produces complete removal of human ataxin-3 protein, due to induction of the autophagy quality control pathway. calpeptin 82-91 ataxin 3 Homo sapiens 127-135 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 0-29 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 31-35 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 156-161 28676741-1 2017 Spinocerebellar ataxia type 3 (SCA3), known as Machado-Joseph disease, is an autosomal dominant disease caused by an abnormal expansion of polyglutamine in ATXN3 gene, leading to neurodegeneration in SCA3 patients. polyglutamine 139-152 ataxin 3 Homo sapiens 200-204 28676741-8 2017 Furthermore, truncated mutant ATXN3 decreased the mitochondrial membrane potential, increased reactive oxygen species and finally increased cell death rate. Reactive Oxygen Species 94-117 ataxin 3 Homo sapiens 30-35 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 129-142 ataxin 3 Homo sapiens 100-108 28485591-3 2017 The combustion of LPG and alcohol (~1011 particles per useful energy delivered, particles/MJd), and kerosene (~1013 particles/MJd), produced emissions that were lower by 2-3 orders of magnitude than solid fuels (1014-1015 particles/MJd). Alcohols 26-33 ataxin 3 Homo sapiens 90-93 28334907-6 2017 We found that ataxin-3 is primarily cleaved at two sites, namely at amino acid positions D208 and S256 and mutating amino acids at both cleavage sites to tryptophan nearly abolished ataxin-3 fragmentation. Tryptophan 154-164 ataxin 3 Homo sapiens 14-22 28334907-6 2017 We found that ataxin-3 is primarily cleaved at two sites, namely at amino acid positions D208 and S256 and mutating amino acids at both cleavage sites to tryptophan nearly abolished ataxin-3 fragmentation. Tryptophan 154-164 ataxin 3 Homo sapiens 182-190 28065793-0 2017 Polyglutamine expansion of ataxin-3 alters its degree of ubiquitination and phosphorylation at specific sites. polyglutamine 0-13 ataxin 3 Homo sapiens 27-35 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 129-142 ataxin 3 Homo sapiens 65-69 28624196-3 2017 Here we tested antisense oligonucleotides (ASOs) that target human ATXN3 in two complementary mouse models of SCA3: yeast artificial chromosome (YAC) MJD-Q84.2 (Q84) mice expressing the full-length human ATXN3 gene and cytomegalovirus (CMV) MJD-Q135 (Q135) mice expressing a human ATXN3 cDNA. Oligonucleotides 25-41 ataxin 3 Homo sapiens 67-72 28624196-3 2017 Here we tested antisense oligonucleotides (ASOs) that target human ATXN3 in two complementary mouse models of SCA3: yeast artificial chromosome (YAC) MJD-Q84.2 (Q84) mice expressing the full-length human ATXN3 gene and cytomegalovirus (CMV) MJD-Q135 (Q135) mice expressing a human ATXN3 cDNA. Oligonucleotides, Antisense 43-47 ataxin 3 Homo sapiens 67-72 30460066-3 2017 The autophagy inhibitor 3-MA increased the steady-state level of ataxin-3 and stabilized SUMO-modified ataxin-3 more prominently than the proteasome inhibitor MG132. 3-methyladenine 24-28 ataxin 3 Homo sapiens 65-73 30460066-3 2017 The autophagy inhibitor 3-MA increased the steady-state level of ataxin-3 and stabilized SUMO-modified ataxin-3 more prominently than the proteasome inhibitor MG132. 3-methyladenine 24-28 ataxin 3 Homo sapiens 103-111 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 144-149 ataxin 3 Homo sapiens 65-69 28236214-8 2017 Our results show that both alpha-Syn and mutant Atx3 overexpression per se increased oxidation of dichlorodihydrofluorescein (DCFH2), and co-expression of these proteins exhibited additive effect on intracellular oxidation, with no correlation with apoptotic features. dichlorodihydrofluorescein 98-124 ataxin 3 Homo sapiens 48-52 28065793-2 2017 In the neurodegenerative disorder spinocerebellar ataxia type 3 (SCA3), the disease causing protein ataxin-3 carries an expanded polyglutamine (polyQ) stretch causing it to aggregate in nuclear inclusions. polyglutamine 144-149 ataxin 3 Homo sapiens 100-108 28065793-8 2017 However, the distribution of ubiquitinated lysine residues was altered in polyQ expanded ataxin-3, with increased ubiquitination at the new identified ubiquitination site lysine-8. Lysine 43-49 ataxin 3 Homo sapiens 89-97 28236214-8 2017 Our results show that both alpha-Syn and mutant Atx3 overexpression per se increased oxidation of dichlorodihydrofluorescein (DCFH2), and co-expression of these proteins exhibited additive effect on intracellular oxidation, with no correlation with apoptotic features. dcfh2 126-131 ataxin 3 Homo sapiens 48-52 28065793-8 2017 However, the distribution of ubiquitinated lysine residues was altered in polyQ expanded ataxin-3, with increased ubiquitination at the new identified ubiquitination site lysine-8. polyglutamine 74-79 ataxin 3 Homo sapiens 89-97 28236214-9 2017 Mutant Atx3 and alpha-Syn also potentiated altered redox status induced by iron and rotenone, a hint to how these proteins might influence neuronal dysfunction under pro-oxidant conditions. Iron 75-79 ataxin 3 Homo sapiens 7-11 28065793-11 2017 However, the observed differences between the normal and polyQ expanded ataxin-3 with respect to the degree of ubiquitination and phosphorylation on specific sites may have an impact on ataxin-3 function and SCA3 pathogenesis. polyglutamine 57-62 ataxin 3 Homo sapiens 72-80 28065793-11 2017 However, the observed differences between the normal and polyQ expanded ataxin-3 with respect to the degree of ubiquitination and phosphorylation on specific sites may have an impact on ataxin-3 function and SCA3 pathogenesis. polyglutamine 57-62 ataxin 3 Homo sapiens 186-194 28236214-9 2017 Mutant Atx3 and alpha-Syn also potentiated altered redox status induced by iron and rotenone, a hint to how these proteins might influence neuronal dysfunction under pro-oxidant conditions. Rotenone 84-92 ataxin 3 Homo sapiens 7-11 28236214-10 2017 We further show that overexpression of wild-type Atx3 decreased intracellular DCFH2 oxidation, possibly exerting a neuroprotective role. dcfh2 78-83 ataxin 3 Homo sapiens 49-53 28065793-11 2017 However, the observed differences between the normal and polyQ expanded ataxin-3 with respect to the degree of ubiquitination and phosphorylation on specific sites may have an impact on ataxin-3 function and SCA3 pathogenesis. polyglutamine 57-62 ataxin 3 Homo sapiens 208-212 28448548-2 2017 We recently found that the endocannabinoid system is altered in the post-mortem cerebellum of SCA-3 patients, and similar results were also found in the cerebellar and brainstem nuclei of a SCA-3 transgenic mouse model. Endocannabinoids 27-42 ataxin 3 Homo sapiens 94-99 28223212-5 2017 Our preliminary data on anti-aggregation and toxic fragment formation using an HEK (human embryonic kidney cells) 293T-84Q-eGFP (green fluorescent protein) cell model identified n-butylidenephthalide (n-BP) as a potential drug treatment for SCA3. butylidenephthalide 178-199 ataxin 3 Homo sapiens 241-245 28223212-5 2017 Our preliminary data on anti-aggregation and toxic fragment formation using an HEK (human embryonic kidney cells) 293T-84Q-eGFP (green fluorescent protein) cell model identified n-butylidenephthalide (n-BP) as a potential drug treatment for SCA3. butylidenephthalide 201-205 ataxin 3 Homo sapiens 241-245 28223212-6 2017 n-BP decreased toxic fragment formation in both SCA3 cell and animal models. butylidenephthalide 0-4 ataxin 3 Homo sapiens 48-52 28223212-8 2017 To comprehend the molecular basis behind the control of toxic fragment formation, we used microarray analysis to identify tryptophan metabolism as a major player in controlling the fate of mutant ATXN3 aggregates. Tryptophan 122-132 ataxin 3 Homo sapiens 196-201 28223212-10 2017 In addition, through the control of TDO2, n-BP also decreases active calpain levels, an important enzyme involved in the proteolysis of mutant ATXN3, thereby decreasing toxic fragment formation and associated neurotoxicity. butylidenephthalide 42-46 ataxin 3 Homo sapiens 143-148 28448548-2 2017 We recently found that the endocannabinoid system is altered in the post-mortem cerebellum of SCA-3 patients, and similar results were also found in the cerebellar and brainstem nuclei of a SCA-3 transgenic mouse model. Endocannabinoids 27-42 ataxin 3 Homo sapiens 190-195 28236575-1 2017 Machado-Joseph disease (MJD) is a genetic neurodegenerative disease caused by an expanded polyglutamine tract within the protein ataxin-3 (ATXN3). polyglutamine 90-103 ataxin 3 Homo sapiens 129-137 28275011-5 2017 Ataxin-3 is recruited to DSBs in a SUMOylation-dependent fashion, and in vitro it directly interacts with and is stimulated by recombinant SUMO, defining a SUMO-dependent mechanism for DUB activity toward MDC1. 1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione 25-29 ataxin 3 Homo sapiens 0-8 28236575-1 2017 Machado-Joseph disease (MJD) is a genetic neurodegenerative disease caused by an expanded polyglutamine tract within the protein ataxin-3 (ATXN3). polyglutamine 90-103 ataxin 3 Homo sapiens 139-144 26861241-0 2017 Effects of the enlargement of polyglutamine segments on the structure and folding of ataxin-2 and ataxin-3 proteins. polyglutamine 30-43 ataxin 3 Homo sapiens 98-106 28449807-10 2017 A significant reduction of cancer as cause of death was observed in SCA3/MJD, suggesting a common effect to all polyglutamine diseases. polyglutamine 112-125 ataxin 3 Homo sapiens 73-76 26861241-1 2017 Spinocerebellar ataxia type 2 (SCA2) and type 3 (SCA3) are two common autosomal-dominant inherited ataxia syndromes, both of which are related to the unstable expansion of trinucleotide CAG repeats in the coding region of the related ATXN2 and ATXN3 genes, respectively. trinucleotide 172-185 ataxin 3 Homo sapiens 244-249 26861241-3 2017 In this study, using the I-TASSER method for 3D structure prediction, we investigated the effect of poly-Q tract enlargement on the structure and folding of ataxin-2 and ataxin-3 proteins. polyglutamine 100-106 ataxin 3 Homo sapiens 170-178 26861241-5 2017 The changes observed in the predicted models of the UIM domains in ataxin-3 when the poly-Q track is enlarged provide new insights on possible pathogenic mechanisms. polyglutamine 85-91 ataxin 3 Homo sapiens 67-75 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. trinucleotide 101-114 ataxin 3 Homo sapiens 0-29 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. trinucleotide 101-114 ataxin 3 Homo sapiens 162-167 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. trinucleotide 101-114 ataxin 3 Homo sapiens 200-208 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. polyglutamine 227-240 ataxin 3 Homo sapiens 0-29 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. polyglutamine 227-240 ataxin 3 Homo sapiens 162-167 28395798-1 2017 Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited neurodegenerative disease caused by a trinucleotide repeat (CAG) expansion in the coding region of ATXN3 gene resulting in production of ataxin-3 with an elongated polyglutamine tract. polyglutamine 227-240 ataxin 3 Homo sapiens 200-208 27878228-1 2016 Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of the polyglutamine domain of the ataxin-3 (ATX3) protein. polyglutamine 148-161 ataxin 3 Homo sapiens 32-61 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 70-83 ataxin 3 Homo sapiens 28-57 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 70-83 ataxin 3 Homo sapiens 59-63 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 85-90 ataxin 3 Homo sapiens 28-57 27647319-1 2016 INTRODUCTION AND OBJECTIVE: Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder for which the routine molecular testing is based on PCR and automated capillary electrophoresis. polyglutamine 85-90 ataxin 3 Homo sapiens 59-63 27878228-1 2016 Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of the polyglutamine domain of the ataxin-3 (ATX3) protein. polyglutamine 148-161 ataxin 3 Homo sapiens 176-184 27878228-1 2016 Machado-Joseph disease (MJD) or spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by expansion of the polyglutamine domain of the ataxin-3 (ATX3) protein. polyglutamine 148-161 ataxin 3 Homo sapiens 186-190 27878228-5 2016 Here, we report on the potential use of lithium carbonate and coenzyme Q10 to reduce cell death caused by the expanded ATX3 in cell culture. Lithium Carbonate 40-57 ataxin 3 Homo sapiens 119-123 27878228-5 2016 Here, we report on the potential use of lithium carbonate and coenzyme Q10 to reduce cell death caused by the expanded ATX3 in cell culture. coenzyme Q10 62-74 ataxin 3 Homo sapiens 119-123 27878228-7 2016 Treatment with lithium carbonate and coenzyme Q10 led to a significant increase in viability of cells expressing expanded ATX3 (Q84). Lithium Carbonate 15-32 ataxin 3 Homo sapiens 122-126 27878228-7 2016 Treatment with lithium carbonate and coenzyme Q10 led to a significant increase in viability of cells expressing expanded ATX3 (Q84). coenzyme Q10 37-49 ataxin 3 Homo sapiens 122-126 27878228-9 2016 Furthermore, there was a significant change in the expanded ATX3 monomer/aggregate ratio after lithium carbonate and coenzyme Q10 treatment, with an increase in the monomer fraction and decrease in aggregates. Lithium Carbonate 95-112 ataxin 3 Homo sapiens 60-64 27878228-9 2016 Furthermore, there was a significant change in the expanded ATX3 monomer/aggregate ratio after lithium carbonate and coenzyme Q10 treatment, with an increase in the monomer fraction and decrease in aggregates. coenzyme Q10 117-129 ataxin 3 Homo sapiens 60-64 27731380-0 2016 Antisense oligonucleotide-mediated exon skipping as a strategy to reduce proteolytic cleavage of ataxin-3. Oligonucleotides 10-25 ataxin 3 Homo sapiens 97-105 27502086-4 2016 Cytosine-adenine-guanine repeats size in the Ataxin-3 gene was measured, and patients with expanded cytosine-adenine-guanine repeats >44 were diagnosed genetically as having spinocerebellar ataxia type 3. cytosine-adenine-guanine 0-24 ataxin 3 Homo sapiens 45-53 27502086-10 2016 The mean number of cytosine-adenine-guanine repeats in the Ataxin-3 gene of the diseased allele was 67 (range 55-76). cytosine-adenine-guanine 19-43 ataxin 3 Homo sapiens 59-67 27731380-1 2016 Spinocerebellar ataxia type-3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine repeat expansion in the ataxin-3 protein. polyglutamine 81-94 ataxin 3 Homo sapiens 0-29 27731380-1 2016 Spinocerebellar ataxia type-3 (SCA3) is a neurodegenerative disorder caused by a polyglutamine repeat expansion in the ataxin-3 protein. polyglutamine 81-94 ataxin 3 Homo sapiens 119-127 27731380-2 2016 Cleavage of mutant ataxin-3 by proteolytic enzymes yields ataxin-3 fragments containing the polyglutamine stretch. polyglutamine 92-105 ataxin 3 Homo sapiens 19-27 27731380-2 2016 Cleavage of mutant ataxin-3 by proteolytic enzymes yields ataxin-3 fragments containing the polyglutamine stretch. polyglutamine 92-105 ataxin 3 Homo sapiens 58-66 27731380-4 2016 As a strategy to prevent formation of toxic cleavage fragments, we investigated an antisense oligonucleotide-mediated modification of the ataxin-3 pre-mRNA through exon skipping of exon 8 and 9, resulting in the removal of a central 88 amino acid region of the ataxin-3 protein. Oligonucleotides 93-108 ataxin 3 Homo sapiens 138-146 27731380-4 2016 As a strategy to prevent formation of toxic cleavage fragments, we investigated an antisense oligonucleotide-mediated modification of the ataxin-3 pre-mRNA through exon skipping of exon 8 and 9, resulting in the removal of a central 88 amino acid region of the ataxin-3 protein. Oligonucleotides 93-108 ataxin 3 Homo sapiens 261-269 27328712-1 2016 Machado Joseph Disease (MJD) is the most frequent autosomal dominantly inherited cerebellar ataxia caused by the over-repetition of a CAG trinucleotide in the ATXN3 gene. