PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33772540-8 2021 The similarities between the ataxin-1 and the huntingtin responses to DNA damage provide further support for a shared pathogenic mechanism for polyglutamine expansion diseases. polyglutamine 143-156 huntingtin Drosophila melanogaster 46-56 34973473-1 2022 Huntington"s disease (HD) is a late-onset; progressive, dominantly inherited neurological disorder marked by an abnormal expansion of polyglutamine (poly Q) repeats in Huntingtin (HTT) protein. polyglutamine 134-147 huntingtin Drosophila melanogaster 168-178 34973473-1 2022 Huntington"s disease (HD) is a late-onset; progressive, dominantly inherited neurological disorder marked by an abnormal expansion of polyglutamine (poly Q) repeats in Huntingtin (HTT) protein. polyglutamine 134-147 huntingtin Drosophila melanogaster 180-183 34973473-1 2022 Huntington"s disease (HD) is a late-onset; progressive, dominantly inherited neurological disorder marked by an abnormal expansion of polyglutamine (poly Q) repeats in Huntingtin (HTT) protein. polyglutamine 149-155 huntingtin Drosophila melanogaster 168-178 34973473-1 2022 Huntington"s disease (HD) is a late-onset; progressive, dominantly inherited neurological disorder marked by an abnormal expansion of polyglutamine (poly Q) repeats in Huntingtin (HTT) protein. polyglutamine 149-155 huntingtin Drosophila melanogaster 180-183 32941796-1 2021 Poly-glutamine expansion near the N-terminus of the huntingtin protein (HTT) is the prime determinant of Huntington"s disease (HD) pathology; however, post-translational modifications and protein context are also reported to influence poly-glutamine induced HD toxicity. polyglutamine 0-14 huntingtin Drosophila melanogaster 52-62 34914364-0 2021 Polyglutamine-Specific Gold Nanoparticle Complex Alleviates Mutant Huntingtin-Induced Toxicity. polyglutamine 0-13 huntingtin Drosophila melanogaster 67-77 32941796-1 2021 Poly-glutamine expansion near the N-terminus of the huntingtin protein (HTT) is the prime determinant of Huntington"s disease (HD) pathology; however, post-translational modifications and protein context are also reported to influence poly-glutamine induced HD toxicity. polyglutamine 0-14 huntingtin Drosophila melanogaster 72-75 32941796-1 2021 Poly-glutamine expansion near the N-terminus of the huntingtin protein (HTT) is the prime determinant of Huntington"s disease (HD) pathology; however, post-translational modifications and protein context are also reported to influence poly-glutamine induced HD toxicity. polyglutamine 235-249 huntingtin Drosophila melanogaster 52-62 32941796-1 2021 Poly-glutamine expansion near the N-terminus of the huntingtin protein (HTT) is the prime determinant of Huntington"s disease (HD) pathology; however, post-translational modifications and protein context are also reported to influence poly-glutamine induced HD toxicity. polyglutamine 235-249 huntingtin Drosophila melanogaster 72-75 32967102-2 2020 As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. polyglutamine 77-90 huntingtin Drosophila melanogaster 37-47 32975927-12 2020 In both models, novel htt-ex1-betaHP analogues exhibiting strong aggregation in spite of their very short polyQ repeat lengths proved to be toxic, dramatically breaking the "repeat length paradigm" and strongly suggesting that the toxic species must be some kind of aggregate. polyglutamine 106-111 huntingtin Drosophila melanogaster 22-25 28871787-1 2017 Huntington"s disease (HD) is a neurodegenerative disorder induced by aggregation of the pathological form of Huntingtin protein that has expanded polyglutamine (polyQ) repeats. polyglutamine 146-159 huntingtin Drosophila melanogaster 109-119 30171891-4 2018 Additional modifications within the polyQ segment produce htt exon1 analogs that populate only spherical oligomers and are non-toxic in cells and flies. polyglutamine 36-41 huntingtin Drosophila melanogaster 58-61 30171891-5 2018 Furthermore, in mixture with expanded-polyQ htt exon1, the latter analogs in vitro suppress amyloid formation and promote oligomer formation, and in vivo