PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33869222-4 2021 Huntington"s disease (HD) is an incurable neurodegenerative disorder that is caused by polyglutamine expansion in the huntingtin (HTT) protein, characterized by the loss of gamma-aminobutyric acid (GABA)-ergic medium spiny neurons (MSNs) in the striatum. polyglutamine 87-100 huntingtin Homo sapiens 118-128 33869222-4 2021 Huntington"s disease (HD) is an incurable neurodegenerative disorder that is caused by polyglutamine expansion in the huntingtin (HTT) protein, characterized by the loss of gamma-aminobutyric acid (GABA)-ergic medium spiny neurons (MSNs) in the striatum. polyglutamine 87-100 huntingtin Homo sapiens 130-133 33712450-8 2021 Loss of p97-UBXN1 results in increased Huntingtin polyQ inclusion bodies both in mammalian cells as well as in a C.elegans model of Huntington"s Disease. polyglutamine 50-55 huntingtin Homo sapiens 39-49 33576152-7 2021 In the cytosol, these degradation intermediates stimulated aggregation of polyglutamine-expanded Huntingtin protein (Htt-polyQ-GFP) by interacting with aggregation-prone proteins, including Htt-polyQ-GFP. polyglutamine 74-87 huntingtin Homo sapiens 97-107 33753744-4 2021 We demonstrate use of DisCo to disrupt condensates of FUS, associated with amyotrophic lateral sclerosis, and to prevent formation of polyglutamine-containing huntingtin condensates, associated with Huntington"s disease. polyglutamine 134-147 huntingtin Homo sapiens 159-169 33730050-6 2021 WDR81 facilitates the recruitment of autophagic proteins onto Htt polyQ aggregates and promotes autophagic clearance of Htt polyQ subsequently. polyglutamine 66-71 huntingtin Homo sapiens 62-65 33730050-6 2021 WDR81 facilitates the recruitment of autophagic proteins onto Htt polyQ aggregates and promotes autophagic clearance of Htt polyQ subsequently. polyglutamine 124-129 huntingtin Homo sapiens 120-123 33730050-7 2021 The BEACH and MFS domains of WDR81 are sufficient for its recruitment onto Htt polyQ aggregates, and its WD40 repeats are essential for WDR81 interaction with covalent bound ATG5-ATG12. polyglutamine 79-84 huntingtin Homo sapiens 75-78 33517535-1 2021 Neuropathologic hallmarks of Huntington Disease (HD) include the progressive neurodegeneration of the striatum and the presence of Huntingtin (HTT) aggregates that result from abnormal polyQ expansion of the HTT gene. polyglutamine 185-190 huntingtin Homo sapiens 131-141 33517535-1 2021 Neuropathologic hallmarks of Huntington Disease (HD) include the progressive neurodegeneration of the striatum and the presence of Huntingtin (HTT) aggregates that result from abnormal polyQ expansion of the HTT gene. polyglutamine 185-190 huntingtin Homo sapiens 143-146 33517535-1 2021 Neuropathologic hallmarks of Huntington Disease (HD) include the progressive neurodegeneration of the striatum and the presence of Huntingtin (HTT) aggregates that result from abnormal polyQ expansion of the HTT gene. polyglutamine 185-190 huntingtin Homo sapiens 208-211 33644966-1 2021 Huntington"s disease arises from polyQ expansion within the exon-1 region of huntingtin (htt ex1 ), resulting in an aggregation prone protein that accumulates in neuronal inclusion bodies. polyglutamine 33-38 huntingtin Homo sapiens 77-87 33659724-1 2021 Huntington"s disease is a neurodegenerative disease caused by CAG repeat in the first exon of HTT (Huntingtin) gene, leading to abnormal form of Htt protein containing enlarged polyglutamine strands of variable length that stick together to form aggregates and is toxic to brain causing brain damage. polyglutamine 177-190 huntingtin Homo sapiens 94-97 33659724-1 2021 Huntington"s disease is a neurodegenerative disease caused by CAG repeat in the first exon of HTT (Huntingtin) gene, leading to abnormal form of Htt protein containing enlarged polyglutamine strands of variable length that stick together to form aggregates and is toxic to brain causing brain damage. polyglutamine 177-190 huntingtin Homo sapiens 99-109 33659724-1 2021 Huntington"s disease is a neurodegenerative disease caused by CAG repeat in the first exon of HTT (Huntingtin) gene, leading to abnormal form of Htt protein containing enlarged polyglutamine strands of variable length that