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 134-137 ataxin 3 Homo sapiens 159-164 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 52-65 ataxin 3 Homo sapiens 87-95 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 77-82 ataxin 3 Homo sapiens 0-4 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 77-82 ataxin 3 Homo sapiens 87-95 27469193-6 2016 The cells expressing ataxin-3-78Q demonstrated decreased viability, and increased sensitivity to metabolic stress in the presence rotenone, an inhibitor of mitochondrial respiration. Rotenone 130-138 ataxin 3 Homo sapiens 21-29 27469193-10 2016 Finally, the expression profile LC3-II, Beclin-1 and p62 suggested that FIR prevent the autophagy inhibiting effects observed in ataxin-3-78Q expressing cells. fir 72-75 ataxin 3 Homo sapiens 129-137 27469193-3 2016 SCA3 is caused by a mutation leading to an abnormal polyglutamine expansion (PolyQ) in ataxin-3 protein. polyglutamine 52-65 ataxin 3 Homo sapiens 0-4 27328712-1 2016 Machado Joseph Disease (MJD) is the most frequent autosomal dominantly inherited cerebellar ataxia caused by the over-repetition of a CAG trinucleotide in the ATXN3 gene. trinucleotide 138-151 ataxin 3 Homo sapiens 159-164 27328712-2 2016 This expansion translates into a polyglutamine tract within the ataxin-3 protein that confers a toxic gain-of-function to the mutant protein ataxin-3, contributing to protein misfolding and intracellular accumulation of aggregates and neuronal degeneration. polyglutamine 33-46 ataxin 3 Homo sapiens 64-72 27328712-2 2016 This expansion translates into a polyglutamine tract within the ataxin-3 protein that confers a toxic gain-of-function to the mutant protein ataxin-3, contributing to protein misfolding and intracellular accumulation of aggregates and neuronal degeneration. polyglutamine 33-46 ataxin 3 Homo sapiens 141-149 26997655-0 2016 Safety and efficacy of valproic acid treatment in SCA3/MJD patients. Valproic Acid 23-36 ataxin 3 Homo sapiens 55-58 27133716-3 2016 In this study, we report that a novel J-protein, DNAJ (HSP40) Homolog, Subfamily C, Member 8 (DNAJC8), suppresses the aggregation of polyQ-containing protein in a cellular model of spinocerebellar ataxia type 3 (SCA3), which is also known as Machado-Joseph disease. polyglutamine 133-138 ataxin 3 Homo sapiens 181-210 27133716-3 2016 In this study, we report that a novel J-protein, DNAJ (HSP40) Homolog, Subfamily C, Member 8 (DNAJC8), suppresses the aggregation of polyQ-containing protein in a cellular model of spinocerebellar ataxia type 3 (SCA3), which is also known as Machado-Joseph disease. polyglutamine 133-138 ataxin 3 Homo sapiens 212-216 27133716-7 2016 These results indicate that DNAJC8 can suppress the polyQ aggregation via a distinct mechanism independent of HSP70-based chaperone machinery and have a unique protective role against the aggregation of expanded polyQ-containing proteins such as pathogenic ataxin-3 proteins. polyglutamine 212-217 ataxin 3 Homo sapiens 257-265 26997655-1 2016 BACKGROUND: Spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD) is one of 10 known polyglutamine (polyQ) diseases. polyglutamine 95-108 ataxin 3 Homo sapiens 71-74 26997655-1 2016 BACKGROUND: Spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD) is one of 10 known polyglutamine (polyQ) diseases. polyglutamine 110-115 ataxin 3 Homo sapiens 71-74 26997655-4 2016 We evaluated the clinical safety and efficacy of VPA treatment for SCA3/MJD patients. Valproic Acid 49-52 ataxin 3 Homo sapiens 72-75 26997655-13 2016 CONCLUSIONS: VPA is a potentially beneficial agent for the treatment of SCA3/MJD. Valproic Acid 13-16 ataxin 3 Homo sapiens 77-80 27047745-1 2016 An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. polyglutamine 31-36 ataxin 3 Homo sapiens 50-58 27047745-2 2016 The crystal structure of the polyQ-containing carboxy-terminal fragment of human ataxin-3 was solved at 2.2-A resolution. polyglutamine 29-34 ataxin 3 Homo sapiens 81-89 27047745-1 2016 An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. polyglutamine 16-29 ataxin 3 Homo sapiens 50-58 27047745-3 2016 The Atxn3 carboxy-terminal fragment including 14 glutamine residues adopts both random coil and alpha-helical conformations in the crystal structure. Glutamine 49-58 ataxin 3 Homo sapiens 4-9 26260925-3 2015 For example, polyglutamine expansion in ataxin-3 allosterically triggers the aggregation of the catalytic Josephin domain. polyglutamine 13-26 ataxin 3 Homo sapiens 40-48 26295831-3 2016 Using a SCA3 ATXN3/Q75-GFP cell model, we found that the ATXN3/Q75 aggregation was significantly prohibited by lactulose and melibiose because of their abilities to up-regulate autophagy. Lactulose 111-120 ataxin 3 Homo sapiens 8-12 26295831-3 2016 Using a SCA3 ATXN3/Q75-GFP cell model, we found that the ATXN3/Q75 aggregation was significantly prohibited by lactulose and melibiose because of their abilities to up-regulate autophagy. Lactulose 111-120 ataxin 3 Homo sapiens 13-18 26295831-3 2016 Using a SCA3 ATXN3/Q75-GFP cell model, we found that the ATXN3/Q75 aggregation was significantly prohibited by lactulose and melibiose because of their abilities to up-regulate autophagy. Lactulose 111-120 ataxin 3 Homo sapiens 57-62 26295831-4 2016 Meanwhile, lactulose and melibiose reduced reactive oxygen species production in ATXN3/Q75 cells. Lactulose 11-20 ataxin 3 Homo sapiens 81-86 26295831-4 2016 Meanwhile, lactulose and melibiose reduced reactive oxygen species production in ATXN3/Q75 cells. Melibiose 25-34 ataxin 3 Homo sapiens 81-86 26295831-4 2016 Meanwhile, lactulose and melibiose reduced reactive oxygen species production in ATXN3/Q75 cells. Reactive Oxygen Species 43-66 ataxin 3 Homo sapiens 81-86 26467707-4 2016 Here we show that overexpression of cystathionine gamma-lyase, a central enzyme in cysteine metabolism, is protective in a Drosophila model for SCA3. Cysteine 83-91 ataxin 3 Homo sapiens 144-148 26538519-0 2015 How Epigallocatechin-3-gallate and Tetracycline Interact with the Josephin Domain of Ataxin-3 and Alter Its Aggregation Mode. epigallocatechin gallate 4-30 ataxin 3 Homo sapiens 85-93 26538519-0 2015 How Epigallocatechin-3-gallate and Tetracycline Interact with the Josephin Domain of Ataxin-3 and Alter Its Aggregation Mode. Tetracycline 35-47 ataxin 3 Homo sapiens 85-93 26538519-3 2015 We previously showed that EGCG and tetracycline can contrast the aggregation process and toxicity of expanded AT3, although by different mechanisms. epigallocatechin gallate 26-30 ataxin 3 Homo sapiens 110-113 26538519-3 2015 We previously showed that EGCG and tetracycline can contrast the aggregation process and toxicity of expanded AT3, although by different mechanisms. Tetracycline 35-47 ataxin 3 Homo sapiens 110-113 26538519-5 2015 By protein solubility assays and FTIR spectroscopy we have first observed that EGCG and tetracycline affect the JD aggregation essentially in the same way displayed when acting on the full-length expanded AT3. epigallocatechin gallate 79-83 ataxin 3 Homo sapiens 205-208 26538519-5 2015 By protein solubility assays and FTIR spectroscopy we have first observed that EGCG and tetracycline affect the JD aggregation essentially in the same way displayed when acting on the full-length expanded AT3. Tetracycline 88-100 ataxin 3 Homo sapiens 205-208 26538519-8 2015 Our investigations provide new details on the JD interaction with EGCG and tetracycline, which could explain the different mechanisms by which the two compounds reduce the toxicity of AT3. epigallocatechin gallate 66-70 ataxin 3 Homo sapiens 184-187 26538519-8 2015 Our investigations provide new details on the JD interaction with EGCG and tetracycline, which could explain the different mechanisms by which the two compounds reduce the toxicity of AT3. Tetracycline 75-87 ataxin 3 Homo sapiens 184-187 26297649-1 2015 BACKGROUND: In a recent phase 2 clinical trial in spinocerebellar ataxia type 3/Machado Joseph disease (SCA3/MJD), a neurogenetic disorder without specific therapy, benefits of lithium carbonate were found only on secondary efficacy outcomes, all related to ataxic features. Lithium Carbonate 177-194 ataxin 3 Homo sapiens 104-108 26808260-0 2016 Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone. polyglutamine 76-89 ataxin 3 Homo sapiens 99-107 26745628-7 2016 Findings of our in silico study strongly point to the closed-like conformation as the most likely for a Josephin Domain in water. Water 123-128 ataxin 3 Homo sapiens 104-112 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. trinucleotide 120-133 ataxin 3 Homo sapiens 26-30 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. trinucleotide 120-133 ataxin 3 Homo sapiens 164-169 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. polyglutamine 201-214 ataxin 3 Homo sapiens 26-30 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. polyglutamine 201-214 ataxin 3 Homo sapiens 164-169 27847820-1 2016 Spinocerebellar ataxia-3 (SCA3) is the most common dominant inherited ataxia worldwide and is caused by an unstable CAG trinucleotide expansion mutation within the ATXN3 gene, resulting in an expanded polyglutamine tract within the ATXN3 protein. polyglutamine 201-214 ataxin 3 Homo sapiens 232-237 27847820-6 2016 Furthermore, we demonstrated that neural differentiation in these iPS cells was accompanied by autophagy and that rapamycin promoted autophagy through degradation of mutant ATXN3 proteins in neurally differentiated spinocerebellar ataxia-3 human induced pluripotent stem cells (p < 0.05). Sirolimus 114-123 ataxin 3 Homo sapiens 173-178 26260925-5 2015 Here, we establish that polyglutamine expansion increases the molecular mobility of two juxtaposed helices critical to ataxin-3 deubiquitinase activity. polyglutamine 24-37 ataxin 3 Homo sapiens 119-127 26123252-1 2015 Machado-Joseph disease (MJD, also known as spinocerebellar ataxia type 3, SCA3), an autosomal dominant neurological disorder, is caused by an abnormal expanded polyglutamine (polyQ) repeat in the ataxin-3 protein. polyglutamine 160-173 ataxin 3 Homo sapiens 196-204 26073430-1 2015 BACKGROUND: Machado-Joseph Disease (MJD), a form of dominantly inherited ataxia belonging to the group of polyQ expansion neurodegenerative disorders, occurs when a threshold value for the number of glutamines in Ataxin-3 (Atx3) polyglutamine region is exceeded. Glutamine 199-209 ataxin 3 Homo sapiens 213-221 26073430-1 2015 BACKGROUND: Machado-Joseph Disease (MJD), a form of dominantly inherited ataxia belonging to the group of polyQ expansion neurodegenerative disorders, occurs when a threshold value for the number of glutamines in Ataxin-3 (Atx3) polyglutamine region is exceeded. Glutamine 199-209 ataxin 3 Homo sapiens 223-227 26073430-1 2015 BACKGROUND: Machado-Joseph Disease (MJD), a form of dominantly inherited ataxia belonging to the group of polyQ expansion neurodegenerative disorders, occurs when a threshold value for the number of glutamines in Ataxin-3 (Atx3) polyglutamine region is exceeded. polyglutamine 229-242 ataxin 3 Homo sapiens 213-221 26073430-5 2015 RESULTS: We demonstrate that Atx3 is SUMOylated at K356 both in vitro and in cells, which contributes for decreased formation of amyloid fibrils and for increased affinity towards p97. potassium iodate 51-55 ataxin 3 Homo sapiens 29-33 26123252-1 2015 Machado-Joseph disease (MJD, also known as spinocerebellar ataxia type 3, SCA3), an autosomal dominant neurological disorder, is caused by an abnormal expanded polyglutamine (polyQ) repeat in the ataxin-3 protein. polyglutamine 175-180 ataxin 3 Homo sapiens 196-204 26266536-9 2015 Based on these data and other related studies, we presumed that de novo mutations of ATXN3 emerging from large ANs are at least one survival mechanisms of mutational ATXN3 and we can redefine the range of CAG repeats as: ANs<=44, 45 <=AIs <=49 and AEs>=50. 1-anilino-8-naphthalenesulfonate 111-114 ataxin 3 Homo sapiens 85-90 26266536-9 2015 Based on these data and other related studies, we presumed that de novo mutations of ATXN3 emerging from large ANs are at least one survival mechanisms of mutational ATXN3 and we can redefine the range of CAG repeats as: ANs<=44, 45 <=AIs <=49 and AEs>=50. 1-anilino-8-naphthalenesulfonate 111-114 ataxin 3 Homo sapiens 166-171 26266536-9 2015 Based on these data and other related studies, we presumed that de novo mutations of ATXN3 emerging from large ANs are at least one survival mechanisms of mutational ATXN3 and we can redefine the range of CAG repeats as: ANs<=44, 45 <=AIs <=49 and AEs>=50. 1-anilino-8-naphthalenesulfonate 221-224 ataxin 3 Homo sapiens 85-90 26266536-9 2015 Based on these data and other related studies, we presumed that de novo mutations of ATXN3 emerging from large ANs are at least one survival mechanisms of mutational ATXN3 and we can redefine the range of CAG repeats as: ANs<=44, 45 <=AIs <=49 and AEs>=50. 1-anilino-8-naphthalenesulfonate 221-224 ataxin 3 Homo sapiens 166-171 26037349-7 2015 Wide type and polyQ-expanded ataxin-3 both showed partial co-localization with ER marker calnexin. polyglutamine 14-19 ataxin 3 Homo sapiens 29-37 26710806-3 2015 The CAG trinucleotide repeats in SCA3 gene in each sample were amplified by polymerase chain reaction (PCR), denaturing polyacrylamide gel electrophoresis and silver staining techniques. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 4-7 ataxin 3 Homo sapiens 33-37 26710806-3 2015 The CAG trinucleotide repeats in SCA3 gene in each sample were amplified by polymerase chain reaction (PCR), denaturing polyacrylamide gel electrophoresis and silver staining techniques. trinucleotide 8-21 ataxin 3 Homo sapiens 33-37 26710806-3 2015 The CAG trinucleotide repeats in SCA3 gene in each sample were amplified by polymerase chain reaction (PCR), denaturing polyacrylamide gel electrophoresis and silver staining techniques. polyacrylamide 120-134 ataxin 3 Homo sapiens 33-37 26710806-3 2015 The CAG trinucleotide repeats in SCA3 gene in each sample were amplified by polymerase chain reaction (PCR), denaturing polyacrylamide gel electrophoresis and silver staining techniques. Silver 159-165 ataxin 3 Homo sapiens 33-37 26018079-4 2015 In the present study, we first established a HEK293 cell line, which stably expresses a fluorescent peroxisome marker protein (DsRed2-Peroxi) and expresses PLA/AT-3 in a tetracycline-dependent manner. Tetracycline 170-182 ataxin 3 Homo sapiens 160-164 26018079-9 2015 Immunoprecipitation analysis showed that PLA/AT-3 binds to Pex19p through its N-terminal proline-rich and C-terminal hydrophobic domains. Proline 89-96 ataxin 3 Homo sapiens 45-49 26037349-9 2015 CONCLUSION: PolyQ-expanded ataxin-3 protein may indirectly affect the integrity of mitochondria, but may cause no effect on the structure and functions of golgi apparatus. polyglutamine 12-17 ataxin 3 Homo sapiens 27-35 25179684-0 2014 Natural compounds against neurodegenerative diseases: molecular characterization of the interaction of catechins from green tea with Abeta1-42, PrP106-126, and ataxin-3 oligomers. Catechin 103-112 ataxin 3 Homo sapiens 160-168 25006867-1 2015 The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). polyglutamine 19-32 ataxin 3 Homo sapiens 55-62 25006867-1 2015 The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). polyglutamine 19-32 ataxin 3 Homo sapiens 70-99 25006867-1 2015 The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). polyglutamine 19-32 ataxin 3 Homo sapiens 101-105 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 146-151 ataxin 3 Homo sapiens 25-30 25700012-3 2015 To complicate matters further, several of the polyglutamine-disease related proteins, including ataxin-3, have a multistage aggregation mechanism in which flanking domain self-assembly precedes polyglutamine aggregation yet is influenced by polyglutamine expansion. polyglutamine 46-59 ataxin 3 Homo sapiens 96-104 25700012-6 2015 We show that the conformational dynamics of the flanking Josephin domain in ataxin-3 with an expanded polyglutamine tract are altered in comparison to those exhibited by its nonexpanded counterpart, specifically within the aggregation-prone region of the Josephin domain (amino acid residues 73-96). polyglutamine 102-115 ataxin 3 Homo sapiens 76-84 25700012-7 2015 Expansion thus exposes this region more frequently in ataxin-3 containing an expanded polyglutamine tract, providing a molecular explanation of why aggregation is accelerated upon polyglutamine expansion. polyglutamine 86-99 ataxin 3 Homo sapiens 54-62 25700012-7 2015 Expansion thus exposes this region more frequently in ataxin-3 containing an expanded polyglutamine tract, providing a molecular explanation of why aggregation is accelerated upon polyglutamine expansion. polyglutamine 180-193 ataxin 3 Homo sapiens 54-62 25700012-11 2015 Overall, the results enable the effect of polyglutamine expansion on every stage of ataxin-3 self-assembly, from monomer through to fibril, to be described and a rationale for expedited aggregation upon polyglutamine expansion to be provided. polyglutamine 42-55 ataxin 3 Homo sapiens 84-92 25866756-2 2015 Both levodopa responsive Parkinson disease (PD) like phenotype and atypical parkinsonism have been described especially in SCA2, SCA3, and SCA17 with geographic differences in prevalence. Levodopa 5-13 ataxin 3 Homo sapiens 129-133 25068645-5 2014 Treatment with valproic acid, a histone deacetylase inhibitor (HDACi), attenuated mutant ataxin-3-induced cell toxicity and suppression of acetyl histone H3, phosphorylated cAMP-responsive element binding protein (p-CREB) as well as c-Fos expression. Cyclic AMP 173-177 ataxin 3 Homo sapiens 89-97 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 131-144 ataxin 3 Homo sapiens 15-23 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 131-144 ataxin 3 Homo sapiens 25-30 25700012-0 2015 Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion. polyglutamine 146-151 ataxin 3 Homo sapiens 15-23 25988170-4 2015 However, specific ubiquitination at lysine 117 in the Josephin domain activates ataxin-3 through an unknown mechanism. Lysine 36-42 ataxin 3 Homo sapiens 80-88 25574208-2 2015 Blood samples were obtained from the family, and mutations in the gene causing spinocerebellar ataxia type 3 (SCA3)/Machado-Joseph disease (MJD), known as MJD1, were analyzed using the polymerase chain reaction, 8% denaturing polyacrylamide gel electrophoresis, and T-vector ligation and sequencing. polyacrylamide 226-240 ataxin 3 Homo sapiens 79-108 25574208-2 2015 Blood samples were obtained from the family, and mutations in the gene causing spinocerebellar ataxia type 3 (SCA3)/Machado-Joseph disease (MJD), known as MJD1, were analyzed using the polymerase chain reaction, 8% denaturing polyacrylamide gel electrophoresis, and T-vector ligation and sequencing. polyacrylamide 226-240 ataxin 3 Homo sapiens 155-159 25451224-0 2014 miR-25 alleviates polyQ-mediated cytotoxicity by silencing ATXN3. polyglutamine 18-23 ataxin 3 Homo sapiens 59-64 25068645-5 2014 Treatment with valproic acid, a histone deacetylase inhibitor (HDACi), attenuated mutant ataxin-3-induced cell toxicity and suppression of acetyl histone H3, phosphorylated cAMP-responsive element binding protein (p-CREB) as well as c-Fos expression. Valproic Acid 15-28 ataxin 3 Homo sapiens 89-97 25179684-1 2014 By combining NMR spectroscopy, transmission electron microscopy, and circular dichroism we have identified the structural determinants involved in the interaction of green tea catechins with Abeta1-42, PrP106-126, and ataxin-3 oligomers. Catechin 176-185 ataxin 3 Homo sapiens 218-226 25268243-1 2014 Spinocerebellar ataxia (SCA) 3, the most common form of SCA, is a neurodegenerative rare disease characterized by polyglutamine tract expansion and