rescue neurons and flies expressing mhtt exon1 from dysfunction and death. polyglutamine 38-43 huntingtin Drosophila melanogaster 44-47 30171891-6 2018 Thus, in our experiments, while htt exon1 toxicity tracks with aggregation propensity, it does so in spite of the toxic construct"s possessing polyQ tracts well below those normally considered to be disease-associated. polyglutamine 143-148 huntingtin Drosophila melanogaster 32-35 28871787-1 2017 Huntington"s disease (HD) is a neurodegenerative disorder induced by aggregation of the pathological form of Huntingtin protein that has expanded polyglutamine (polyQ) repeats. polyglutamine 161-166 huntingtin Drosophila melanogaster 109-119 28235896-1 2017 Huntington"s disease (HD) is a neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) stretch within the Huntingtin (Htt) protein. polyglutamine 83-96 huntingtin Drosophila melanogaster 124-134 28235896-1 2017 Huntington"s disease (HD) is a neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) stretch within the Huntingtin (Htt) protein. polyglutamine 83-96 huntingtin Drosophila melanogaster 136-139 28235896-1 2017 Huntington"s disease (HD) is a neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) stretch within the Huntingtin (Htt) protein. polyglutamine 98-103 huntingtin Drosophila melanogaster 124-134 28235896-1 2017 Huntington"s disease (HD) is a neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) stretch within the Huntingtin (Htt) protein. polyglutamine 98-103 huntingtin Drosophila melanogaster 136-139 27506601-1 2016 Huntington"s disease (HD) is late-onset, progressive neurodegenerative disorder caused by expansion of polyglutamine (polyQ) repeat within Huntingtin (Htt) protein. polyglutamine 103-116 huntingtin Drosophila melanogaster 139-149 27506601-1 2016 Huntington"s disease (HD) is late-onset, progressive neurodegenerative disorder caused by expansion of polyglutamine (polyQ) repeat within Huntingtin (Htt) protein. polyglutamine 103-116 huntingtin Drosophila melanogaster 151-154 27506601-1 2016 Huntington"s disease (HD) is late-onset, progressive neurodegenerative disorder caused by expansion of polyglutamine (polyQ) repeat within Huntingtin (Htt) protein. polyglutamine 118-123 huntingtin Drosophila melanogaster 139-149 27506601-1 2016 Huntington"s disease (HD) is late-onset, progressive neurodegenerative disorder caused by expansion of polyglutamine (polyQ) repeat within Huntingtin (Htt) protein. polyglutamine 118-123 huntingtin Drosophila melanogaster 151-154 26920069-2 2016 The polyQ expansion increases the propensity of htt to aggregate and accumulate, and manipulations that mitigate protein misfolding or facilitate the clearance of misfolded proteins are predicted to slow disease progression in HD models. polyglutamine 4-9 huntingtin Drosophila melanogaster 48-51 26728250-1 2016 Huntington"s disease (HD) is a progressive, dominantly inherited neurological disorder caused by an abnormal expansion of polyglutamine (polyQ) repeat within the Huntingtin (Htt) protein with no disease modifying treatments. polyglutamine 122-135 huntingtin Drosophila melanogaster 162-172 26728250-1 2016 Huntington"s disease (HD) is a progressive, dominantly inherited neurological disorder caused by an abnormal expansion of polyglutamine (polyQ) repeat within the Huntingtin (Htt) protein with no disease modifying treatments. polyglutamine 122-135 huntingtin Drosophila melanogaster 174-177 26728250-1 2016 Huntington"s disease (HD) is a progressive, dominantly inherited neurological disorder caused by an abnormal expansion of polyglutamine (polyQ) repeat within the Huntingtin (Htt) protein with no disease modifying treatments. polyglutamine 137-142 huntingtin Drosophila melanogaster 162-172 26728250-1 2016 Huntington"s disease (HD) is a progressive, dominantly inherited neurological disorder caused by an abnormal expansion of polyglutamine (polyQ) repeat within the Huntingtin (Htt) protein with no disease modifying treatments. polyglutamine 137-142 huntingtin Drosophila melanogaster 174-177 26728250-2 2016 In a Drosophila model of HD, expression of