stick together to form aggregates and is toxic to brain causing brain damage. polyglutamine 177-190 huntingtin Homo sapiens 145-148 33335120-4 2020 Here we evaluate mutant polyglutamine-expanded (mHTT) and polyglutamine-independent HTT specific immunoassays for validation in human HD and control fibroblasts and use to elucidate the CSF/brain and peripheral tissue expression of HTT in preclinical HD models. polyglutamine 58-71 huntingtin Homo sapiens 84-87 33130095-2 2021 As a consequence of polyQ expansion, htt associates into a variety of aggregate species that are thought to underlie cellular toxicity. polyglutamine 20-25 huntingtin Homo sapiens 37-40 33425919-2 2020 It is caused by a polyglutamine expansion in the huntingtin protein that leads to striatal degeneration via the transcriptional dysregulation of several genes, including genes that are involved in the calcium (Ca2+) signalosome. polyglutamine 18-31 huntingtin Homo sapiens 49-59 33285261-2 2021 Here we show that SIRT3 is neuroprotective in Huntington"s disease (HD), a motor neurodegenerative disorder caused by an abnormal expansion of polyglutamines in the huntingtin protein (HTT). polyglutamine 143-157 huntingtin Homo sapiens 165-175 33285261-2 2021 Here we show that SIRT3 is neuroprotective in Huntington"s disease (HD), a motor neurodegenerative disorder caused by an abnormal expansion of polyglutamines in the huntingtin protein (HTT). polyglutamine 143-157 huntingtin Homo sapiens 185-188 33454006-10 2020 We demonstrate the versatility of AggreCount by analyzing a number of different cellular aggregates including aggresomes, stress granules, and inclusion bodies caused by huntingtin polyglutamine expansion. polyglutamine 181-194 huntingtin Homo sapiens 170-180 33256402-1 2020 Huntington"s disease (HD) is a neurodegenerative disorder caused by the abnormal expansion of a polyglutamine (polyQ) tract in the first exon of the htt protein (htt). polyglutamine 96-109 huntingtin Homo sapiens 149-152 33256402-1 2020 Huntington"s disease (HD) is a neurodegenerative disorder caused by the abnormal expansion of a polyglutamine (polyQ) tract in the first exon of the htt protein (htt). polyglutamine 96-109 huntingtin Homo sapiens 162-165 33256402-1 2020 Huntington"s disease (HD) is a neurodegenerative disorder caused by the abnormal expansion of a polyglutamine (polyQ) tract in the first exon of the htt protein (htt). polyglutamine 111-116 huntingtin Homo sapiens 149-152 33256402-1 2020 Huntington"s disease (HD) is a neurodegenerative disorder caused by the abnormal expansion of a polyglutamine (polyQ) tract in the first exon of the htt protein (htt). polyglutamine 111-116 huntingtin Homo sapiens 162-165 33256402-2 2020 PolyQ expansion triggers the aggregation of htt into a variety of structures, including oligomers and fibrils. polyglutamine 0-5 huntingtin Homo sapiens 44-47 33256402-3 2020 This aggregation is impacted by the first 17 N-terminal amino acids (Nt17) of htt that directly precedes the polyQ domain. polyglutamine 109-114 huntingtin Homo sapiens 78-81 33098802-1 2020 BACKGROUND: Huntington"s disease is a fatal neurodegenerative disorder that is caused by CAG-CAA repeat expansion, encoding polyglutamine, in the huntingtin (HTT) gene. polyglutamine 124-137 huntingtin Homo sapiens 146-156 33228685-1 2020 BACKGROUND: Huntington"s disease (HD) is an inherited disorder caused by the polyglutamine (poly-Q) mutations of the HTT gene results in neurodegeneration characterized by chorea, loss of coordination, cognitive decline. polyglutamine 77-90 huntingtin Homo sapiens 117-120 33228685-1 2020 BACKGROUND: Huntington"s disease (HD) is an inherited disorder caused by the polyglutamine (poly-Q) mutations of the HTT gene results in neurodegeneration characterized by chorea, loss of coordination, cognitive decline. polyglutamine 92-98 huntingtin Homo sapiens 117-120 33096080-2 2020 This expansion results in an elongated polyglutamine (polyQ) domain that increases the propensity of huntingtin exon-1 (HTTex1) to form cross-beta fibrils. polyglutamine 39-52 huntingtin Homo sapiens 101-111 33096080-2 2020 This expansion results in an elongated polyglutamine (polyQ) domain that increases the propensity of huntingtin exon-1 (HTTex1) to