self-assembly of Ataxin3 (At3) misfolded proteins into highly organized fibrillar aggregates. polyglutamine 114-127 ataxin 3 Homo sapiens 0-30 24293103-2 2014 The C-terminus of the ataxin-3 protein contains a polyglutamine (PolyQ) region that, when mutationally expanded to over 52 glutamines, causes the neurodegenerative disease spinocerebellar ataxia 3 (SCA3). polyglutamine 65-70 ataxin 3 Homo sapiens 22-30 25158237-0 2014 p62/sequestosome 1 regulates aggresome formation of pathogenic ataxin-3 with expanded polyglutamine. polyglutamine 86-99 ataxin 3 Homo sapiens 63-71 25158237-4 2014 In this study we demonstrate that p62 directly interacts with pathogenic Machado Joseph Disease (MJD)-associated protein ataxin-3 with polyglutamine (polyQ) expansion. polyglutamine 135-148 ataxin 3 Homo sapiens 121-129 25158237-4 2014 In this study we demonstrate that p62 directly interacts with pathogenic Machado Joseph Disease (MJD)-associated protein ataxin-3 with polyglutamine (polyQ) expansion. polyglutamine 150-155 ataxin 3 Homo sapiens 121-129 23617879-1 2014 AIMS: Spinocerebellar ataxia type 3 (SCA3) is an inherited spinocerebellar ataxia caused by the expansion of trinucleotide CAG repeats in the gene encoding ataxin-3. trinucleotide 109-122 ataxin 3 Homo sapiens 6-35 23617879-1 2014 AIMS: Spinocerebellar ataxia type 3 (SCA3) is an inherited spinocerebellar ataxia caused by the expansion of trinucleotide CAG repeats in the gene encoding ataxin-3. trinucleotide 109-122 ataxin 3 Homo sapiens 37-41 23617879-1 2014 AIMS: Spinocerebellar ataxia type 3 (SCA3) is an inherited spinocerebellar ataxia caused by the expansion of trinucleotide CAG repeats in the gene encoding ataxin-3. trinucleotide 109-122 ataxin 3 Homo sapiens 156-164 24675225-5 2014 In this study, we demonstrate the aggregate-inhibitory effect of Glycyrrhiza inflata herb extract and its constituents licochalcone A and ammonium glycyrrhizinate (AMGZ) in both 293 and SH-SY5Y ATXN3/Q75 cells, SCA3 cell models. AMMONIUM GLYCYRRHIZINATE 138-162 ataxin 3 Homo sapiens 194-199 24675225-5 2014 In this study, we demonstrate the aggregate-inhibitory effect of Glycyrrhiza inflata herb extract and its constituents licochalcone A and ammonium glycyrrhizinate (AMGZ) in both 293 and SH-SY5Y ATXN3/Q75 cells, SCA3 cell models. AMMONIUM GLYCYRRHIZINATE 164-168 ataxin 3 Homo sapiens 194-199 24675225-7 2014 G. inflata extract, licochalcone A, and AMGZ upregulated PPARGC1A expression and its downstream target genes, SOD2 and CYCS, in the 293 ATXN3/Q75 cell model. inflata extract 3-18 ataxin 3 Homo sapiens 136-141 24675225-7 2014 G. inflata extract, licochalcone A, and AMGZ upregulated PPARGC1A expression and its downstream target genes, SOD2 and CYCS, in the 293 ATXN3/Q75 cell model. licochalcone A 20-34 ataxin 3 Homo sapiens 136-141 24675225-7 2014 G. inflata extract, licochalcone A, and AMGZ upregulated PPARGC1A expression and its downstream target genes, SOD2 and CYCS, in the 293 ATXN3/Q75 cell model. AMMONIUM GLYCYRRHIZINATE 40-44 ataxin 3 Homo sapiens 136-141 24675225-10 2014 G. inflata extract and its constituents significantly elevated GSH/GSSG ratio and reduced reactive oxidative species in ATXN3/Q75 cells. inflata extract 3-18 ataxin 3 Homo sapiens 120-125 25231079-0 2014 Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology. polyglutamine 15-28 ataxin 3 Homo sapiens 38-46 25231079-3 2014 We found that the aggregates formed by polyQ-expanded Atx3 sequester its interacting partners, such as P97/VCP and ubiquitin conjugates, into the protein inclusions through specific interactions both in vitro and in cells. polyglutamine 39-44 ataxin 3 Homo sapiens 54-58 25231079-5 2014 However, expansion of polyQ tract in Atx3 does not alter the conformation of its surrounding regions and the interaction affinities with the interacting partners, although it indeed facilitates misfolding and aggregation of the Atx3 protein. polyglutamine 22-27 ataxin 3 Homo sapiens 37-41 25231079-5 2014 However, expansion of polyQ tract in Atx3 does not alter the conformation of its surrounding regions and the interaction affinities with the interacting partners, although it indeed facilitates misfolding and aggregation of the Atx3 protein. polyglutamine 22-27 ataxin 3 Homo sapiens 228-232 25144244-1 2014 Polyglutamine repeat expansion in ataxin-3 causes neurodegeneration in the most common dominant ataxia, spinocerebellar ataxia type 3 (SCA3). polyglutamine 0-13 ataxin 3 Homo sapiens 34-42 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 124-137 ataxin 3 Homo sapiens 0-8 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 124-137 ataxin 3 Homo sapiens 10-13 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 139-144 ataxin 3 Homo sapiens 0-8 24685680-1 2014 Ataxin-3 (AT3) is the protein that triggers the inherited neurodegenerative disorder spinocerebellar ataxia type 3 when its polyglutamine (polyQ) stretch close to the C-terminus exceeds a critical length. polyglutamine 139-144 ataxin 3 Homo sapiens 10-13 24293103-2 2014 The C-terminus of the ataxin-3 protein contains a polyglutamine (PolyQ) region that, when mutationally expanded to over 52 glutamines, causes the neurodegenerative disease spinocerebellar ataxia 3 (SCA3). polyglutamine 65-70 ataxin 3 Homo sapiens 198-202 24293103-2 2014 The C-terminus of the ataxin-3 protein contains a polyglutamine (PolyQ) region that, when mutationally expanded to over 52 glutamines, causes the neurodegenerative disease spinocerebellar ataxia 3 (SCA3). Glutamine 123-133 ataxin 3 Homo sapiens 22-30 24293103-2 2014 The C-terminus of the ataxin-3 protein contains a polyglutamine (PolyQ) region that, when mutationally expanded to over 52 glutamines, causes the neurodegenerative disease spinocerebellar ataxia 3 (SCA3). Glutamine 123-133 ataxin 3 Homo sapiens 198-202 24293103-5 2014 Instead, the soluble PolyQ containing fragments arising from proteolytic cleavage of ataxin-3 by caspases and calpains are now regarded to be of greater influence in pathogenesis. polyglutamine 21-26 ataxin 3 Homo sapiens 85-93 24418350-16 2014 Also, varenicline for SCA3 patients (level B) can be considered. Varenicline 6-17 ataxin 3 Homo sapiens 22-26 24486383-3 2014 Here we show the anti-aggregation potential of Gardenia jasminoides (G. jasminoides) and its components/metabolite geniposide, crocin, and genipin, in ATXN3/Q75-GFP 293 cells, a putative SCA3 cell model. geniposide 115-125 ataxin 3 Homo sapiens 151-156 24486383-3 2014 Here we show the anti-aggregation potential of Gardenia jasminoides (G. jasminoides) and its components/metabolite geniposide, crocin, and genipin, in ATXN3/Q75-GFP 293 cells, a putative SCA3 cell model. geniposide 115-125 ataxin 3 Homo sapiens 187-191 24486383-3 2014 Here we show the anti-aggregation potential of Gardenia jasminoides (G. jasminoides) and its components/metabolite geniposide, crocin, and genipin, in ATXN3/Q75-GFP 293 cells, a putative SCA3 cell model. crocin 127-133 ataxin 3 Homo sapiens 151-156 24486383-3 2014 Here we show the anti-aggregation potential of Gardenia jasminoides (G. jasminoides) and its components/metabolite geniposide, crocin, and genipin, in ATXN3/Q75-GFP 293 cells, a putative SCA3 cell model. genipin 139-146 ataxin 3 Homo sapiens 151-156 24196352-5 2013 Inhibiting Atx3 with eeyarestatin-I did not affect D2:p97 binding but decreased UbD2 retrotranslocation and caused ER accumulation of high-molecular weight UbD2 bands possibly by interfering with the D2-ubiquitin-specific peptidases binding. 1-(4-chlorophenyl)-3-(3-(4-chlorophenyl)-5,5-dimethyl-1-(3-(5-nitrofuran-2-yl)allyldienehydrazinocarbonylmethyl)-2-oxoimidazolidin-4-yl)-1-hydroxyurea 21-35 ataxin 3 Homo sapiens 11-15 24266403-3 2013 Here we test how UNA substitutions affect allele-selective inhibition of expression of trinucleotide repeat genes Huntingtin (HTT) and Ataxin-3 (ATX-3). trinucleotide 87-100 ataxin 3 Homo sapiens 145-150 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. Oxygen 129-135 ataxin 3 Homo sapiens 82-90 24266403-3 2013 Here we test how UNA substitutions affect allele-selective inhibition of expression of trinucleotide repeat genes Huntingtin (HTT) and Ataxin-3 (ATX-3). trinucleotide 87-100 ataxin 3 Homo sapiens 135-143 23659897-1 2013 Spinocerebellar ataxia type 3 is caused by a polyglutamine expansion in the ataxin-3 protein, resulting in gain of toxic function of the mutant protein. polyglutamine 45-58 ataxin 3 Homo sapiens 76-84 24251111-5 2013 Here, we report on the production of milligrams of highly pure Josephin mono-ubiquitinated on lysine 117 through large scale in vitro enzymatic ubiquitination. Lysine 94-100 ataxin 3 Homo sapiens 63-71 23659897-2 2013 The expanded glutamine stretch in the protein is the result of a CAG triplet repeat expansion in the penultimate exon of the ATXN3 gene. Glutamine 13-22 ataxin 3 Homo sapiens 125-130 23659897-4 2013 Here, we propose a novel protein modification approach to reduce mutant ataxin-3 toxicity by removing the toxic polyglutamine repeat from the ataxin-3 protein through antisense oligonucleotide-mediated exon skipping while maintaining important wild type functions of the protein. polyglutamine 112-125 ataxin 3 Homo sapiens 72-80 23659897-4 2013 Here, we propose a novel protein modification approach to reduce mutant ataxin-3 toxicity by removing the toxic polyglutamine repeat from the ataxin-3 protein through antisense oligonucleotide-mediated exon skipping while maintaining important wild type functions of the protein. polyglutamine 112-125 ataxin 3 Homo sapiens 142-150 23659897-4 2013 Here, we propose a novel protein modification approach to reduce mutant ataxin-3 toxicity by removing the toxic polyglutamine repeat from the ataxin-3 protein through antisense oligonucleotide-mediated exon skipping while maintaining important wild type functions of the protein. Oligonucleotides 177-192 ataxin 3 Homo sapiens 72-80 23659897-4 2013 Here, we propose a novel protein modification approach to reduce mutant ataxin-3 toxicity by removing the toxic polyglutamine repeat from the ataxin-3 protein through antisense oligonucleotide-mediated exon skipping while maintaining important wild type functions of the protein. Oligonucleotides 177-192 ataxin 3 Homo sapiens 142-150 23562578-0 2013 Ataxin-3 protects cells against H2O2-induced oxidative stress by enhancing the interaction between Bcl-X(L) and Bax. Hydrogen Peroxide 32-36 ataxin 3 Homo sapiens 0-8 23894474-0 2013 Conformational behavior and aggregation of ataxin-3 in SDS. Sodium Dodecyl Sulfate 55-58 ataxin 3 Homo sapiens 43-51 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 52-65 ataxin 3 Homo sapiens 0-29 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 52-65 ataxin 3 Homo sapiens 31-35 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 67-72 ataxin 3 Homo sapiens 0-29 23894474-1 2013 Spinocerebellar ataxia type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases all characterized by the presence of intraneuronal inclusions that contain aggregated protein. polyglutamine 67-72 ataxin 3 Homo sapiens 31-35 23894474-6 2013 We have characterized the effects of the membrane mimetic sodium dodecyl sulfate (SDS) on ataxin-3 structure and aggregation, to show that both micellar and non-micellar SDS have differing effects on the two stages of ataxin-3 aggregation. Sodium Dodecyl Sulfate 58-80 ataxin 3 Homo sapiens 90-98 23894474-6 2013 We have characterized the effects of the membrane mimetic sodium dodecyl sulfate (SDS) on ataxin-3 structure and aggregation, to show that both micellar and non-micellar SDS have differing effects on the two stages of ataxin-3 aggregation. Sodium Dodecyl Sulfate 82-85 ataxin 3 Homo sapiens 90-98 23894474-6 2013 We have characterized the effects of the membrane mimetic sodium dodecyl sulfate (SDS) on ataxin-3 structure and aggregation, to show that both micellar and non-micellar SDS have differing effects on the two stages of ataxin-3 aggregation. Sodium Dodecyl Sulfate 170-173 ataxin 3 Homo sapiens 218-226 23894474-7 2013 We also demonstrate that fibrillar ataxin-3 binds phospholipids, in particular phosphorylated phosphotidylinositols. Phospholipids 50-63 ataxin 3 Homo sapiens 35-43 23894474-7 2013 We also demonstrate that fibrillar ataxin-3 binds phospholipids, in particular phosphorylated phosphotidylinositols. phosphotidylinositols 94-115 ataxin 3 Homo sapiens 35-43 23894474-8 2013 These results highlight the effect of intracellular factors on the ataxin-3 misfolding landscape and their implications in SCA3 and polyQ diseases in general are discussed. polyglutamine 132-137 ataxin 3 Homo sapiens 67-75 23562578-1 2013 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder associated with polyglutamine (polyQ) protein ataxin-3. polyglutamine 85-98 ataxin 3 Homo sapiens 0-29 23562578-1 2013 Spinocerebellar ataxia type 3 (SCA3) is a neurodegenerative disorder associated with polyglutamine (polyQ) protein ataxin-3. polyglutamine 85-98 ataxin 3 Homo sapiens 115-123 23562578-3 2013 Here we demonstrate that ataxin-3 plays a protective role against cellular oxidative stress induced by H2O2 in a Bcl-XL-dependent manner. Hydrogen Peroxide 103-107 ataxin 3 Homo sapiens 25-33 25844046-6 2013 The C-terminal region of ataxin-3 which contains the glutamine-rich sequences is largely unstructured, showing little resistance to limited proteolysis. Glutamine 53-62 ataxin 3 Homo sapiens 25-33 25317135-4 2012 Gene analysis showed abnormal amplification of the CAG trinucleotide repeat in exon 10 of the ataxin-3 (ATXN3) gene, resulting in 70-81 CAG repeats in the patient, with a significant positive family history. trinucleotide 55-68 ataxin 3 Homo sapiens 94-102 23382880-0 2013 SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity. polyglutamine 31-36 ataxin 3 Homo sapiens 46-54 23382880-2 2013 Spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD) is an autosomal dominant neurodegenerative disease caused by polyQ-expanded ataxin-3. polyglutamine 125-130 ataxin 3 Homo sapiens 140-148 25317135-4 2012 Gene analysis showed abnormal amplification of the CAG trinucleotide repeat in exon 10 of the ataxin-3 (ATXN3) gene, resulting in 70-81 CAG repeats in the patient, with a significant positive family history. trinucleotide 55-68 ataxin 3 Homo sapiens 104-109 22133674-1 2012 Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is the most common inherited spinocerebellar ataxia and one of many polyglutamine neurodegenerative diseases. polyglutamine 150-163 ataxin 3 Homo sapiens 44-73 23135006-8 2012 Artesunate tablet AT2 failed the uniformity of mass test while artesunate tablets AT3 & AT4 as well as amodiaquine tablets AM4 & AM6 failed the crushing strength test. Artesunate 63-73 ataxin 3 Homo sapiens 82-85 22337953-4 2012 Conversely, transgenic expression of polyglutamine-encoding (exp)CAA ATXN3 was not toxic. polyglutamine 37-50 ataxin 3 Homo sapiens 69-74 22133674-1 2012 Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), is the most common inherited spinocerebellar ataxia and one of many polyglutamine neurodegenerative diseases. polyglutamine 150-163 ataxin 3 Homo sapiens 75-79 22133674-2 2012 In MJD, a CAG repeat expansion encodes an abnormally long polyglutamine (polyQ) tract in the disease protein, ATXN3. polyglutamine 58-71 ataxin 3 Homo sapiens 110-115 22133674-2 2012 In MJD, a CAG repeat expansion encodes an abnormally long polyglutamine (polyQ) tract in the disease protein, ATXN3. polyglutamine 73-78 ataxin 3 Homo sapiens 110-115 22133674-6 2012 Expansion of the polyQ tract in ATXN3 is thought to promote an altered conformation in the protein, leading to changes in interactions with native partners and to the formation of insoluble aggregates. polyglutamine 17-22 ataxin 3 Homo sapiens 32-37 22133674-7 2012 The development of a wide range of cellular and animal models of MJD has been crucial to the emerging understanding of ATXN3 dysfunction upon polyQ expansion. polyglutamine 142-147 ataxin 3 Homo sapiens 119-124 21740957-0 2011 Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease. polyglutamine 0-13 ataxin 3 Homo sapiens 44-52 22081612-3 2012 Moreover, ataxin-3-dependent deubiquitination of parkin required the catalytic cysteine 14 in ataxin-3, although the precise mechanism remained unclear. Cysteine 79-87 ataxin 3 Homo sapiens 10-18 22081612-3 2012 Moreover, ataxin-3-dependent deubiquitination of parkin required the catalytic cysteine 14 in ataxin-3, although the precise mechanism remained unclear. Cysteine 79-87 ataxin 3 Homo sapiens 94-102 22113611-1 2011 Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of polyglutamine (polyQ)-encoding CAG repeats in the MJD1 gene (also known as ATXN3). polyglutamine 159-172 ataxin 3 Homo sapiens 209-213 22113611-1 2011 Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of polyglutamine (polyQ)-encoding CAG repeats in the MJD1 gene (also known as ATXN3). polyglutamine 174-179 ataxin 3 Homo sapiens 209-213 22113611-1 2011 Machado-Joseph disease (MJD; also called spinocerebellar ataxia type 3) is a dominantly inherited late-onset neurodegenerative disorder caused by expansion of polyglutamine (polyQ)-encoding CAG repeats in the MJD1 gene (also known as ATXN3). polyglutamine 174-179 ataxin 3 Homo sapiens 234-239 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 103-107 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 121-129 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 131-136 22113611-2 2011 Proteolytic liberation of highly aggregation-prone polyQ fragments from the protective sequence of the MJD1 gene product ataxin 3 (ATXN3) has been proposed to trigger the formation of ATXN3-containing aggregates, the neuropathological hallmark of MJD. polyglutamine 51-56 ataxin 3 Homo sapiens 184-189 22113611-5 2011 Here we show that