mutant Huntingtin (Htt) protein with expanded polyQ leads to formation of inclusion bodies (IBs), increase in cellular toxicity, progression of motor disabilities and reduced viability. polyglutamine 89-94 huntingtin Drosophila melanogaster 50-60 26728250-2 2016 In a Drosophila model of HD, expression of mutant Huntingtin (Htt) protein with expanded polyQ leads to formation of inclusion bodies (IBs), increase in cellular toxicity, progression of motor disabilities and reduced viability. polyglutamine 89-94 huntingtin Drosophila melanogaster 62-65 25848931-1 2015 Huntington"s disease (HD) is a currently incurable neurodegenerative condition caused by an abnormally expanded polyglutamine tract in huntingtin (HTT). polyglutamine 112-125 huntingtin Drosophila melanogaster 135-145 27309588-1 2016 Polyglutamine (polyQ) expansion within Huntingtin (Htt) causes the fatal neurodegenerative disorder Huntington"s Disease (HD). polyglutamine 0-13 huntingtin Drosophila melanogaster 39-49 27309588-1 2016 Polyglutamine (polyQ) expansion within Huntingtin (Htt) causes the fatal neurodegenerative disorder Huntington"s Disease (HD). polyglutamine 0-13 huntingtin Drosophila melanogaster 51-54 27309588-1 2016 Polyglutamine (polyQ) expansion within Huntingtin (Htt) causes the fatal neurodegenerative disorder Huntington"s Disease (HD). polyglutamine 15-20 huntingtin Drosophila melanogaster 39-49 27309588-1 2016 Polyglutamine (polyQ) expansion within Huntingtin (Htt) causes the fatal neurodegenerative disorder Huntington"s Disease (HD). polyglutamine 15-20 huntingtin Drosophila melanogaster 51-54 25848931-1 2015 Huntington"s disease (HD) is a currently incurable neurodegenerative condition caused by an abnormally expanded polyglutamine tract in huntingtin (HTT). polyglutamine 112-125 huntingtin Drosophila melanogaster 147-150 25761110-1 2015 Huntington"s disease is a neurodegenerative disorder caused by toxic insertions of polyglutamine residues in the Huntingtin protein and characterized by progressive deterioration of cognitive and motor functions. polyglutamine 83-96 huntingtin Drosophila melanogaster 113-123 25305076-1 2015 Although Huntington"s disease is caused by the expansion of a CAG triplet repeat within the context of the 3144-amino acid huntingtin protein (HTT), studies reveal that N-terminal fragments of HTT containing the expanded PolyQ region can be produced by proteolytic processing and/or aberrant splicing. polyglutamine 221-226 huntingtin Drosophila melanogaster 123-133 25305076-1 2015 Although Huntington"s disease is caused by the expansion of a CAG triplet repeat within the context of the 3144-amino acid huntingtin protein (HTT), studies reveal that N-terminal fragments of HTT containing the expanded PolyQ region can be produced by proteolytic processing and/or aberrant splicing. polyglutamine 221-226 huntingtin Drosophila melanogaster 193-196 26942103-2 2014 Cardiac disease is the second leading cause of death in HD, which has been mainly studied as a neurodegenerative disease that is caused by expanded polyglutamine repeats in the huntingtin protein. polyglutamine 148-161 huntingtin Drosophila melanogaster 177-187 23980182-1 2013 Huntington disease (HD) is a progressive neurodegenerative disorder caused by dominant polyglutamine (polyQ) expansion within the N terminus of huntingtin (Htt) protein. polyglutamine 87-100 huntingtin Drosophila melanogaster 144-154 24022020-1 2013 Huntington disease (HD) is an inherited neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the huntingtin (Htt) gene. polyglutamine 79-92 huntingtin Drosophila melanogaster 118-128 24022020-1 2013 Huntington disease (HD) is an inherited neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the huntingtin (Htt) gene. polyglutamine 79-92 huntingtin Drosophila melanogaster 130-133 24022020-1 2013 Huntington disease (HD) is an inherited neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the huntingtin (Htt) gene. polyglutamine 94-99 huntingtin Drosophila melanogaster 118-128 24022020-1 2013 Huntington disease (HD) is an inherited neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the