L-glutamate-induced excitation of patient-specific induced pluripotent stem cell (iPSC)-derived neurons initiates Ca(2+)-dependent proteolysis of ATXN3 followed by the formation of SDS-insoluble aggregates. Glutamic Acid 18-29 ataxin 3 Homo sapiens 164-169 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 67-72 ataxin 3 Homo sapiens 31-35 22234302-1 2012 Ataxin-3 (AT3) triggers spinocerebellar ataxia type 3 when it carries a polyglutamine stretch expanded beyond a critical threshold. polyglutamine 72-85 ataxin 3 Homo sapiens 0-8 22234302-1 2012 Ataxin-3 (AT3) triggers spinocerebellar ataxia type 3 when it carries a polyglutamine stretch expanded beyond a critical threshold. polyglutamine 72-85 ataxin 3 Homo sapiens 10-13 22323747-1 2012 OBJECTIVE: The objective of this double-blind, placebo-controlled, randomized study was to evaluate the efficacy of varenicline (Chantix), a partial agonist at alpha4beta2 neuronal nicotinic acetylcholine receptors used for smoking cessation, in patients with spinocerebellar ataxia (SCA) 3. Varenicline 116-127 ataxin 3 Homo sapiens 260-290 21827905-3 2012 Like many other dominantly inherited ataxias, MJD/SCA3 shows remarkable clinical heterogeneity, reflecting the underlying genetic defect: an unstable CAG trinucleotide repeat that varies in size among affected persons. trinucleotide 154-167 ataxin 3 Homo sapiens 50-54 21827905-4 2012 This pathogenic repeat in MJD/SCA3 encodes an expanded tract of the amino acid glutamine in the disease protein, which is known as ataxin-3. Glutamine 79-88 ataxin 3 Homo sapiens 30-34 21827905-4 2012 This pathogenic repeat in MJD/SCA3 encodes an expanded tract of the amino acid glutamine in the disease protein, which is known as ataxin-3. Glutamine 79-88 ataxin 3 Homo sapiens 131-139 21827905-5 2012 MJD/SCA3 is one of nine identified polyglutamine neurodegenerative diseases which share features of pathogenesis centered on protein misfolding and accumulation. polyglutamine 35-48 ataxin 3 Homo sapiens 4-8 21827905-6 2012 The specific properties of MJD/SCA3 and its disease protein are discussed in light of what is known about the entire class of polyglutamine diseases. polyglutamine 126-139 ataxin 3 Homo sapiens 31-35 22970133-2 2012 Machado-Joseph disease (MJD) or Spinocerebellar Ataxia type 3 is caused by a polyglutamine-encoding CAG expansion in the ATXN3 gene, which encodes a 42 kDa deubiquitinating enzyme (DUB), ataxin-3. polyglutamine 77-90 ataxin 3 Homo sapiens 121-126 22970133-2 2012 Machado-Joseph disease (MJD) or Spinocerebellar Ataxia type 3 is caused by a polyglutamine-encoding CAG expansion in the ATXN3 gene, which encodes a 42 kDa deubiquitinating enzyme (DUB), ataxin-3. polyglutamine 77-90 ataxin 3 Homo sapiens 187-195 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 52-65 ataxin 3 Homo sapiens 0-29 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 52-65 ataxin 3 Homo sapiens 31-35 21780213-1 2011 Spinocerebellar Ataxia Type 3 (SCA3) is one of nine polyglutamine (polyQ) diseases that are all characterized by progressive neuronal dysfunction and the presence of neuronal inclusions containing aggregated polyQ protein, suggesting that protein misfolding is a key part of this disease. polyglutamine 67-72 ataxin 3 Homo sapiens 0-29 21780213-2 2011 Ataxin-3, the causative protein of SCA3, contains a globular, structured N-terminal domain (the Josephin domain) and a flexible polyQ-containing C-terminal tail, the repeat-length of which modulates pathogenicity. polyglutamine 128-133 ataxin 3 Homo sapiens 0-8 21780213-2 2011 Ataxin-3, the causative protein of SCA3, contains a globular, structured N-terminal domain (the Josephin domain) and a flexible polyQ-containing C-terminal tail, the repeat-length of which modulates pathogenicity. polyglutamine 128-133 ataxin 3 Homo sapiens 35-39 21780213-3 2011 It has been suggested that the fibrillogenesis pathway of ataxin-3 begins with a non-polyQ-dependent step mediated by Josephin domain interactions, followed by a polyQ-dependent step. polyglutamine 85-90 ataxin 3 Homo sapiens 58-66 21780213-3 2011 It has been suggested that the fibrillogenesis pathway of ataxin-3 begins with a non-polyQ-dependent step mediated by Josephin domain interactions, followed by a polyQ-dependent step. polyglutamine 162-167 ataxin 3 Homo sapiens 58-66 21780213-6 2011 These data support the hypothesis that the first stage of ataxin-3 fibrillogenesis is caused by interactions involving the non-polyQ containing Josephin domain and that the thermodynamic stability of this domain is linked to the aggregation propensity of ataxin-3. polyglutamine 127-132 ataxin 3 Homo sapiens 58-66 21740957-4 2011 Machado-Joseph disease (MJD), the most common form of spinocerebellar ataxia worldwide, is a progressive and ultimately fatal neurodegenerative disorder caused by polyQ expansion in ataxin-3 (atx3), a conserved and ubiquitous protein known to bind polyubiquitin chains and to function as a deubiquitinating enzyme. polyglutamine 163-168 ataxin 3 Homo sapiens 182-190 21740957-4 2011 Machado-Joseph disease (MJD), the most common form of spinocerebellar ataxia worldwide, is a progressive and ultimately fatal neurodegenerative disorder caused by polyQ expansion in ataxin-3 (atx3), a conserved and ubiquitous protein known to bind polyubiquitin chains and to function as a deubiquitinating enzyme. polyglutamine 163-168 ataxin 3 Homo sapiens 192-196 21740957-7 2011 Expanded atx3 pathogenicity is likely the result of a series of events implicating both atx3 dysfunction and aggregation, possibly involving both full-length atx3 and polyQ-containing fragments that may act as seeds for protein aggregation. polyglutamine 167-172 ataxin 3 Homo sapiens 9-13 21536589-6 2011 In response to oxidative stress, LCs from SCA3 patients show a specific impairment to upregulate SOD2 expression in correlation with a significantly increased formation of reactive oxygen species and cytotoxicity. oxygen species 181-195 ataxin 3 Homo sapiens 42-46 21855799-7 2011 In addition, the results shed light on disease pathogenesis in SCA3, a neurodegenerative disorder caused by polyglutamine expansion in ataxin-3. polyglutamine 108-121 ataxin 3 Homo sapiens 63-67 21855799-7 2011 In addition, the results shed light on disease pathogenesis in SCA3, a neurodegenerative disorder caused by polyglutamine expansion in ataxin-3. polyglutamine 108-121 ataxin 3 Homo sapiens 135-143 20851218-1 2011 Expansion of a polyglutamine tract in ataxin-3 (polyQ) causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation. polyglutamine 15-28 ataxin 3 Homo sapiens 38-46 21743142-5 2011 RESULTS: The ratio of NAA/Cr in SCA3/MJD patients showed a significant reduction in the cerebellar cortex, dentatum, cerebellar vermis and medipeduncle (P<0.01) compared with the controls. N-acetylaspartate 22-25 ataxin 3 Homo sapiens 32-36 21743142-5 2011 RESULTS: The ratio of NAA/Cr in SCA3/MJD patients showed a significant reduction in the cerebellar cortex, dentatum, cerebellar vermis and medipeduncle (P<0.01) compared with the controls. N-acetylaspartate 22-25 ataxin 3 Homo sapiens 37-40 21743142-5 2011 RESULTS: The ratio of NAA/Cr in SCA3/MJD patients showed a significant reduction in the cerebellar cortex, dentatum, cerebellar vermis and medipeduncle (P<0.01) compared with the controls. Creatine 26-28 ataxin 3 Homo sapiens 32-36 21743142-5 2011 RESULTS: The ratio of NAA/Cr in SCA3/MJD patients showed a significant reduction in the cerebellar cortex, dentatum, cerebellar vermis and medipeduncle (P<0.01) compared with the controls. Creatine 26-28 ataxin 3 Homo sapiens 37-40 21533208-0 2011 A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation. polyglutamine 28-41 ataxin 3 Homo sapiens 75-83 21533208-0 2011 A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation. Hydrogen 42-50 ataxin 3 Homo sapiens 75-83 21533208-1 2011 The protein ataxin-3 consists of an N-terminal globular Josephin domain (JD) and an unstructured C-terminal region containing a stretch of consecutive glutamines that triggers the neurodegenerative disorder spinocerebellar ataxia type 3, when it is expanded beyond a critical threshold. Glutamine 151-161 ataxin 3 Homo sapiens 12-20 20810784-4 2011 Ataxin-3, the protein responsible for Spinocerebellar ataxia type 3, a polyglutamine expansion disease, represents one of such examples. polyglutamine 71-84 ataxin 3 Homo sapiens 0-8 20810784-5 2011 Polyglutamine expansion is central for determining solubility and aggregation rates of ataxin-3, but these properties are profoundly modulated by its N-terminal Josephin domain. polyglutamine 0-13 ataxin 3 Homo sapiens 87-95 20810784-5 2011 Polyglutamine expansion is central for determining solubility and aggregation rates of ataxin-3, but these properties are profoundly modulated by its N-terminal Josephin domain. polyglutamine 0-13 ataxin 3 Homo sapiens 161-169 21635785-8 2011 Mutated ATXN3 alleles consensually present about 61 to 87 CAG repeats, resulting in an expanded polyglutamine tract in ataxin-3. polyglutamine 96-109 ataxin 3 Homo sapiens 8-13 21635785-8 2011 Mutated ATXN3 alleles consensually present about 61 to 87 CAG repeats, resulting in an expanded polyglutamine tract in ataxin-3. polyglutamine 96-109 ataxin 3 Homo sapiens 119-127 21504740-3 2011 It was also shown that expanded ataxin-3 aggregates via a two-stage mechanism initially involving Josephin self-association, followed by a polyQ-dependent step. polyglutamine 139-144 ataxin 3 Homo sapiens 32-40 20809346-0 2011 Striatal dopamine function in a family with multiple SCA-3 phenotypes. Dopamine 9-17 ataxin 3 Homo sapiens 53-58 20809346-4 2011 SCA-3 can present with a levodopa responsive parkinsonism phenotype, and an abnormal DAT scan showing predominant impairment of presynaptic dopamine function. Levodopa 25-33 ataxin 3 Homo sapiens 0-5 20851218-1 2011 Expansion of a polyglutamine tract in ataxin-3 (polyQ) causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation. polyglutamine 48-53 ataxin 3 Homo sapiens 38-46 20851218-4 2011 In this study, we used N-terminal-truncated pathogenic ataxin-3 with a 71-glutamine repeat (DeltaNAT-3Q71) and found that MITOL promoted DeltaNAT-3Q71 degradation via the ubiquitin-proteasome pathway and attenuated mitochondrial accumulation of DeltaNAT-3Q71. Glutamine 74-83 ataxin 3 Homo sapiens 55-63 20943656-0 2010 Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117. Lysine 141-147 ataxin 3 Homo sapiens 97-105 20732421-1 2011 The presence of aggregates of abnormally expanded polyglutamine (polyQ)-containing proteins are a pathological hallmark of a number of neurodegenerative diseases including Huntington"s disease (HD) and spinocerebellar ataxia-3 (SCA3). polyglutamine 50-63 ataxin 3 Homo sapiens 228-232 20732421-1 2011 The presence of aggregates of abnormally expanded polyglutamine (polyQ)-containing proteins are a pathological hallmark of a number of neurodegenerative diseases including Huntington"s disease (HD) and spinocerebellar ataxia-3 (SCA3). polyglutamine 65-70 ataxin 3 Homo sapiens 228-232 21909428-6 2011 The most effective antisense oligonucleotide, (CUG)(7), also reduced mutant ataxin-1 and ataxin-3 mRNA levels in spinocerebellar ataxia 1 and 3, respectively, and atrophin-1 in dentatorubral-pallidoluysian atrophy patient derived fibroblasts. Oligonucleotides 29-44 ataxin 3 Homo sapiens 89-97 20943656-3 2010 We identify Lys-117, which resides near the catalytic triad, as the primary site of ubiquitination in wild type and pathogenic ataxin-3. Lysine 12-15 ataxin 3 Homo sapiens 127-135 20943656-4 2010 Further studies indicate that ubiquitin-dependent activation of ataxin-3 at Lys-117 is important for its ability to reduce high molecular weight ubiquitinated species in cells. Lysine 76-79 ataxin 3 Homo sapiens 64-72 20943656-5 2010 Ubiquitination at Lys-117 also facilitates the ability of ataxin-3 to induce aggresome formation in cells. Lysine 18-21 ataxin 3 Homo sapiens 58-66 20943656-6 2010 Finally, structure-function studies support a model of activation whereby ubiquitination at Lys-117 enhances ataxin-3 activity independent of the known ubiquitin-binding sites in ataxin-3, most likely through a direct conformational change in or near the catalytic domain. Lysine 92-95 ataxin 3 Homo sapiens 109-117 20308049-1 2010 Machado-Joseph disease or spinocerebellar ataxia type 3 (MJD/SCA3) is a fatal, autosomal dominant disorder caused by a cytosine-adenine-guanine expansion in the coding region of the MJD1 gene. Cytosine 119-127 ataxin 3 Homo sapiens 57-60 20637808-2 2010 Expansion of a polyglutamine tract in ATXN3 causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation and specific neuronal death. polyglutamine 15-28 ataxin 3 Homo sapiens 38-43 20865150-0 2010 Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3. polyub 53-59 ataxin 3 Homo sapiens 30-38 20865150-0 2010 Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3. polyub 53-59 ataxin 3 Homo sapiens 95-103 20809107-8 2010 Therefore, tandospirone is useful for cerebellar ataxia in patients with MJD and SCA6. tandospirone 11-23 ataxin 3 Homo sapiens 73-76 20829225-7 2010 PSA inhibition also increased the levels of polyQ-expanded ataxin-3 as well as mutant alpha-synuclein and superoxide dismutase 1. polyglutamine 44-49 ataxin 3 Homo sapiens 59-67 20308049-1 2010 Machado-Joseph disease or spinocerebellar ataxia type 3 (MJD/SCA3) is a fatal, autosomal dominant disorder caused by a cytosine-adenine-guanine expansion in the coding region of the MJD1 gene. Adenine 128-136 ataxin 3 Homo sapiens 57-60 20308049-1 2010 Machado-Joseph disease or spinocerebellar ataxia type 3 (MJD/SCA3) is a fatal, autosomal dominant disorder caused by a cytosine-adenine-guanine expansion in the coding region of the MJD1 gene. Guanine 136-143 ataxin 3 Homo sapiens 57-60 20064935-0 2010 Nuclear aggregation of polyglutamine-expanded ataxin-3: fragments escape the cytoplasmic quality control. polyglutamine 23-36 ataxin 3 Homo sapiens 46-54 20334689-4 2010 METHODS: Normal and expanded alleles of ATXN3 were detected via PCR using LA Taq DNA polymerase (better for GC-rich sequences) and denaturing polyacrylamide gel electrophoresis in 150 normal individuals and 138 unrelated probands from autosomal dominant SCA families. polyacrylamide 142-156 ataxin 3 Homo sapiens 40-45 20064935-4 2010 We found that the conserved putative nuclear localization sequence Arg-Lys-Arg-Arg, which is retained in a highly aggregation-prone fragment of ataxin-3, did not affect the site and degree of inclusion formation in a cell culture model of spinocerebellar ataxia type 3. Arginine 67-70 ataxin 3 Homo sapiens 144-152 19843543-1 2010 Spinocerebellar ataxia type 3 (SCA3)/Machado Joseph disease results from expansion of the polyglutamine domain in ataxin-3 (Atx3). polyglutamine 90-103 ataxin 3 Homo sapiens 114-122 20199210-1 2010 We report on a Chinese family with three members who have CAG repeat expansion in the ataxin-3, two members present with expanded trinucleotide repeat in both the ataxin-3 and tata-binding protein (TBP) and an individual who carries expanded CAG/CAA repeat in the TBP. trinucleotide 130-143 ataxin 3 Homo sapiens 163-171 19843543-1 2010 Spinocerebellar ataxia type 3 (SCA3)/Machado Joseph disease results from expansion of the polyglutamine domain in ataxin-3 (Atx3). polyglutamine 90-103 ataxin 3 Homo sapiens 124-128 19843543-7 2010 However, serine-111 of Atx3 was required for nuclear localization of the Josephin domain and regulated nuclear localization of full-length Atx3. Serine 9-15 ataxin 3 Homo sapiens 23-27 19843543-7 2010 However, serine-111 of Atx3 was required for nuclear localization of the Josephin domain and regulated nuclear localization of full-length Atx3. Serine 9-15 ataxin 3 Homo sapiens 139-143 19910924-11 2010 Indeed, HDAC6-dependent reduction of cellular aggregate formation and increased cytotoxicity of polyQ-expanded ataxin-3 were found in TDP-43 silenced cells. polyglutamine 96-101 ataxin 3 Homo sapiens 111-119 20140862-0 2010 [Polyglutamine-expanded ataxin-3 is degraded by autophagy]. polyglutamine 1-14 ataxin 3 Homo sapiens 24-32 20140862-2 2010 METHODS: HEK293 cells expressing polyglutamine-expanded ataxin-3 were used as cell model for SCA3/MJD. polyglutamine 33-46 ataxin 3 Homo sapiens 56-64 20140862-3 2010 The level of polyglutamine-expanded ataxin-3 was detected after cells were treated with different inhibitors or inducer of autophagy. polyglutamine 13-26 ataxin 3 Homo sapiens 36-44 20140862-5 2010 CONCLUSION: The data suggested that autophagy is involved in the degradation of mutant ataxin-3, resulting in a decrease in the proportions of aggregate-containing cells and cell death in HEK293 cells expressing polyglutamine-expanded ataxin-3. polyglutamine 212-225 ataxin 3 Homo sapiens 87-95 20140862-5 2010 CONCLUSION: The data suggested that autophagy is involved in the degradation of mutant ataxin-3, resulting in a decrease in the proportions of aggregate-containing cells and cell death in HEK293 cells expressing polyglutamine-expanded ataxin-3. polyglutamine 212-225 ataxin 3 Homo sapiens 235-243 19811945-3 2010 Current hypotheses regarding pathogenesis favor the view that mutated ataxin-3, with its polyglutamine expansion, is prone to adopt an abnormal conformation, engage in altered protein-protein interactions and aggregate. polyglutamine 89-102 ataxin 3 Homo sapiens 70-78 26023252-6 2009 SCA3 is caused by a polyQ expansion in the carboxy-terminal portion of a cytosolic protein ataxin-3 (Atxn3). polyglutamine 20-25 ataxin 3 Homo sapiens 0-4 19783548-2 2009 Ataxin-3 protein with an expanded polyglutamine (polyQ) repeat causes spinocerebellar ataxia type-3 (SCA3), also called Machado-Joseph disease, and is cleaved in mammalian cells, transgenic mice and