huntingtin (Htt) gene. polyglutamine 94-99 huntingtin Drosophila melanogaster 130-133 23980182-1 2013 Huntington disease (HD) is a progressive neurodegenerative disorder caused by dominant polyglutamine (polyQ) expansion within the N terminus of huntingtin (Htt) protein. polyglutamine 87-100 huntingtin Drosophila melanogaster 156-159 23980182-1 2013 Huntington disease (HD) is a progressive neurodegenerative disorder caused by dominant polyglutamine (polyQ) expansion within the N terminus of huntingtin (Htt) protein. polyglutamine 102-107 huntingtin Drosophila melanogaster 144-154 23980182-1 2013 Huntington disease (HD) is a progressive neurodegenerative disorder caused by dominant polyglutamine (polyQ) expansion within the N terminus of huntingtin (Htt) protein. polyglutamine 102-107 huntingtin Drosophila melanogaster 156-159 23980182-7 2013 Strikingly, substitution of two potential copper-binding residues of Htt, Met8 and His82, completely dissociates the copper-intensifying toxicity of Htt exon1-polyQ. polyglutamine 159-164 huntingtin Drosophila melanogaster 69-72 23980182-7 2013 Strikingly, substitution of two potential copper-binding residues of Htt, Met8 and His82, completely dissociates the copper-intensifying toxicity of Htt exon1-polyQ. polyglutamine 159-164 huntingtin Drosophila melanogaster 149-152 24367279-1 2013 Amyloid-like inclusions have been associated with Huntington"s disease (HD), which is caused by expanded polyglutamine repeats in the Huntingtin protein. polyglutamine 105-118 huntingtin Drosophila melanogaster 134-144 23652004-2 2013 Here we show that transitional endoplasmic reticulum ATPase (TERA)/valosin-containing protein (VCP)/p97 directly binds to multiple polyglutamine disease proteins (huntingtin, ataxin-1, ataxin-7 and androgen receptor) via polyglutamine sequence. polyglutamine 131-144 huntingtin Drosophila melanogaster 163-173 23555909-1 2013 Huntington"s disease (HD) is a devastating dominantly inherited neurodegenerative disorder caused by an abnormal polyglutamine expansion in the N-terminal part of the huntingtin (HTT) protein. polyglutamine 113-126 huntingtin Drosophila melanogaster 167-177 23555909-1 2013 Huntington"s disease (HD) is a devastating dominantly inherited neurodegenerative disorder caused by an abnormal polyglutamine expansion in the N-terminal part of the huntingtin (HTT) protein. polyglutamine 113-126 huntingtin Drosophila melanogaster 179-182 24367279-3 2013 We have generated a Drosophila model of cardiac amyloidosis that exhibits accumulation of PolyQ aggregates and oxidative stress in myocardial cells, upon heart-specific expression of Huntingtin protein fragments (Htt-PolyQ) with disease-causing poly-glutamine repeats (PolyQ-46, PolyQ-72, and PolyQ-102). polyglutamine 245-259 huntingtin Drosophila melanogaster 183-193 24367279-3 2013 We have generated a Drosophila model of cardiac amyloidosis that exhibits accumulation of PolyQ aggregates and oxidative stress in myocardial cells, upon heart-specific expression of Huntingtin protein fragments (Htt-PolyQ) with disease-causing poly-glutamine repeats (PolyQ-46, PolyQ-72, and PolyQ-102). polyglutamine 245-259 huntingtin Drosophila melanogaster 213-216 24367279-4 2013 Cardiac expression of GFP-tagged Htt-PolyQs resulted in PolyQ length-dependent functional defects that included increased incidence of arrhythmias and extreme cardiac dilation, accompanied by a significant decrease in contractility. polyglutamine 37-43 huntingtin Drosophila melanogaster 33-36 24367279-4 2013 Cardiac expression of GFP-tagged Htt-PolyQs resulted in PolyQ length-dependent functional defects that included increased incidence of arrhythmias and extreme cardiac dilation, accompanied by a significant decrease in contractility. polyglutamine 37-42 huntingtin Drosophila melanogaster 33-36 22466800-2 2012 The polyglutamine expansion in the huntingtin (htt) protein that underlies this disorder leads to perturbations in many cellular pathways, including the disruption of Rab11-dependent endosomal recycling. polyglutamine 4-17 huntingtin Drosophila melanogaster 35-45 22733771-6 2012 Increased microtubule dynamics and global neuronal stabilization were also activated by expression of expanded polyglutamine (poly-Q) proteins SCA1, SCA3, and huntingtin. polyglutamine 111-124 huntingtin Drosophila melanogaster 159-169 22733771-6 2012 Increased microtubule dynamics and global neuronal stabilization were also activated by expression of expanded polyglutamine (poly-Q) proteins SCA1, SCA3, and huntingtin. polyglutamine 126-132 huntingtin Drosophila melanogaster 159-169 22817726-1 2012 HD (Huntington"s disease) is a fatal inherited gain-of-function disorder caused by a polyQ (polyglutamine) expansion in the htt (huntingtin protein). polyglutamine 85-90 huntingtin Drosophila melanogaster 124-127 22817726-1 2012 HD (Huntington"s disease) is a fatal inherited gain-of-function disorder caused by a polyQ (polyglutamine) expansion in the htt (huntingtin protein). polyglutamine 85-90 huntingtin Drosophila melanogaster 129-139 22817726-1 2012 HD (Huntington"s disease) is a fatal inherited gain-of-function disorder caused by a polyQ (polyglutamine) expansion in the htt (huntingtin protein). polyglutamine 92-105 huntingtin Drosophila melanogaster 124-127 22817726-1 2012 HD (Huntington"s disease) is a fatal inherited gain-of-function disorder caused by a polyQ (polyglutamine) expansion in the htt (huntingtin protein). polyglutamine 92-105 huntingtin Drosophila melanogaster 129-139 22466800-2 2012 The polyglutamine expansion in the huntingtin (htt) protein that underlies this disorder leads to perturbations in many cellular pathways, including the disruption of Rab11-dependent endosomal recycling. polyglutamine 4-17 huntingtin Drosophila melanogaster 47-50 21912091-1 2012 Huntingtin peptides with elongated polyglutamine domains, the root causes of Huntington"s disease, hinder histone acetylation, which leads to transcriptional dysregulation. polyglutamine 35-48 huntingtin Drosophila melanogaster 0-10 22634544-1 2012 Huntington disease (HD) is a fatal inherited neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin protein (htt). polyglutamine 84-97 huntingtin Drosophila melanogaster 115-133 22634544-1 2012 Huntington disease (HD) is a fatal inherited neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin protein (htt). polyglutamine 84-97 huntingtin Drosophila melanogaster 135-138 21909362-2 2011 Drosophila primary neurons offer a sensitive readout for neurotoxicty, as their neurites develop dysmorphic features in the presence of mutant polyglutamine-expanded Huntingtin compared to nonpathogenic Huntingtin. polyglutamine 143-156 huntingtin Drosophila melanogaster 166-176 21700213-1 2011 Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine expansion within Huntingtin (Htt) protein. polyglutamine 70-83 huntingtin Drosophila melanogaster 101-111 21700213-1 2011 Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine expansion within Huntingtin (Htt) protein. polyglutamine 70-83 huntingtin Drosophila melanogaster 113-116 21636279-2 2011 A central hallmark of HD is neurodegeneration caused by a polyglutamine expansion in the huntingtin (htt) protein [2]. polyglutamine 58-71 huntingtin Drosophila melanogaster 89-99 21636279-2 2011 A central hallmark of HD is neurodegeneration caused by a polyglutamine expansion in the huntingtin (htt) protein [2]. polyglutamine 58-71 huntingtin Drosophila melanogaster 101-104 22180703-4 2011 Increasing experimental evidence from genetic model systems such as mice, zebrafish, and Drosophila suggest that polyglutamine expansion within the Huntingtin protein also disrupts its normal biological function. polyglutamine 113-126 huntingtin Drosophila melanogaster 148-158 20100940-4 2010 We generated transgenic fly lines that express enhanced-GFP-tagged mutant Huntingtin (Htt) fragments with different lengths of polyglutamine (polyQ) tract and showed that these Htt mutants develop protein aggregates in a polyQ-length- and age-dependent manner in Drosophila. polyglutamine 127-140 huntingtin Drosophila melanogaster 74-84 21087194-1 2010 Huntington"s disease is an autosomal dominant neurodegenerative