SCA3 patient brain tissue. polyglutamine 34-47 ataxin 3 Homo sapiens 0-8 19783548-2 2009 Ataxin-3 protein with an expanded polyglutamine (polyQ) repeat causes spinocerebellar ataxia type-3 (SCA3), also called Machado-Joseph disease, and is cleaved in mammalian cells, transgenic mice and SCA3 patient brain tissue. polyglutamine 49-54 ataxin 3 Homo sapiens 0-8 19713033-3 2009 Similar sized expansions of the CAG trinucleotide repeats in one allele of the ataxin-3 (ATXN3) gene were found in both the patient and his father, although in the other allele the length of the CAG repeats was shorter in the father compared with the patient. trinucleotide 36-49 ataxin 3 Homo sapiens 79-87 19713033-3 2009 Similar sized expansions of the CAG trinucleotide repeats in one allele of the ataxin-3 (ATXN3) gene were found in both the patient and his father, although in the other allele the length of the CAG repeats was shorter in the father compared with the patient. trinucleotide 36-49 ataxin 3 Homo sapiens 89-94 26023252-6 2009 SCA3 is caused by a polyQ expansion in the carboxy-terminal portion of a cytosolic protein ataxin-3 (Atxn3). polyglutamine 20-25 ataxin 3 Homo sapiens 91-99 26023252-6 2009 SCA3 is caused by a polyQ expansion in the carboxy-terminal portion of a cytosolic protein ataxin-3 (Atxn3). polyglutamine 20-25 ataxin 3 Homo sapiens 101-106 26023252-14 2009 These studies also suggested that dantrolene and other Ca2+ signaling inhibitors and stabilizers may have a therapeutic value for treatment of SCA2 and SCA3. Dantrolene 34-44 ataxin 3 Homo sapiens 152-156 19575245-5 2009 After titration with these cations, the AT3 Q36 secondary structure content (27% alpha-helices in the presence of either ion, 31 and 27% beta-sheets for Cu(2+) and Ni(2+), respectively) was similar to that observed for the aggregated form of the protein (27% alpha-helices, 36% beta-sheets). Copper 153-155 ataxin 3 Homo sapiens 40-43 19036964-5 2008 Our results indicate that deranged Ca(2+) signaling may play an important role in SCA3 pathology and that Ca(2+) signaling stabilizers such as dantrolene may be considered as potential therapeutic drugs for treatment of SCA3 patients. Dantrolene 143-153 ataxin 3 Homo sapiens 220-224 19503814-5 2009 In order to characterize the nuclear shuttling activity of Atx3, we performed yeast nuclear import assays and found that Atx3 is actively imported into the nucleus, by means of a classical nuclear localizing sequence formed by a cluster of lysine and arginine residues. Lysine 240-246 ataxin 3 Homo sapiens 59-63 19503814-5 2009 In order to characterize the nuclear shuttling activity of Atx3, we performed yeast nuclear import assays and found that Atx3 is actively imported into the nucleus, by means of a classical nuclear localizing sequence formed by a cluster of lysine and arginine residues. Lysine 240-246 ataxin 3 Homo sapiens 121-125 19503814-5 2009 In order to characterize the nuclear shuttling activity of Atx3, we performed yeast nuclear import assays and found that Atx3 is actively imported into the nucleus, by means of a classical nuclear localizing sequence formed by a cluster of lysine and arginine residues. Arginine 251-259 ataxin 3 Homo sapiens 59-63 19503814-5 2009 In order to characterize the nuclear shuttling activity of Atx3, we performed yeast nuclear import assays and found that Atx3 is actively imported into the nucleus, by means of a classical nuclear localizing sequence formed by a cluster of lysine and arginine residues. Arginine 251-259 ataxin 3 Homo sapiens 121-125 19503814-6 2009 On the other hand, when active nuclear export was inhibited using leptomycin B, a specific inhibitor of the nuclear export receptor CRM1, both endogenous Atx3 and transfected GFP-Atx3 accumulated inside the nucleus of a subpopulation of COS-7 cells, whereas both proteins are normally predominant in the cytoplasm. leptomycin B 66-78 ataxin 3 Homo sapiens 154-158 19503814-6 2009 On the other hand, when active nuclear export was inhibited using leptomycin B, a specific inhibitor of the nuclear export receptor CRM1, both endogenous Atx3 and transfected GFP-Atx3 accumulated inside the nucleus of a subpopulation of COS-7 cells, whereas both proteins are normally predominant in the cytoplasm. leptomycin B 66-78 ataxin 3 Homo sapiens 179-183 19503814-6 2009 On the other hand, when active nuclear export was inhibited using leptomycin B, a specific inhibitor of the nuclear export receptor CRM1, both endogenous Atx3 and transfected GFP-Atx3 accumulated inside the nucleus of a subpopulation of COS-7 cells, whereas both proteins are normally predominant in the cytoplasm. carbonyl sulfide 237-240 ataxin 3 Homo sapiens 154-158 19036964-0 2008 Deranged calcium signaling and neurodegeneration in spinocerebellar ataxia type 3. Calcium 9-16 ataxin 3 Homo sapiens 52-81 19036964-1 2008 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in ataxin-3 (ATX3; MJD1) protein. polyglutamine 146-159 ataxin 3 Homo sapiens 0-29 19036964-1 2008 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in ataxin-3 (ATX3; MJD1) protein. polyglutamine 146-159 ataxin 3 Homo sapiens 31-35 19036964-1 2008 Spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease (MJD), is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in ataxin-3 (ATX3; MJD1) protein. polyglutamine 146-159 ataxin 3 Homo sapiens 173-181 19660550-1 2009 Spinocerebellar ataxia type 3 (SCA3) or Machado-Joseph disease (MJD) belongs to a group of autosomal dominant neurodegenerative diseases, which are caused by the expansion of a polyglutamine repeat in the affected protein, in this case ataxin-3. polyglutamine 177-190 ataxin 3 Homo sapiens 236-244 19672991-4 2009 [(11)C]-CFT PET in detected members in SCA2 and SCA3/MJD families showed decrements of (11)C-CFT uptake. c-cft 91-96 ataxin 3 Homo sapiens 48-52 19672991-4 2009 [(11)C]-CFT PET in detected members in SCA2 and SCA3/MJD families showed decrements of (11)C-CFT uptake. c-cft 91-96 ataxin 3 Homo sapiens 53-56 19542537-3 2009 Serine 340 and 352 within the third ubiquitin-interacting motif of ATXN3 were particularly important for nuclear localization of normal and expanded ATXN3 and mutation of these sites robustly reduced the formation of nuclear inclusions; a putative nuclear leader sequence was not required. Serine 0-6 ataxin 3 Homo sapiens 67-72 19542537-3 2009 Serine 340 and 352 within the third ubiquitin-interacting motif of ATXN3 were particularly important for nuclear localization of normal and expanded ATXN3 and mutation of these sites robustly reduced the formation of nuclear inclusions; a putative nuclear leader sequence was not required. Serine 0-6 ataxin 3 Homo sapiens 149-154 20017304-0 2009 [Detection of the CAG trinucleotide repeats of MJD1 gene by recombinant DNA technology]. trinucleotide 22-35 ataxin 3 Homo sapiens 47-51 20017304-1 2009 OBJECTIVE: To establish a stable, accurate and intuitive method for detecting the CAG trinucleotide repeats of MJD1 gene. trinucleotide 86-99 ataxin 3 Homo sapiens 111-115 20017304-2 2009 METHODS: The CAG trinucleotide polymorphism of the MJD1 gene was analyzed by recombinant DNA technology and DNA sequencing in 35 spinocerebellar ataxia 3/Machado-Joseph disease (SCA3/MJD) patients from Mainland China. trinucleotide 17-30 ataxin 3 Homo sapiens 51-55 20017304-2 2009 METHODS: The CAG trinucleotide polymorphism of the MJD1 gene was analyzed by recombinant DNA technology and DNA sequencing in 35 spinocerebellar ataxia 3/Machado-Joseph disease (SCA3/MJD) patients from Mainland China. trinucleotide 17-30 ataxin 3 Homo sapiens 178-182 20017304-8 2009 CONCLUSION: Recombinant DNA technology can stably, accurately and intuitively detect the CAG trinucleotide repeat of the MJD1 gene. trinucleotide 93-106 ataxin 3 Homo sapiens 121-125 19185026-1 2009 Machado-Joseph disease (MJD)/spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by polyglutamine expansion in the ataxin-3 protein that confers a toxic gain of function. polyglutamine 128-141 ataxin 3 Homo sapiens 159-167 19185026-9 2009 Overall, mutant ataxin-3 may influence the activity of enzymatic components to remove O(2)(-) and H(2)O(2) efficiently and promote mitochondrial DNA damage or depletion, which leads to dysfunction of mitochondria. Oxygen 86-90 ataxin 3 Homo sapiens 16-24 19185026-9 2009 Overall, mutant ataxin-3 may influence the activity of enzymatic components to remove O(2)(-) and H(2)O(2) efficiently and promote mitochondrial DNA damage or depletion, which leads to dysfunction of mitochondria. h(2)o 98-103 ataxin 3 Homo sapiens 16-24 19492089-8 2009 Analogous cytotoxic results are observed following conformational targeting of normal or polyglutamine-expanded human ataxin-3, which partially aggregate through non-polyglutamine domains. polyglutamine 89-102 ataxin 3 Homo sapiens 118-126 19492089-8 2009 Analogous cytotoxic results are observed following conformational targeting of normal or polyglutamine-expanded human ataxin-3, which partially aggregate through non-polyglutamine domains. polyglutamine 166-179 ataxin 3 Homo sapiens 118-126 19278999-6 2009 We found that the anti-aggregation effect of ROCK inhibitors was not limited to the mutant htt and AR and that Y-27632 was also able to reduce the aggregation of ataxin-3 and atrophin-1 with expanded polyQ. Y 27632 111-118 ataxin 3 Homo sapiens 162-170 19429074-1 2009 Machado-Joseph disease is an autosomal dominant spinocerebellar degeneration caused by the expansion of a polyglutamine tract within the gene product, ataxin-3. polyglutamine 106-119 ataxin 3 Homo sapiens 151-159 19036964-2 2008 In biochemical experiments, we demonstrate that mutant ATX3(exp) specifically associated with the type 1 inositol 1,4,5-trisphosphate receptor (InsP(3)R1), an intracellular calcium (Ca(2+)) release channel. Calcium 173-180 ataxin 3 Homo sapiens 55-59 18599482-5 2008 Ataxin-3 shows even greater activity toward mixed linkage polyubiquitin, cleaving Lys(63) linkages in chains that contain both Lys(48) and Lys(63) linkages. Lysine 82-85 ataxin 3 Homo sapiens 0-8 18599482-2 2008 Here we show that the polyglutamine disease protein, ataxin-3, binds and cleaves ubiquitin chains in a manner suggesting that it functions as a mixed linkage, chain-editing enzyme. polyglutamine 22-35 ataxin 3 Homo sapiens 53-61 18599482-5 2008 Ataxin-3 shows even greater activity toward mixed linkage polyubiquitin, cleaving Lys(63) linkages in chains that contain both Lys(48) and Lys(63) linkages. Lysine 127-130 ataxin 3 Homo sapiens 0-8 18599482-3 2008 Ataxin-3 cleaves ubiquitin chains through its amino-terminal Josephin domain and binds ubiquitin chains through a carboxyl-terminal cluster of ubiquitin interaction motifs neighboring the pathogenic polyglutamine tract. polyglutamine 199-212 ataxin 3 Homo sapiens 0-8 18599482-4 2008 Ataxin-3 binds both Lys(48)- or Lys(63)-linked chains yet preferentially cleaves Lys(63) linkages. Lysine 20-23 ataxin 3 Homo sapiens 0-8 18599482-5 2008 Ataxin-3 shows even greater activity toward mixed linkage polyubiquitin, cleaving Lys(63) linkages in chains that contain both Lys(48) and Lys(63) linkages. Lysine 127-130 ataxin 3 Homo sapiens 0-8 17983597-1 2008 Machado-Joseph disease/Spinocerebellar ataxia type 3 is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 114-127 ataxin 3 Homo sapiens 137-145 18599482-4 2008 Ataxin-3 binds both Lys(48)- or Lys(63)-linked chains yet preferentially cleaves Lys(63) linkages. Lysine 32-35 ataxin 3 Homo sapiens 0-8 18599482-4 2008 Ataxin-3 binds both Lys(48)- or Lys(63)-linked chains yet preferentially cleaves Lys(63) linkages. Lysine 32-35 ataxin 3 Homo sapiens 0-8 18665420-2 2008 These include complex diseases like Alzheimer"s disease and Parkinson"s disease, and Mendelian diseases caused by polyglutamine expansion mutations [like Huntington"s disease (HD) and various spinocerebellar ataxias (SCAs), like SCA3]. polyglutamine 114-127 ataxin 3 Homo sapiens 229-233 18385100-2 2008 MJD results from polyglutamine repeat expansion in the MJD-1 gene, conferring a toxic gain of function to the ataxin-3 protein. polyglutamine 17-30 ataxin 3 Homo sapiens 55-60 18385100-2 2008 MJD results from polyglutamine repeat expansion in the MJD-1 gene, conferring a toxic gain of function to the ataxin-3 protein. polyglutamine 17-30 ataxin 3 Homo sapiens 110-118 18385100-6 2008 In substantia nigra, unilateral overexpression of mutant ataxin-3 led to: apomorphine-induced turning behavior; formation of ubiquitinated ataxin-3 aggregates; alpha-synuclein immunoreactivity; and loss of dopaminergic markers (TH and VMAT2). Apomorphine 74-85 ataxin 3 Homo sapiens 57-65 18418060-3 2008 Recently it was proposed that rapamycin and its derivatives enhance the clearance (and/or reduce the accumulation) of mutant intracellular proteins causing proteinopathies such as tau, alpha-synuclein, ataxin-3, and full-length or fragments of huntingtin containing a polyglutamine (polyQ) expansion, by upregulating macroautophagy. Sirolimus 30-39 ataxin 3 Homo sapiens 202-210 18839019-1 2008 OBJECTIVE: Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by an expansion of polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 155-168 ataxin 3 Homo sapiens 202-206 18839019-1 2008 OBJECTIVE: Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by an expansion of polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 155-168 ataxin 3 Homo sapiens 221-229 17953484-1 2007 Spinocerebellar ataxia type-3 (SCA3) is among the most common dominantly inherited ataxias, and is one of nine devastating human neurodegenerative diseases caused by the expansion of a CAG repeat encoding glutamine within the gene. Glutamine 205-214 ataxin 3 Homo sapiens 0-29 17878166-8 2007 The Ala(71) in SCA3, replacing the Gly(71) in SCA1, has no predictable effect on structure. Alanine 4-7 ataxin 3 Homo sapiens 15-19 17878166-9 2007 The Arg(26) in SCA3, replacing the Gly(26) in SCA1, is predicted to cause structural changes that result in a significantly reduced volume for the internal hydrophobic cavity in SCA3. Arginine 4-7 ataxin 3 Homo sapiens 15-19 17878166-9 2007 The Arg(26) in SCA3, replacing the Gly(26) in SCA1, is predicted to cause structural changes that result in a significantly reduced volume for the internal hydrophobic cavity in SCA3. Arginine 4-7 ataxin 3 Homo sapiens 178-182 17878166-9 2007 The Arg(26) in SCA3, replacing the Gly(26) in SCA1, is predicted to cause structural changes that result in a significantly reduced volume for the internal hydrophobic cavity in SCA3. Glycine 35-38 ataxin 3 Homo sapiens 15-19 17878166-9 2007 The Arg(26) in SCA3, replacing the Gly(26) in SCA1, is predicted to cause structural changes that result in a significantly reduced volume for the internal hydrophobic cavity in SCA3. Glycine 35-38 ataxin 3 Homo sapiens 178-182 18688568-4 2008 Onset data from MJD patients with Azorean origin was used for residual risk estimates according to different ages. azorean 34-41 ataxin 3 Homo sapiens 16-19 17953484-1 2007 Spinocerebellar ataxia type-3 (SCA3) is among the most common dominantly inherited ataxias, and is one of nine devastating human neurodegenerative diseases caused by the expansion of a CAG repeat encoding glutamine within the gene. Glutamine 205-214 ataxin 3 Homo sapiens 31-35 17953484-2 2007 The polyglutamine domain confers toxicity on the protein Ataxin-3 leading to neuronal dysfunction and loss. polyglutamine 4-17 ataxin 3 Homo sapiens 57-65 17510732-2 2007 Analyses of more than 100 recorded clinical items revealed several specifics: I) 50% of patients with probable MSA had asymmetry of symptoms at disease onset and tremor at rest was present in 25%; II) a positive response to levodopa was recorded in 51% of patients identified initially with severe autonomic failure and cerebellar ataxia; III) a positive family history was recorded in 11% (n = 23), two of these patients were identified with spinocerebellar ataxia type 3 (SCA3). Levodopa 224-232 ataxin 3 Homo sapiens 443-472 17696782-1 2007 The neurodegenerative disease spinocerebellar ataxia type 3 (SCA3) is caused by the presence of an extended polyglutamine stretch (polyQ) in the unstructured C-terminus of the human ataxin-3 (AT3) protein. polyglutamine 108-121 ataxin 3 Homo sapiens 182-190 17696782-1 2007 The neurodegenerative disease spinocerebellar ataxia type 3 (SCA3) is caused by the presence of an extended polyglutamine stretch (polyQ) in the unstructured C-terminus of the human ataxin-3 (AT3) protein. polyglutamine 108-121 ataxin 3 Homo sapiens 192-195 17510732-2 2007 Analyses of more than 100 recorded clinical items revealed several specifics: I) 50% of patients with probable MSA had asymmetry of symptoms at disease onset and tremor at rest was present in 25%; II) a positive response to levodopa was recorded in 51% of patients identified initially with severe autonomic failure and cerebellar ataxia; III) a positive family history was recorded in 11% (n = 23), two of these patients were identified with spinocerebellar ataxia type 3 (SCA3). Levodopa 224-232 ataxin 3 Homo sapiens 474-478 17488727-0 2007 Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. polyglutamine 60-73 ataxin 3 Homo sapiens 83-91 17526020-5 2007 Here, we evaluate three different polyglutamine disease proteins--ataxin-1, ataxin-3, and huntingtin--for their ability to disrupt Cajal body localization and reduce the splicing of an artificial reporter in HeLa cells. polyglutamine 34-47 ataxin 3 Homo sapiens 76-84 17488727-4 2007 We analyzed ataxin-3 proteolysis in neuroblastoma cells and in vitro and show that calcium-dependent calpain proteases generate aggregation-competent ataxin-3 fragments. Calcium 83-90 ataxin 3 Homo sapiens 12-20 17488727-4 2007 We analyzed ataxin-3 proteolysis in neuroblastoma cells and in vitro