disorder that is caused by abnormal expansion of a polyglutamine tract in the huntingtin protein, resulting in intracellular aggregate formation and neurodegeneration. polyglutamine 115-128 huntingtin Drosophila melanogaster 142-152 20336775-4 2010 Recently, the compound B2 has been shown to increase inclusion formation and decrease toxicity of polyglutamine-expanded huntingtin in cultured cells. polyglutamine 98-111 huntingtin Drosophila melanogaster 121-131 20531388-6 2010 As a consequence, the beta-transducin repeat-containing protein (beta-TrCP) rescues polyglutamine (polyQ)-huntingtin-induced toxicity in striatal neurons and in a Drosophila model of HD, through the specific degradation of beta-catenin. polyglutamine 84-97 huntingtin Drosophila melanogaster 106-116 20531388-6 2010 As a consequence, the beta-transducin repeat-containing protein (beta-TrCP) rescues polyglutamine (polyQ)-huntingtin-induced toxicity in striatal neurons and in a Drosophila model of HD, through the specific degradation of beta-catenin. polyglutamine 99-104 huntingtin Drosophila melanogaster 106-116 20399860-1 2010 Huntington"s disease (HD) is a lethal, neurodegenerative disorder caused by expansion of the polyglutamine repeat in the Huntingtin gene (HTT), leading to mutant protein misfolding, aggregation, and neuronal death. polyglutamine 93-106 huntingtin Drosophila melanogaster 121-131 20399860-1 2010 Huntington"s disease (HD) is a lethal, neurodegenerative disorder caused by expansion of the polyglutamine repeat in the Huntingtin gene (HTT), leading to mutant protein misfolding, aggregation, and neuronal death. polyglutamine 93-106 huntingtin Drosophila melanogaster 138-141 20100940-4 2010 We generated transgenic fly lines that express enhanced-GFP-tagged mutant Huntingtin (Htt) fragments with different lengths of polyglutamine (polyQ) tract and showed that these Htt mutants develop protein aggregates in a polyQ-length- and age-dependent manner in Drosophila. polyglutamine 127-140 huntingtin Drosophila melanogaster 177-180 20100940-4 2010 We generated transgenic fly lines that express enhanced-GFP-tagged mutant Huntingtin (Htt) fragments with different lengths of polyglutamine (polyQ) tract and showed that these Htt mutants develop protein aggregates in a polyQ-length- and age-dependent manner in Drosophila. polyglutamine 142-147 huntingtin Drosophila melanogaster 177-180 19380309-1 2009 A polyglutamine expansion in the huntingtin (HTT) gene causes neurodegeneration in Huntington"s disease (HD), but the in vivo function of the native protein (Htt) is largely unknown. polyglutamine 2-15 huntingtin Drosophila melanogaster 33-43 19380309-1 2009 A polyglutamine expansion in the huntingtin (HTT) gene causes neurodegeneration in Huntington"s disease (HD), but the in vivo function of the native protein (Htt) is largely unknown. polyglutamine 2-15 huntingtin Drosophila melanogaster 45-48 19268537-1 2009 Huntington"s Disease is a neurodegenerative condition caused by a polyglutamine expansion in the huntingtin (Htt) protein, which aggregates and also causes neuronal dysfunction. polyglutamine 66-79 huntingtin Drosophila melanogaster 97-107 19268537-1 2009 Huntington"s Disease is a neurodegenerative condition caused by a polyglutamine expansion in the huntingtin (Htt) protein, which aggregates and also causes neuronal dysfunction. polyglutamine 66-79 huntingtin Drosophila melanogaster 109-112 18430781-1 2008 Huntington disease (HD) is caused by a polyglutamine-expansion mutation in huntingtin (HTT) that makes the protein toxic and aggregate-prone. polyglutamine 39-52 huntingtin Drosophila melanogaster 75-85 18417352-1 2008 Huntington"s disease is caused by polyglutamine expansion in the huntingtin protein. polyglutamine 34-47 huntingtin Drosophila melanogaster 65-75 18423405-1 2008 Polyglutamine expansion in huntingtin (Htt) and the androgen receptor (AR) causes untreatable neurodegenerative diseases. polyglutamine 0-13 huntingtin Drosophila melanogaster 27-37 18423405-1 2008 Polyglutamine expansion in huntingtin (Htt) and the androgen receptor (AR) causes untreatable neurodegenerative diseases. polyglutamine 0-13 huntingtin Drosophila melanogaster 39-42 18430781-1 2008 Huntington disease (HD) is caused by a polyglutamine-expansion mutation in huntingtin (HTT) that makes the protein toxic and aggregate-prone. polyglutamine 39-52 huntingtin Drosophila melanogaster 87-90 16497721-3 2006 We previously showed that rapamycin protects against mutant huntingtin-induced neurodegeneration in cell, fly and mouse models of Huntington"s disease [Ravikumar, B., Duden, R. and Rubinsztein, D.C. (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. polyglutamine 236-249 huntingtin Drosophila melanogaster 60-70 18065778-1 2008 Huntington"s disease (HD) is caused by an extended polyglutamine (polyQ) tract in the Huntingtin protein. polyglutamine 51-64 huntingtin Drosophila melanogaster 86-96 18065778-1 2008 Huntington"s disease (HD) is caused by an extended polyglutamine (polyQ) tract in the Huntingtin protein. polyglutamine 66-71 huntingtin Drosophila melanogaster 86-96 17961788-1 2007 Huntington disease is caused by polyglutamine expansion in huntingtin, a 350 kD protein that is ubiquitously expressed and widely distributed at the subcellular level. polyglutamine 32-45 huntingtin Drosophila melanogaster 59-69 11607033-4 2001 Here we show that the polyglutamine-containing domain of Htt, Htt exon 1 protein (Httex1p), directly binds the acetyltransferase domains of two distinct proteins: CREB-binding protein (CBP) and p300/CBP-associated factor (P/CAF). polyglutamine 22-35 huntingtin Drosophila melanogaster 57-60 15677486-1 2005 Huntington"s disease (HD) is a late onset heritable neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) sequence in the protein huntingtin (Htt). polyglutamine 104-117 huntingtin Drosophila melanogaster 150-160 15677486-1 2005 Huntington"s disease (HD) is a late onset heritable neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) sequence in the protein huntingtin (Htt). polyglutamine 104-117 huntingtin Drosophila melanogaster 162-165 15677486-1 2005 Huntington"s disease (HD) is a late onset heritable neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) sequence in the protein huntingtin (Htt). polyglutamine 119-124 huntingtin Drosophila melanogaster 150-160 15677486-1 2005 Huntington"s disease (HD) is a late onset heritable neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) sequence in the protein huntingtin (Htt). polyglutamine 119-124 huntingtin Drosophila melanogaster 162-165 15677486-4 2005 We targeted the expression of the polyQ-containing domain of Htt or an extended polyQ peptide alone in a subset of Drosophila glial cells, where the only fly glutamate transporter, dEAAT1, is detected. polyglutamine 34-39 huntingtin Drosophila melanogaster 61-64 12379151-1 2002 BACKGROUND: Huntington"s disease (HD) pathogenesis is due to an expanded polyglutamine tract in huntingtin, but the specificity of neuronal loss compared with other polyglutamine disorders also implies a role for the protein"s unknown inherent function. polyglutamine 73-86 huntingtin Drosophila melanogaster 96-106 15590702-1 2005 Huntington"s disease (HD) is caused by expansion of a polyglutamine tract near the N-terminal of huntingtin. polyglutamine 54-67 huntingtin Drosophila melanogaster 97-107 15064418-1 2004 Huntington"s disease (HD) is characterized by the accumulation of a pathogenic protein, Huntingtin (Htt), that contains an abnormal polyglutamine expansion. polyglutamine 132-145 huntingtin Drosophila melanogaster 88-98 14978262-1 2004 Huntington"s disease is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine tract in the huntingtin protein that results in intracellular aggregate formation and neurodegeneration. polyglutamine 98-111 huntingtin Drosophila melanogaster 125-135 10441347-5 1999 Analysis of the genomic and cDNA sequences indicates that Drosophila HD has 29 exons, compared with the 67 exons present in vertebrate HD genes, and that Drosophila huntingtin lacks the polyglutamine and polyproline stretches present in its mammalian counterparts. polyglutamine 186-199 huntingtin Drosophila melanogaster 165-175