and show that calcium-dependent calpain proteases generate aggregation-competent ataxin-3 fragments. Calcium 83-90 ataxin 3 Homo sapiens 150-158 17092742-7 2007 In postmortem brain material of both Huntington disease and SCA3, E2-25K staining of polyglutamine aggregates was observed in a subset of neurons bearing intranuclear neuronal inclusions. polyglutamine 85-98 ataxin 3 Homo sapiens 60-64 17440947-1 2007 Recent reports suggest that CAG triplet expansions of spinocerebellar ataxia type 2 and 3 (SCA2 and SCA3) genes are the cause of typical levodopa-responsive Parkinson"s disease (PD) in familial cases, several of which were ethnic Chinese. Levodopa 137-145 ataxin 3 Homo sapiens 100-104 17434145-0 2007 Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3. Serine 65-71 ataxin 3 Homo sapiens 19-27 17434145-0 2007 Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3. Serine 65-71 ataxin 3 Homo sapiens 105-113 17434145-1 2007 Machado-Joseph disease (MJD) is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract in MJD-1 gene product, ataxin-3. polyglutamine 100-113 ataxin 3 Homo sapiens 123-128 17434145-1 2007 Machado-Joseph disease (MJD) is a dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract in MJD-1 gene product, ataxin-3. polyglutamine 100-113 ataxin 3 Homo sapiens 143-151 17434145-4 2007 Here we show that S256 site in ataxin-3 is phosphorylated by GSK 3beta. Coumaphos 18-22 ataxin 3 Homo sapiens 31-39 17434145-7 2007 Our results imply that phosphorylation of serine 256 in ataxin-3 by GSK 3beta regulates ataxin-3 aggregation. Serine 42-48 ataxin 3 Homo sapiens 56-64 17434145-7 2007 Our results imply that phosphorylation of serine 256 in ataxin-3 by GSK 3beta regulates ataxin-3 aggregation. Serine 42-48 ataxin 3 Homo sapiens 88-96 17302910-1 2007 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD-1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 158-163 17302910-1 2007 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD-1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 178-186 17302910-6 2007 The effect of p45 on ataxin-3 degradation is blocked by MG132, a proteasome inhibitor. benzyloxycarbonylleucyl-leucyl-leucine aldehyde 56-61 ataxin 3 Homo sapiens 21-29 17362987-0 2007 Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein. polyglutamine 97-110 ataxin 3 Homo sapiens 14-22 17300980-0 2007 Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis. Metals 60-65 ataxin 3 Homo sapiens 48-56 16801344-5 2006 There may be a link between diseases caused by polyglutamine and polyalanine expansion mutations as it has been shown that the expanded CAG/polyglutamine tract within the SCA3 gene can shift to the GCA[corrected]/polyalanine frame. polyglutamine 47-60 ataxin 3 Homo sapiens 171-175 17300980-1 2007 Ataxin-3 (AT3), a protein that causes spinocerebellar ataxia type 3, has a C-terminus containing a polyglutamine stretch, the length of which can be expanded in its pathological variants. polyglutamine 99-112 ataxin 3 Homo sapiens 0-8 17300980-1 2007 Ataxin-3 (AT3), a protein that causes spinocerebellar ataxia type 3, has a C-terminus containing a polyglutamine stretch, the length of which can be expanded in its pathological variants. polyglutamine 99-112 ataxin 3 Homo sapiens 10-13 17300980-2 2007 Here, we report on the role of Cu(2+), Mn(2+), Zn(2+) and Al(3+) in the induction of defective protein structures and subsequent aggregation/fibrillogenesis of three different non-pathological forms of AT3, i.e. murine (Q6), human non-expanded (Q26) and human moderately expanded (Q36). Copper 31-33 ataxin 3 Homo sapiens 202-205 17300980-3 2007 AT3 variants showed an intrinsic propensity to misfolding/aggregation; on the other hand, Zn(2+) and Al(3+) strongly stimulated the amplitude and kinetics of these conformational conversions. Zinc 90-92 ataxin 3 Homo sapiens 0-3 17300980-3 2007 AT3 variants showed an intrinsic propensity to misfolding/aggregation; on the other hand, Zn(2+) and Al(3+) strongly stimulated the amplitude and kinetics of these conformational conversions. ALUMINUM ION 101-107 ataxin 3 Homo sapiens 0-3 17300980-7 2007 The observation that Zn(2+) and Al(3+) promote AT3 fibrillogenesis is consistent with similar results found for other amyloidogenic molecules, such as beta-amyloid and prion proteins. Zinc 21-23 ataxin 3 Homo sapiens 47-50 17300980-7 2007 The observation that Zn(2+) and Al(3+) promote AT3 fibrillogenesis is consistent with similar results found for other amyloidogenic molecules, such as beta-amyloid and prion proteins. Aluminum 32-34 ataxin 3 Homo sapiens 47-50 17300980-9 2007 Studies of liposomes as membrane models showed dramatic changes in the structural properties of the lipid bilayer in the presence of AT3, which were enhanced after supplementing the protein with Zn(2+) and Al(3+). Zinc 195-197 ataxin 3 Homo sapiens 133-136 17300980-9 2007 Studies of liposomes as membrane models showed dramatic changes in the structural properties of the lipid bilayer in the presence of AT3, which were enhanced after supplementing the protein with Zn(2+) and Al(3+). Aluminum 206-208 ataxin 3 Homo sapiens 133-136 17172864-5 2006 These studies showed that upregulation of ban mitigates degeneration induced by the pathogenic polyglutamine (polyQ) protein Ataxin-3, which is mutated in the human polyglutamine disease spinocerebellar ataxia type 3 (SCA3). polyglutamine 95-108 ataxin 3 Homo sapiens 218-222 17172864-5 2006 These studies showed that upregulation of ban mitigates degeneration induced by the pathogenic polyglutamine (polyQ) protein Ataxin-3, which is mutated in the human polyglutamine disease spinocerebellar ataxia type 3 (SCA3). polyglutamine 110-115 ataxin 3 Homo sapiens 218-222 16801344-5 2006 There may be a link between diseases caused by polyglutamine and polyalanine expansion mutations as it has been shown that the expanded CAG/polyglutamine tract within the SCA3 gene can shift to the GCA[corrected]/polyalanine frame. polyalanine 65-76 ataxin 3 Homo sapiens 171-175 16801344-5 2006 There may be a link between diseases caused by polyglutamine and polyalanine expansion mutations as it has been shown that the expanded CAG/polyglutamine tract within the SCA3 gene can shift to the GCA[corrected]/polyalanine frame. polyalanine 213-224 ataxin 3 Homo sapiens 171-175 16939621-1 2006 The protein ataxin-3 is responsible for spinocerebellar ataxia type 3, a neurodegenerative disease triggered when the length of a stretch of consecutive glutamines exceeds a critical threshold. Glutamine 153-163 ataxin 3 Homo sapiens 12-20 16765348-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant inherited neurodegenerative disease caused by the expansion of a polyglutamine repeat within the disease protein, ataxin-3. polyglutamine 127-140 ataxin 3 Homo sapiens 0-29 16765348-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant inherited neurodegenerative disease caused by the expansion of a polyglutamine repeat within the disease protein, ataxin-3. polyglutamine 127-140 ataxin 3 Homo sapiens 176-184 17079677-6 2006 For transcriptional repression normal AT3 cooperates with HDAC3 and requires its intact ubiquitin-interacting motifs (UIMs), whereas aberrant transcriptional activation by expanded AT3 is independent of the UIMs but requires the catalytic cysteine of the ubiquitin protease domain. Cysteine 239-247 ataxin 3 Homo sapiens 181-184 16194547-1 2005 Machado-Joseph"s disease is caused by a CAG trinucleotide repeat expansion that is translated into an abnormally long polyglutamine tract in the protein ataxin-3. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 40-43 ataxin 3 Homo sapiens 153-161 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 15-28 ataxin 3 Homo sapiens 38-46 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 15-28 ataxin 3 Homo sapiens 48-51 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 134-147 ataxin 3 Homo sapiens 38-46 16822850-1 2006 Expansion of a polyglutamine tract in ataxin-3 (AT3) results in spinocerebellar ataxia type 3/Machado-Joseph disease, one of the nine polyglutamine neurodegenerative diseases. polyglutamine 134-147 ataxin 3 Homo sapiens 48-51 16822850-2 2006 Understanding the normal functions of AT3 as well as its function in the context of expansion of the polyglutamine tract is critical for understanding the disease process. polyglutamine 101-114 ataxin 3 Homo sapiens 38-41 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 129-142 ataxin 3 Homo sapiens 0-3 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 129-142 ataxin 3 Homo sapiens 223-226 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 129-142 ataxin 3 Homo sapiens 223-226 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 190-203 ataxin 3 Homo sapiens 0-3 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 190-203 ataxin 3 Homo sapiens 223-226 16822850-7 2006 AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta. polyglutamine 190-203 ataxin 3 Homo sapiens 223-226 16687213-1 2006 Recent reports of SCA2 and SCA3 patients who presented with levodopa responsive parkinsonism have generated considerable interest as they have implications for genetic testing. Levodopa 60-68 ataxin 3 Homo sapiens 27-31 16624810-0 2006 The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. polyglutamine 61-74 ataxin 3 Homo sapiens 25-33 16624810-3 2006 Ataxin-3 consists of a folded Josephin domain followed by two ubiquitin-interacting motifs and a C-terminal polyglutamine tract, which in the non-pathological form is less than 45 residues in length. polyglutamine 108-121 ataxin 3 Homo sapiens 0-8 16624810-4 2006 We demonstrate that ataxin-3 with 64 glutamines (at(Q64)) undergoes a two-stage aggregation. Glutamine 37-47 ataxin 3 Homo sapiens 20-28 16624810-9 2006 These observations demonstrate that ataxin-3 has an inherent capacity to aggregate through its non-polyglutamine domains. polyglutamine 99-112 ataxin 3 Homo sapiens 36-44 16791428-4 2006 Using a transfected mammalian cell line, we demonstrate that ATX3 aggregation is noticeably reduced by deletion or replacement of regions other than the polyglutamine tract. polyglutamine 153-166 ataxin 3 Homo sapiens 61-65 16407371-0 2006 Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. polyglutamine 24-37 ataxin 3 Homo sapiens 47-55 16407371-0 2006 Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. polyglutamine 24-37 ataxin 3 Homo sapiens 118-126 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 49-62 ataxin 3 Homo sapiens 0-29 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 49-62 ataxin 3 Homo sapiens 31-35 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 64-69 ataxin 3 Homo sapiens 0-29 16407371-1 2006 Spinocerebellar ataxia type 3 (SCA3), like other polyglutamine (polyQ) diseases, is characterized by the formation of intraneuronal inclusions, but the mechanism underlying their formation is poorly understood. polyglutamine 64-69 ataxin 3 Homo sapiens 31-35 16407371-3 2006 We demonstrate that the removal of the N-terminus of polyQ-expanded ataxin-3 (AT3) is required for aggregation in vitro and in vivo. polyglutamine 53-58 ataxin 3 Homo sapiens 68-76 16112867-0 2006 Polyglutamine-expanded ataxin-3 activates mitochondrial apoptotic pathway by upregulating Bax and downregulating Bcl-xL. polyglutamine 0-13 ataxin 3 Homo sapiens 23-31 16112867-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Homo sapiens 0-29 16112867-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Homo sapiens 31-35 16112867-1 2006 Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disease caused by polyglutamine-expanded ataxin-3. polyglutamine 98-111 ataxin 3 Homo sapiens 121-129 16112867-8 2006 Our results suggest that polyglutamine-expanded ataxin-3-Q79 activates mitochondrial apoptotic pathway and induces neuronal death by upregulating Bax expression and downregulating Bcl-xL expression. polyglutamine 25-38 ataxin 3 Homo sapiens 48-56 17046388-4 2006 In this report, we describe a purification protocol for ataxin-3, which, in its polyglutamine-expanded form, causes Machado-Joseph disease. polyglutamine 80-93 ataxin 3 Homo sapiens 56-64 17046388-5 2006 Purification of different length ataxin-3 variants, including one of pathological length, is facilitated by an N-terminal hexa-histidine tag, which enables binding to a nickel-chelated agarose resin. Histidine 127-136 ataxin 3 Homo sapiens 33-41 17046388-5 2006 Purification of different length ataxin-3 variants, including one of pathological length, is facilitated by an N-terminal hexa-histidine tag, which enables binding to a nickel-chelated agarose resin. Nickel 169-175 ataxin 3 Homo sapiens 33-41 17046388-5 2006 Purification of different length ataxin-3 variants, including one of pathological length, is facilitated by an N-terminal hexa-histidine tag, which enables binding to a nickel-chelated agarose resin. Sepharose 185-192 ataxin 3 Homo sapiens 33-41 16194547-1 2005 Machado-Joseph"s disease is caused by a CAG trinucleotide repeat expansion that is translated into an abnormally long polyglutamine tract in the protein ataxin-3. trinucleotide 44-57 ataxin 3 Homo sapiens 153-161 16194547-1 2005 Machado-Joseph"s disease is caused by a CAG trinucleotide repeat expansion that is translated into an abnormally long polyglutamine tract in the protein ataxin-3. polyglutamine 118-131 ataxin 3 Homo sapiens 153-161 16194547-4 2005 Human ataxin-3 containing a non-pathological number of glutamine residues (14Q), as well as its Caenorhabditis elegans (1Q) orthologue, showed a high tendency towards self-interaction and aggregation, under near-physiological conditions. Glutamine 55-64 ataxin 3 Homo sapiens 6-14 16194547-7 2005 Furthermore, non-expanded ataxin-3 oligomers are recognized by a specific antibody that targets a conformational epitope present in soluble cytotoxic species found in the fibrillization pathway of expanded polyglutamine proteins and other amyloid-forming proteins. polyglutamine 206-219 ataxin 3 Homo sapiens 26-34 16040601-8 2005 Although this post-translational modification occurs in a UIM-dependent manner, it becomes independent of UIMs when the catalytic cysteine residue of ataxin-3 is mutated, suggesting that ataxin-3 ubiquitination is itself regulated in trans by its own de-ubiquitinating activity. Cysteine 130-138 ataxin 3 Homo sapiens 150-158 16040601-8 2005 Although this post-translational modification occurs in a UIM-dependent manner, it becomes independent of UIMs when the catalytic cysteine residue of ataxin-3 is mutated, suggesting that ataxin-3 ubiquitination is itself regulated in trans by its own de-ubiquitinating activity. Cysteine 130-138 ataxin 3 Homo sapiens 187-195 15876340-2 2005 PATIENTS AND METHODS: This study involved the clinical response of lamotrigine (LTG) on six MJD patients with early truncal ataxia and the effect of LTG on the alteration of ataxin-3 expression in the transformed MJD lymphoblastoid cells. Lamotrigine 149-152 ataxin 3 Homo sapiens 174-182 16087686-3 2005 We have previously demonstrated that in SCA3, the expanded CAG tract in the MJD-1 transcript is prone to frameshifting, which may lead to the production of polyalanine-containing proteins. polyalanine 156-167 ataxin 3 Homo sapiens 76-81 16020535-4 2005 By using the Josephin structure and the availability of NMR chemical shift assignments, we have mapped the enzyme active site by using the typical cysteine protease inhibitors, transepoxysuccinyl-L-eucylamido-4-guanidino-butane (E-64) and [L-3-trans-(propylcarbamyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline (CA-074). transepoxysuccinyl-l-eucylamido-4-guanidino-butane 177-227 ataxin 3 Homo sapiens 13-21 16020535-4 2005 By using the Josephin structure and the availability of NMR chemical shift assignments, we have mapped the enzyme active site by using the typical cysteine protease inhibitors, transepoxysuccinyl-L-eucylamido-4-guanidino-butane (E-64) and [L-3-trans-(propylcarbamyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline (CA-074). E 64 229-233 ataxin 3 Homo sapiens 13-21 15911147-4 2005 l-Dopa-responsive parkinsonism with minimal cerebellar deficits has been described in SCA2 and SCA3. Levodopa 0-6 ataxin 3 Homo sapiens 95-99 16118278-2 2005 The affected protein, ataxin-3, which contains an N-terminal Josephin domain followed by tandem ubiquitin (Ub)-interacting motifs (UIMs) and a polyglutamine stretch, has been implicated in the function of the Ub proteasome system. polyglutamine 143-156 ataxin 3 Homo sapiens 22-30 16118278-4 2005 Mutation of the catalytic Cys enhances the stability of a complex between ataxin-3 and polyubiquitinated proteins. Cysteine 26-29 ataxin 3 Homo sapiens 74-82 16020535-4 2005 By using the Josephin structure and the availability of NMR chemical shift assignments, we have mapped the enzyme active site by using the typical cysteine protease inhibitors, transepoxysuccinyl-L-eucylamido-4-guanidino-butane (E-64) and [L-3-trans-(propylcarbamyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline (CA-074). [l-3-trans-(propylcarbamyl)oxirane-2-carbonyl]-l-isoleucyl-l-proline 239-307 ataxin 3 Homo sapiens 13-21 16020535-4 2005 By using the Josephin structure and the availability of NMR chemical shift assignments, we have mapped the enzyme active site by using the typical cysteine protease inhibitors, transepoxysuccinyl-L-eucylamido-4-guanidino-butane (E-64) and [L-3-trans-(propylcarbamyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline (CA-074). N-(3-propylcarbamoyloxirane-2-carbonyl)-isoleucyl-proline 309-315 ataxin 3 Homo sapiens 13-21 15876340-4 2005 In Western blot analysis of ataxin-3 in MJD lymphoblastoid cells, extracellular application of LTG, while leaving the normal level of ataxin-3 intact, decreased the expression of mutant ataxin-3 in a dose-related manner. Lamotrigine 95-98 ataxin 3 Homo sapiens 28-36 15876340-4 2005 In Western blot analysis of ataxin-3 in MJD lymphoblastoid cells, extracellular application of LTG, while leaving the normal level of ataxin-3 intact, decreased the expression of mutant ataxin-3 in a dose-related manner. Lamotrigine 95-98 ataxin 3 Homo sapiens 134-142 15876340-4 2005 In Western blot analysis of ataxin-3 in MJD lymphoblastoid cells, extracellular application of LTG, while leaving the normal level of ataxin-3 intact, decreased the expression of mutant ataxin-3 in a dose-related manner. Lamotrigine 95-98 ataxin 3 Homo sapiens 134-142 15876340-5 2005 CONCLUSION: Our results indicated that LTG may have significant benefits in relief of gait disturbance in MJD patients with early ataxia, and may be related to the decreased expression of mutant ataxin-3. Lamotrigine 39-42 ataxin 3 Homo sapiens 195-203 15952105-5 2005 RESULTS: Five novel ataxin-3 interacting proteins were obtained, among which were three known proteins, namely human rhodopsin guanosine diphosphate dissociation inhibitor alpha, small ubiquitin-like modifier 1, and human neuronal amiloride-sensitive cation channel 2; the other two were unknown. Guanosine Diphosphate 127-148 ataxin 3 Homo sapiens 20-28 16080609-1 2005 Expansion of CAG trinucleotide repeats has been shown to cause a number of autosomal dominant spinocerebellar ataxias such as SCA1, SCA2, SCA3/MJD, SCA6 and SCA7. trinucleotide 17-30 ataxin 3 Homo sapiens 138-142 16080609-1 2005 Expansion of CAG trinucleotide repeats has been shown to cause a number of autosomal dominant spinocerebellar ataxias such as SCA1, SCA2, SCA3/MJD, SCA6 and SCA7. trinucleotide 17-30 ataxin 3 Homo sapiens 143-146 15952105-6 2005 Interacting domain analysis revealed that an unknown protein interacted with the C-terminus near the polyglutamine tract of ataxin-3, the other four all interacted with the N-terminus. polyglutamine 101-114 ataxin 3 Homo sapiens 124-132 15504352-5 2004 Concentration- and time-dependent experiments showed that the increase in staurosporine-induced cell death was more pronounced and accelerated in cells containing expanded ataxin-3 via MTS assays. Staurosporine 74-87 ataxin 3 Homo sapiens 172-180 15895563-2 2005 The translated proteins contain abnormally long polyglutamine stretches, and SCA-1, SCA-2, SCA-3/Machado-Joseph disease (MJD), SCA-6, SCA-7, and SCA-17 are "polyglutamine diseases". polyglutamine 157-170 ataxin 3 Homo sapiens 91-96 15895563-10 2005 The dentate nucleus displays "grumose" degeneration in SCA-3/MJD while the cerebellar cortex and the inferior olivary nuclei remain largely unaffected. grumose 30-37 ataxin 3 Homo sapiens 55-60 15544810-1 2004 Expansion of the polyglutamine (polyQ) region in the protein ataxin-3 is associated with spinocerebellar ataxia type 3, an inherited neurodegenerative disorder that belongs to the family of polyQ diseases. polyglutamine 17-30 ataxin 3 Homo sapiens 61-69 15544810-1 2004 Expansion of the polyglutamine (polyQ) region in the protein ataxin-3 is associated with spinocerebellar ataxia type 3, an inherited neurodegenerative disorder that belongs to the family of polyQ diseases. polyglutamine 32-37 ataxin 3 Homo sapiens 61-69 15544810-3 2004 In a previous study, we determined the domain architecture of ataxin-3, suggesting that it comprises a globular domain, named Josephin, and a more flexible C-terminal region, that includes the polyQ tract. polyglutamine 193-198 ataxin 3 Homo sapiens 62-70 15630566-0 2004 Assignment of the 1H, 13C, and 15N resonances of the Josephin domain of human ataxin-3. Hydrogen 18-20 ataxin 3 Homo sapiens 78-86 15630566-0 2004 Assignment of the 1H, 13C, and 15N resonances of the Josephin domain of human ataxin-3. 13c 22-25 ataxin 3 Homo sapiens 78-86 15630566-0 2004 Assignment of the 1H, 13C, and 15N resonances of the Josephin domain of human ataxin-3. 15n 31-34 ataxin 3 Homo sapiens 78-86 15918882-10 2005 Virus-induced gene silencing of AT3 resulted in a decrease in the accumulation of capsaicinoids, a phenotype consistent with pun1. Capsaicin 82-95 ataxin 3 Homo sapiens 32-35 15767577-1 2005 The polyglutamine-containing neurodegenerative protein ataxin 3 (AT3) has deubiquitylating activity and binds ubiquitin chains with a preference for chains of four or more ubiquitins. polyglutamine 4-17 ataxin 3 Homo sapiens 55-63 15637221-5 2004 Endonuclease activity is crucial for protecting against the expansion/contraction of the trinucleotide repeats in the genes that encode for proteins such as Ataxin 3--the "mutant" chaperone protein that hallmarks the central nervous system (CNS) of MJD sufferers. trinucleotide 89-102 ataxin 3 Homo sapiens 157-165 15504352-10 2004 In our cellular model, full-length expanded ataxin-3 that leads to neurodegenerative disorders significantly impaired the expression of Bcl-2 protein, which may be, at least in part, responsible for the weak tolerance to polyglutamine toxicity at the early stage of disease and ultimately resulted in an increase of stress-induced cell death upon apoptotic stress. polyglutamine 221-234 ataxin 3 Homo sapiens 44-52 15345714-0 2004 Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. polyglutamine 0-13 ataxin 3 Homo sapiens 27-35 15345714-3 2004 In this study, we have investigated the hypothesis that polyglutamine expansion in the protein ataxin-3 destabilizes the native protein, leading to the accumulation of a partially unfolded, aggregation-prone intermediate. polyglutamine 56-69 ataxin 3 Homo sapiens 95-103 15325242-0 2004 Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin-3. polyglutamine 65-78 ataxin 3 Homo sapiens 42-50 15325242-0 2004 Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin-3. polyglutamine 65-78 ataxin 3 Homo sapiens 87-95 15140190-0 2004 Caspase-mediated proteolysis of the polyglutamine disease protein ataxin-3. polyglutamine 36-49 ataxin 3 Homo sapiens 66-74 15192175-0 2004 Dramatic levodopa responsiveness of dystonia in a sporadic case of spinocerebellar ataxia type 3. Levodopa 9-17 ataxin 3 Homo sapiens 67-96 15192175-3 2004 A trial of levodopa for dystonia in SCA 3 may be of therapeutic benefit, at least in the initial stage of the disease. Levodopa 11-19 ataxin 3 Homo sapiens 36-41 15080863-7 2004 The SCA3/MJD CAG trinucleotide repeat expansion in 60 affected individuals from 26 families (32%) was expanded to 71-85 CAG repeats. trinucleotide 17-30 ataxin 3 Homo sapiens 4-8 15080863-7 2004 The SCA3/MJD CAG trinucleotide repeat expansion in 60 affected individuals from 26 families (32%) was expanded to 71-85 CAG repeats. trinucleotide 17-30 ataxin 3 Homo sapiens 9-12 15140190-4 2004 Using cellular models we now show that the endogenous spinocerebellar ataxia type-3 disease protein, ataxin-3, is proteolyzed in apoptotic paradigms, resulting in the loss of full-length ataxin-3 and the corresponding appearance of an approximately 28-kDa fragment containing the glutamine repeat. Glutamine 280-289 ataxin 3 Homo sapiens 101-109 14749733-2 2004 We now show that ataxin-3, in which the abnormal expansion of a polyglutamine tract is responsible for spinocerebellar ataxia type 3 (SCA3), undergoes ubiquitylation and degradation by the proteasome. polyglutamine 64-77 ataxin 3 Homo sapiens 17-25 14749733-2 2004 We now show that ataxin-3, in which the abnormal expansion of a polyglutamine tract is responsible for spinocerebellar ataxia type 3 (SCA3), undergoes ubiquitylation and degradation by the proteasome. polyglutamine 64-77 ataxin 3 Homo sapiens 103-132 14749733-2 2004 We now show that ataxin-3, in which the abnormal expansion of a polyglutamine tract is responsible for spinocerebellar ataxia type 3 (SCA3), undergoes ubiquitylation and degradation by the proteasome. polyglutamine 64-77 ataxin 3 Homo sapiens 134-138 15639784-5 2004 Ataxin-3 (both full length and truncated) with normal glutamine repeats are not ubiquitinated, however, ataxin-3 with expanded polyglutamine is ubiquitinated and the ubiquitination depends on the misfolding propensity of the polyglutamine expanded ataxin-3. polyglutamine 225-238 ataxin 3 Homo sapiens 104-112 14659761-1 2004 Ataxin-3 is a member of the polyglutamine family of proteins, which are associated with at least nine different neurodegenerative diseases. polyglutamine 28-41 ataxin 3 Homo sapiens 0-8 14659761-6 2004 We describe here the first equilibrium folding pathway delineated for any polyglutamine protein and show that ataxin-3 folds reversibly via a single intermediate species. polyglutamine 74-87 ataxin 3 Homo sapiens 110-118 15354398-2 2004 Aim of the present study was to evaluate the diagnostic potential of TCS in spinocerebellar ataxia type 3 (SCA3), a neurodegenerative disease affecting the cerebellum, multiple pontine nuclei, substantia nigra, pallidum, putamen, caudate nucleus and long spinal tracts. 9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide 69-72 ataxin 3 Homo sapiens 76-105 15354398-2 2004 Aim of the present study was to evaluate the diagnostic potential of TCS in spinocerebellar ataxia type 3 (SCA3), a neurodegenerative disease affecting the cerebellum, multiple pontine nuclei, substantia nigra, pallidum, putamen, caudate nucleus and long spinal tracts. 9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide 69-72 ataxin 3 Homo sapiens 107-111 15354398-3 2004 METHODS: 15 patients with a molecular diagnosis of SCA3 and 15 age- and sex-matched healthy control individuals were examined with TCS. 9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide 131-134 ataxin 3 Homo sapiens 51-55 15354398-10 2004 CONCLUSIONS: TCS is a suitable and non-invasive bed-side method to detect basal ganglia hyperechogenic lesions and posterior fossa abnormalities in SCA3 patients. 9-ethyl-N-(3,4,5-trimethoxyphenyl)carbazole-3-sulfonamide 13-16 ataxin 3 Homo sapiens 148-152 15639784-0 2004 Misfolding promotes the ubiquitination of polyglutamine-expanded ataxin-3, the defective gene product in SCA3/MJD. polyglutamine 42-55 ataxin 3 Homo sapiens 65-73 15639784-0 2004 Misfolding promotes the ubiquitination of polyglutamine-expanded ataxin-3, the defective gene product in SCA3/MJD. polyglutamine 42-55 ataxin 3 Homo sapiens 105-109 15639784-3 2004 By using ataxin-3, the defective gene product of SCA3/MJD, we demonstrate here that the misfolding propensity and the cellular toxicity of a polyglutamine protein is directly proportional to the length of the glutamine repeats and inversely dependent on the size of the corresponding protein. polyglutamine 141-154 ataxin 3 Homo sapiens 9-17 15639784-3 2004 By using ataxin-3, the defective gene product of SCA3/MJD, we demonstrate here that the misfolding propensity and the cellular toxicity of a polyglutamine protein is directly proportional to the length of the glutamine repeats and inversely dependent on the size of the corresponding protein. polyglutamine 141-154 ataxin 3 Homo sapiens 49-53 15639784-3 2004 By using ataxin-3, the defective gene product of SCA3/MJD, we demonstrate here that the misfolding propensity and the cellular toxicity of a polyglutamine protein is directly proportional to the length of the glutamine repeats and inversely dependent on the size of the corresponding protein. Glutamine 145-154 ataxin 3 Homo sapiens 9-17 15639784-3 2004 By using ataxin-3, the defective gene product of SCA3/MJD, we demonstrate here that the misfolding propensity and the cellular toxicity of a polyglutamine protein is directly proportional to the length of the glutamine repeats and inversely dependent on the size of the corresponding protein. Glutamine 145-154 ataxin 3 Homo sapiens 49-53 15639784-5 2004 Ataxin-3 (both full length and truncated) with normal glutamine repeats are not ubiquitinated, however, ataxin-3 with expanded polyglutamine is ubiquitinated and the ubiquitination depends on the misfolding propensity of the polyglutamine expanded ataxin-3. Glutamine 54-63 ataxin 3 Homo sapiens 0-8 15639784-5 2004 Ataxin-3 (both full length and truncated) with normal glutamine repeats are not ubiquitinated, however, ataxin-3 with expanded polyglutamine is ubiquitinated and the ubiquitination depends on the misfolding propensity of the polyglutamine expanded ataxin-3. polyglutamine 127-140 ataxin 3 Homo sapiens 104-112 15152500-1 2003 Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is neurodegenerative disease which is caused by polyglutamine expansion in a responsible gene product, MJD1/Ataxin3. polyglutamine 114-127 ataxin 3 Homo sapiens 169-173 14661975-0 2003 Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36). polyglutamine 124-137 ataxin 3 Homo sapiens 84-92 14661975-1 2003 The protein ataxin-3 is responsible for Machado-Joseph disease/spinocerebellar ataxia type 3, a neurodegenerative disorder caused by the presence of an expanded polyglutamine tract. polyglutamine 161-174 ataxin 3 Homo sapiens 12-20 14661975-11 2003 In contrast, human Q36 ataxin-3 underwent a progressive increase in the beta-sheet and a concomitant decrease in helical content when the temperature was shifted from 37 to 80 degrees C, followed by the irreversible formation of aggregates above 80 degrees C. They were shown to consist of amyloid fibrils, as supported by both electron microscopy images and the typical spectral shift displayed by Congo red when it was added to the protein at growing temperatures. Congo Red 399-408 ataxin 3 Homo sapiens 23-31 14559776-7 2003 Mutating the predicted catalytic cysteine in AT3 inhibits each of these ubiquitin protease activities. Cysteine 33-41 ataxin 3 Homo sapiens 45-48 15152500-3 2003 MJD1 with expanded polyglutamine tract was more resistant to degradation than normal MJD1. polyglutamine 19-32 ataxin 3 Homo sapiens 0-4 15152500-1 2003 Machado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is neurodegenerative disease which is caused by polyglutamine expansion in a responsible gene product, MJD1/Ataxin3. polyglutamine 114-127 ataxin 3 Homo sapiens 174-181 15152500-7 2003 UFD2a markedly promoted ubiquitylation and degradation of MJD1 with expanded polyglutamine tract, resulting in the clearance of MJD1 protein. polyglutamine 77-90 ataxin 3 Homo sapiens 58-62 15152500-7 2003 UFD2a markedly promoted ubiquitylation and degradation of MJD1 with expanded polyglutamine tract, resulting in the clearance of MJD1 protein. polyglutamine 77-90 ataxin 3 Homo sapiens 128-132 15152500-9 2003 In Drosophila model, overexpression of UFD2a significantly suppressed the neurodegeneration induced by expression of MJD1 with expanded polyglutamine tract. polyglutamine 136-149 ataxin 3 Homo sapiens 117-121 12873751-2 2003 We describe a Chinese patient with a mutation at the SCA 3 locus with clinical features of levodopa-responsive dystonia. Levodopa 91-99 ataxin 3 Homo sapiens 53-58 12873751-6 2003 This expands the wide and varied phenotypic manifestations of SCA 3, and highlights the observation that features suggestive of levodopa-responsive dystonia (DRD) such as focal dystonia, gait difficulty with diurnal fluctuation of symptoms, and a marked response to low doses of levodopa can be presenting features of SCA 3. Levodopa 128-136 ataxin 3 Homo sapiens 318-323 12944474-1 2003 Machado-Joseph disease is caused by an expansion of a trinucleotide CAG repeat in the gene encoding the protein ataxin-3. trinucleotide 54-67 ataxin 3 Homo sapiens 112-120 11572942-0 2001 An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta -fibrils. Glutamine 12-21 ataxin 3 Homo sapiens 49-57 12914917-1 2003 Anomalous expansion of a polyglutamine (polyQ) tract in the protein ataxin-3 causes spinocerebellar ataxia type 3, an autosomal dominant neurodegenerative disease. polyglutamine 25-38 ataxin 3 Homo sapiens 68-76 12116198-1 2002 Expansions of trinucleotide repeats have been discovered in spinocerebellar ataxia (SCA) types 1, 2, 6, 7, 12, and 17, Machado-Joseph disease (MJD/SCA3), and dentatorubropallidoluysian atrophy (DRPLA). trinucleotide 14-27 ataxin 3 Homo sapiens 143-146 12116198-1 2002 Expansions of trinucleotide repeats have been discovered in spinocerebellar ataxia (SCA) types 1, 2, 6, 7, 12, and 17, Machado-Joseph disease (MJD/SCA3), and dentatorubropallidoluysian atrophy (DRPLA). trinucleotide 14-27 ataxin 3 Homo sapiens 147-151 12486728-0 2003 Structural modeling of ataxin-3 reveals distant homology to adaptins. adaptins 60-68 ataxin 3 Homo sapiens 23-31 12297501-4 2002 The C-terminal polyglutamine-containing domain of ataxin-3 inhibits coactivator-dependent transcription and is required for binding coactivators. polyglutamine 15-28 ataxin 3 Homo sapiens 50-58 12460614-1 2002 Nuclear aggregates (NAs) and neurodegeneration in brains from patients with Machado-Joseph disease (MJD) are both triggered by pathological expansion of CAG/polyglutamine repeat in ataxin-3, but it remains to be clarified whether NA formation is associated with accelerated neurodegeneration. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 153-156 ataxin 3 Homo sapiens 181-189 12460614-1 2002 Nuclear aggregates (NAs) and neurodegeneration in brains from patients with Machado-Joseph disease (MJD) are both triggered by pathological expansion of CAG/polyglutamine repeat in ataxin-3, but it remains to be clarified whether NA formation is associated with accelerated neurodegeneration. polyglutamine 157-170 ataxin 3 Homo sapiens 181-189 12430715-4 2002 First, we examined the relationship between MBs and polyglutamine proteins and demonstrated that one of the polyglutamine proteins, ataxin-3, as well as a 19S proteasomal protein, was preferentially recruited into MBs even in the absence of expanded polyglutamine. polyglutamine 52-65 ataxin 3 Homo sapiens 132-140 12430715-4 2002 First, we examined the relationship between MBs and polyglutamine proteins and demonstrated that one of the polyglutamine proteins, ataxin-3, as well as a 19S proteasomal protein, was preferentially recruited into MBs even in the absence of expanded polyglutamine. polyglutamine 108-121 ataxin 3 Homo sapiens 132-140 12084819-4 2002 Additional studies of green fluorescent protein-tagged cAMP response element binding protein coexpressed with either of two mutant polyglutamine proteins, ataxin-3 and huntingtin, support a model of disease in which coaggregation of transcriptional components contributes to pathogenesis. Cyclic AMP 55-59 ataxin 3 Homo sapiens 155-163 11572863-3 2001 Here, in studies of the spinocerebellar ataxia type 3 disease protein ataxin-3, we demonstrate that the protein sequence surrounding polyQ specifies the constituents of nuclear inclusions (NI) formed by the disease protein. polyglutamine 133-138 ataxin 3 Homo sapiens 70-78 11572863-6 2001 Moreover, normal ataxin-3 represses cAMP response element-binding protein-mediated transcription, indicating a functional consequence of ataxin-3 interactions with CBP. Cyclic AMP 36-40 ataxin 3 Homo sapiens 17-25 11572863-6 2001 Moreover, normal ataxin-3 represses cAMP response element-binding protein-mediated transcription, indicating a functional consequence of ataxin-3 interactions with CBP. Cyclic AMP 36-40 ataxin 3 Homo sapiens 137-145 11572942-1 2001 The protein ataxin-3 contains a polyglutamine region; increasing the number of glutamines beyond 55 in this region gives rise to the neurodegenerative disease spinocerebellar ataxia type 3. polyglutamine 32-45 ataxin 3 Homo sapiens 12-20 11572942-1 2001 The protein ataxin-3 contains a polyglutamine region; increasing the number of glutamines beyond 55 in this region gives rise to the neurodegenerative disease spinocerebellar ataxia type 3. Glutamine 79-89 ataxin 3 Homo sapiens 12-20 11563629-4 2001 Triple-labeling immunofluorescence demonstrated colocalization of ataxin-2 and ataxin-3 in NIIs containing expanded polyglutamine, irrespective of the disease examined. polyglutamine 116-129 ataxin 3 Homo sapiens 79-87 11719247-5 2001 Recently, the transglutaminase activity has been hypothesized to be involved in the pathogenetic mechanisms responsible for the formation of cellular inclusions present in Huntington disease and in all the other polyglutamine (polyQ) diseases hitherto identified, such as spinobulbar muscular atrophy or Kennedy disease, spinocerebellar ataxias (SCA-1, SCA-2, SCA-3 or Machado-Joseph disease, SCA-6 and SCA-7) and dentatorubropallidoluysian atrophy. polyglutamine 227-232 ataxin 3 Homo sapiens 360-365 11719271-1 2001 Ataxin-3, a protein coded by the Machado-Joseph disease gene, possesses a polyglutamine stretch whose expansion is known to produce neuronal intranuclear inclusion and neurodegeneration. polyglutamine 74-87 ataxin 3 Homo sapiens 0-8 11719271-5 2001 Our data indicates that susceptibility to cell death produced by mutant truncated ataxin-3 differs significantly among different cell lines and provides useful information when using a cultured cell line as an in vitro cellular model of polyglutamine disease. polyglutamine 237-250 ataxin 3 Homo sapiens 82-90 11561037-3 2001 Because this nuclear inclusion is thought to be formed in response to cellular stress, as occurs in hepatic encephalopathy, even in the absence of an expanded CAG/polyglutamine repeat, recruitment of ataxin-3 and ubiquitin into Marinesco bodies may represent a cellular response to noxious external stimuli unrelated to expanded CAG/polyglutamine. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 329-332 ataxin 3 Homo sapiens 200-208 11561037-3 2001 Because this nuclear inclusion is thought to be formed in response to cellular stress, as occurs in hepatic encephalopathy, even in the absence of an expanded CAG/polyglutamine repeat, recruitment of ataxin-3 and ubiquitin into Marinesco bodies may represent a cellular response to noxious external stimuli unrelated to expanded CAG/polyglutamine. polyglutamine 333-346 ataxin 3 Homo sapiens 200-208 11342385-2 2000 Here we report the results of the analysis of five trinucleotide repeats containing genes (SCA1, MJD/SCA3, DRPLA, FRDA and MD) in HD patients and in a group of healthy controls. trinucleotide 51-64 ataxin 3 Homo sapiens 101-105 11461169-1 2001 We previously verified the effectiveness of tetrahydrobiopterin (BH4) on the ataxia in Machado-Joseph disease (MJD; SCA3 [spinocerebellar ataxia type 3]) as one of the most common types of dominantly inherited spinocerebellar ataxias. sapropterin 44-63 ataxin 3 Homo sapiens 116-120 11461169-1 2001 We previously verified the effectiveness of tetrahydrobiopterin (BH4) on the ataxia in Machado-Joseph disease (MJD; SCA3 [spinocerebellar ataxia type 3]) as one of the most common types of dominantly inherited spinocerebellar ataxias. sapropterin 65-68 ataxin 3 Homo sapiens 116-120 11396263-4 2001 METHODS: Genotyping was based on cytosine-adenine-guanine (CAG)-repeat expansion detection in the SCA1, SCA2, SCA3, SCA6 and SCA7 genes. cytosine-adenine-guanine 33-57 ataxin 3 Homo sapiens 110-114 11396263-4 2001 METHODS: Genotyping was based on cytosine-adenine-guanine (CAG)-repeat expansion detection in the SCA1, SCA2, SCA3, SCA6 and SCA7 genes. GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER] 59-62 ataxin 3 Homo sapiens 110-114 11396263-12 2001 The length of the trinucleotide repeat accounted for 65% of the variance in age of onset in SCA3. trinucleotide 18-31 ataxin 3 Homo sapiens 92-96 10069576-1 1998 Spinocerebellar ataxia type 3 or Machado-Joseph disease (SCA3/MJD) is an autosomal dominant neurodegenerative disorder caused by an unstable and expanded CAG trinucleotide repeat that leads to the expansion of a polyglutamine tract in a protein of unknown function, ataxin-3. trinucleotide 158-171 ataxin 3 Homo sapiens 266-274 10993685-2 2000 The gene responsible for the disease, a novel gene of unknown function, encodes ataxin-3 containing a polyglutamine stretch. polyglutamine 102-115 ataxin 3 Homo sapiens 80-88 10993685-7 2000 These results were confirmed in the same inclusions by double immunofluorescent staining, suggesting that expanded ataxin-3 forms a core, thereby recruiting wild-type ataxin-3 into the nucleus around the core portion, and then followed by activation of the ubiquitin/ATP-dependent pathway. Adenosine Triphosphate 267-270 ataxin 3 Homo sapiens 115-123 10942424-0 2000 CAG tract of MJD-1 may be prone to frameshifts causing polyalanine accumulation. polyalanine 55-66 ataxin 3 Homo sapiens 13-18 10915768-1 2000 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 158-162 10915768-1 2000 Machado-Joseph disease (MJD) is an autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. polyglutamine 111-124 ataxin 3 Homo sapiens 177-185 11002696-5 2000 RESULTS: Analysis of the SCA3/MJD CAG trinucleotide repeat at the ataxin 3 gene in the DNA of the proband and one of his daughters demonstrated an expanded allele of 63 CAG repeat units. trinucleotide 38-51 ataxin 3 Homo sapiens 66-74 10556285-0 1999 Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix. polyglutamine 55-68 ataxin 3 Homo sapiens 0-8 10556285-6 1999 In addition, expression of ataxin-3 within the nucleus exposes the glutamine domain of the full-length non-pathological protein, allowing it to bind the monoclonal antibody 1C2. Glutamine 67-76 ataxin 3 Homo sapiens 27-35 10556285-7 1999 Fractionation and immunochemical experiments indicate that this novel conformation of intranuclear ataxin-3 is not due to proteolysis, suggesting instead that association with nuclear protein(s) alters the structure of full-length ataxin-3 which exposes the polyglutamine domain. polyglutamine 258-271 ataxin 3 Homo sapiens 99-107 10556285-7 1999 Fractionation and immunochemical experiments indicate that this novel conformation of intranuclear ataxin-3 is not due to proteolysis, suggesting instead that association with nuclear protein(s) alters the structure of full-length ataxin-3 which exposes the polyglutamine domain. polyglutamine 258-271 ataxin 3 Homo sapiens 231-239 10556285-9 1999 The pathological form of ataxin-3 with an expanded polyglutamine domain also associates with the nuclear matrix. polyglutamine 51-64 ataxin 3 Homo sapiens 25-33 10556285-10 1999 These data suggest that an early event in the pathogenesis of SCA3/MJD may be an altered conformation of ataxin-3 within the nucleus that exposes the polyglutamine domain. polyglutamine 150-163 ataxin 3 Homo sapiens 62-66 10556285-10 1999 These data suggest that an early event in the pathogenesis of SCA3/MJD may be an altered conformation of ataxin-3 within the nucleus that exposes the polyglutamine domain. polyglutamine 150-163 ataxin 3 Homo sapiens 67-70 10556285-10 1999 These data suggest that an early event in the pathogenesis of SCA3/MJD may be an altered conformation of ataxin-3 within the nucleus that exposes the polyglutamine domain. polyglutamine 150-163 ataxin 3 Homo sapiens 105-113 10072437-0 1999 Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. polyglutamine 39-52 ataxin 3 Homo sapiens 100-104 10072437-0 1999 Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. polyglutamine 39-52 ataxin 3 Homo sapiens 105-108 10072437-1 1999 Spinocerebellar ataxia type 3, also known as Machado-Joseph disease (SCA3/MJD), is one of at least eight inherited neurodegenerative diseases caused by expansion of a polyglutamine tract in the disease protein. polyglutamine 167-180 ataxin 3 Homo sapiens 69-73 10072437-1 1999 Spinocerebellar ataxia type 3, also known as Machado-Joseph disease (SCA3/MJD), is one of at least eight inherited neurodegenerative diseases caused by expansion of a polyglutamine tract in the disease protein. polyglutamine 167-180 ataxin 3 Homo sapiens 74-77 10928570-4 2000 The first type of mutation present in SCA1, SCA2, SCA3, and SCA7 is an expanded CAG repeat in genes of unknown function that are translated into proteins with expanded polyglutamine tracts. polyglutamine 168-181 ataxin 3 Homo sapiens 50-54 10712199-2 2000 The mutant proteins have shown an expanded polyglutamine tract in SCA1, SCA2, MJD/SCA3, SCA6, SCA7, and DRPLA; a glycine-to-arginine substitution was found in SCA6 as well. polyglutamine 43-56 ataxin 3 Homo sapiens 82-86 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. Arginine 124-132 ataxin 3 Homo sapiens 82-86 10465503-1 1999 Variation in the number of CAG repeats in the Machado-Joseph disease gene (MJD1) was examined by polymerase chain reaction and denaturing polyacrylamide gel electrophoresis analysis of 2134 normal and 135 affected chromosomes of Japanese individuals. polyacrylamide 138-152 ataxin 3 Homo sapiens 75-79 10465503-7 1999 The observed distribution peak of normal MJD1 alleles corresponding to peptides containing 10, 15, 20, and 24 glutamine suggests that stretches of 5 and 10 glutamine might constitute a functional domain of human MJD1. Glutamine 110-119 ataxin 3 Homo sapiens 41-45 10465503-7 1999 The observed distribution peak of normal MJD1 alleles corresponding to peptides containing 10, 15, 20, and 24 glutamine suggests that stretches of 5 and 10 glutamine might constitute a functional domain of human MJD1. Glutamine 110-119 ataxin 3 Homo sapiens 212-216 10465503-7 1999 The observed distribution peak of normal MJD1 alleles corresponding to peptides containing 10, 15, 20, and 24 glutamine suggests that stretches of 5 and 10 glutamine might constitute a functional domain of human MJD1. Glutamine 156-165 ataxin 3 Homo sapiens 41-45 10465503-7 1999 The observed distribution peak of normal MJD1 alleles corresponding to peptides containing 10, 15, 20, and 24 glutamine suggests that stretches of 5 and 10 glutamine might constitute a functional domain of human MJD1. Glutamine 156-165 ataxin 3 Homo sapiens 212-216 9852144-2 1998 Here in cell-based studies of the spinocerebellar ataxia type-3 disease protein, ataxin-3, we address two issues central to aggregation: the role of polyglutamine in recruiting proteins into NI and the role of nuclear localization in promoting aggregation. polyglutamine 149-162 ataxin 3 Homo sapiens 81-89 9852144-5 1998 Finally, we show that nuclear localization promotes aggregation: an ataxin-3 fragment containing a nonpathologic repeat of 27 glutamines forms inclusions only when targeted to the nucleus. Glutamine 126-136 ataxin 3 Homo sapiens 68-76 10069576-1 1998 Spinocerebellar ataxia type 3 or Machado-Joseph disease (SCA3/MJD) is an autosomal dominant neurodegenerative disorder caused by an unstable and expanded CAG trinucleotide repeat that leads to the expansion of a polyglutamine tract in a protein of unknown function, ataxin-3. polyglutamine 212-225 ataxin 3 Homo sapiens 266-274 10069576-6 1998 In the brain, only one ataxin-3 isoform containing the polyglutamine stretch was detected, and normal and mutated proteins were found equally expressed in all patient brain regions analyzed. polyglutamine 55-68 ataxin 3 Homo sapiens 23-31 9758625-3 1998 The relative prevalences of MJD/SCA3, SCA6, and DRPLA were significantly higher in Japanese pedigrees (43%, 11%, and 20%, respectively) than in Caucasian pedigrees (30%, 5%, and 0%, respectively), corresponding to the observation that the frequencies of large ANs of MJD/SCA3 (>27 repeats), SCA6 (>13 repeats), and DRPLA (>17 repeats) were significantly higher in Japanese than in Caucasians. 1-anilino-8-naphthalenesulfonate 260-263 ataxin 3 Homo sapiens 28-31 9630233-6 1998 In 5 of them (SCA-1, SCA-2, SCA-3, SCA-6, and SCA-7), expanded cytosine-adenine-guanine (CAG)-trinucleotide repeats and their abnormal gene products cause the ataxic condition. cytosine-adenine-guanine 63-87 ataxin 3 Homo sapiens 28-33 9635424-1 1998 Spinocerebellar ataxia type 3 (SCA3/MJD) is one of at least eight human neurodegenerative diseases caused by glutamine-repeat expansion. Glutamine 109-118 ataxin 3 Homo sapiens 31-35 9635424-1 1998 Spinocerebellar ataxia type 3 (SCA3/MJD) is one of at least eight human neurodegenerative diseases caused by glutamine-repeat expansion. Glutamine 109-118 ataxin 3 Homo sapiens 36-39 9635424-2 1998 We have recreated glutamine-repeat disease in Drosophila using a segment of the SCA3/MJD protein. Glutamine 18-27 ataxin 3 Homo sapiens 80-84 9635424-2 1998 We have recreated glutamine-repeat disease in Drosophila using a segment of the SCA3/MJD protein. Glutamine 18-27 ataxin 3 Homo sapiens 85-88 9580663-1 1998 It has been reported that the ataxin-3 protein containing a polyglutamine sequence in the pathological range (61-84Q) is localized within the nucleus of neuronal cells, whereas ataxin-3 with a normal repeat length (12-37Q) is predominantly a cytoplasmic protein. polyglutamine 60-73 ataxin 3 Homo sapiens 30-38 9580663-2 1998 In this study, the subcellular localization of the full-length ataxin-3 protein with a glutamine sequence in the normal range (Q3KQ22) was analysed in two mammalian cell lines. Glutamine 87-96 ataxin 3 Homo sapiens 63-71 9580663-3 1998 Using two affinity-purified polyclonal antibodies raised against the N- or C-terminal portion of ataxin-3, the protein was detected predominantly, but not exclusively, in the nucleus of COS-7 as well as neuroblastoma cells by immunofluorescence and confocal laser scanning microscopy (CLSM). carbonyl sulfide 186-189 ataxin 3 Homo sapiens 97-105 9630233-13 1998 In SCA-3, abnormal ataxin-3 is aggregated in neuronal nuclei, and in SCA-6, a mutated alpha1A-calcium channel protein is the likely cause of abnormal calcium channel function in Purkinje cells and in the death of these neurons. Calcium 94-101 ataxin 3 Homo sapiens 19-27 9215676-0 1997 Single sperm analysis of the CAG repeats in the gene for Machado-Joseph disease (MJD1): evidence for non-Mendelian transmission of the MJD1 gene and for the effect of the intragenic CGG/GGG polymorphism on the intergenerational instability. ggg 186-189 ataxin 3 Homo sapiens 81-85 9215676-4 1997 These findings in single sperm confirm non-Mendelian transmission of the MJD1 gene and the effect of the intragenic CGG/GGG polymorphism on the intergenerational instability of the CAG repeats in the MJD1 gene, which have been observed in clinical and genetic studies. ggg 120-123 ataxin 3 Homo sapiens 200-204 9153459-7 1997 The length of trinucleotide repeats in the MJD1 gene was in the normal range for all affected individuals. trinucleotide 14-27 ataxin 3 Homo sapiens 43-47 9023182-3 1997 strain AT3 grew with dl-tropic acid, the aromatic component of the alkaloid atropine, as the sole source of carbon and energy. tropic acid 21-35 ataxin 3 Homo sapiens 7-10 9023182-3 1997 strain AT3 grew with dl-tropic acid, the aromatic component of the alkaloid atropine, as the sole source of carbon and energy. Alkaloids 67-75 ataxin 3 Homo sapiens 7-10 9023182-3 1997 strain AT3 grew with dl-tropic acid, the aromatic component of the alkaloid atropine, as the sole source of carbon and energy. Atropine 76-84 ataxin 3 Homo sapiens 7-10 9023182-3 1997 strain AT3 grew with dl-tropic acid, the aromatic component of the alkaloid atropine, as the sole source of carbon and energy. Carbon 108-114 ataxin 3 Homo sapiens 7-10 8968739-1 1996 Expansion of trinucleotide CAG repeats coding for polyglutamine has been implicated in five neurodegenerative disorders, including spinocerebellar ataxia (SCA) 1 and SCA3 or Machado-Joseph disease (SCA3/MJD), two forms of type I autosomal dominant cerebellar ataxias (ADCA). trinucleotide 13-26 ataxin 3 Homo sapiens 166-170 8968739-1 1996 Expansion of trinucleotide CAG repeats coding for polyglutamine has been implicated in five neurodegenerative disorders, including spinocerebellar ataxia (SCA) 1 and SCA3 or Machado-Joseph disease (SCA3/MJD), two forms of type I autosomal dominant cerebellar ataxias (ADCA). polyglutamine 50-63 ataxin 3 Homo sapiens 166-170