form cross-beta fibrils. polyglutamine 54-59 huntingtin Homo sapiens 101-111 33094816-2 2020 Our previous research has demonstrated that USP19 up-regulates the protein level and aggregation of polyQ-expanded huntingtin through the involvement of heat shock protein 90 (HSP90). polyglutamine 100-105 huntingtin Homo sapiens 115-125 33094816-6 2020 A mechanism of auto-inhibition of USP19 and activation by HSP90 is proposed, on which USP19 modulates the protein level of polyQ-expanded huntingtin in cells. polyglutamine 136-141 huntingtin Homo sapiens 151-161 33167595-2 2020 These expansions lead to a prolongation of the poly-glutamine stretch at the N-terminus of Huntingtin causing protein misfolding and aggregation. polyglutamine 47-61 huntingtin Homo sapiens 91-101 33098802-1 2020 BACKGROUND: Huntington"s disease is a fatal neurodegenerative disorder that is caused by CAG-CAA repeat expansion, encoding polyglutamine, in the huntingtin (HTT) gene. polyglutamine 124-137 huntingtin Homo sapiens 158-161 32975927-8 2020 Insights into the aggregation properties of htt-ex1 derivatives-as well as into the nucleation process itself-were obtained using fluorescence correlation spectroscopy (FCS) and a novel thioflavin-T (ThT) protocol that allows quantitation of htt-ex1 assembly intermediates.Using these tools, we quantified physical states of htt-ex1 at different growth times in mammalian PC12 cells engineered for inducible expression of both normal and expanded polyQ repeat length versions of htt-ex1. polyglutamine 447-452 huntingtin Homo sapiens 44-47 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 125-138 huntingtin Homo sapiens 77-87 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 125-138 huntingtin Homo sapiens 94-97 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 125-138 huntingtin Homo sapiens 162-180 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 125-138 huntingtin Homo sapiens 182-185 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 140-145 huntingtin Homo sapiens 77-87 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 140-145 huntingtin Homo sapiens 94-97 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 140-145 huntingtin Homo sapiens 162-180 33122998-3 2020 HD-causing mutation consists in an expansion of repeated CAG triplets in the huntingtin gene (HTT), encoding for an expanded polyglutamine (polyQ) stretch in the huntingtin protein (htt). polyglutamine 140-145 huntingtin Homo sapiens 182-185 32880177-3 2020 The pan-neuronal expression of a pathogenic fragment of the human Huntingtin (HTT) protein containing a 93-repeat polyglutamine expansion (Httex1p Q93) in transgenic flies induces a neuropathology with several characteristics of the human disease. polyglutamine 114-127 huntingtin Homo sapiens 66-76 32880177-3 2020 The pan-neuronal expression of a pathogenic fragment of the human Huntingtin (HTT) protein containing a 93-repeat polyglutamine expansion (Httex1p Q93) in transgenic flies induces a neuropathology with several characteristics of the human disease. polyglutamine 114-127 huntingtin Homo sapiens 78-81 32668197-6 2020 These results provide a molecular basis for the effect of the polyQ segment on HTT structure and activity, which may be important for HTT pathology. polyglutamine 62-67 huntingtin Homo sapiens 134-137 31796991-1 2020 Huntington"s disease (HD) is a severe neurodegenerative disorder caused by poly Q repeat expansion in the Huntingtin (Htt) gene. polyglutamine 75-81 huntingtin Homo sapiens 106-116 31796991-1 2020 Huntington"s disease (HD) is a severe neurodegenerative disorder caused by poly Q repeat expansion in the Huntingtin (Htt) gene. polyglutamine 75-81 huntingtin Homo sapiens 118-121 31796991-5 2020 Co-expression of Orb2 can partially rescue the lethality associated with poly Q expanded Htt. polyglutamine 73-79 huntingtin Homo sapiens 89-92 32668197-0 2020 The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. polyglutamine 4-17 huntingtin Homo sapiens 49-59 32668197-1 2020 The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington"s disease (HD). polyglutamine 4-9 huntingtin Homo sapiens 23-33 32668197-1 2020 The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington"s disease (HD). polyglutamine 4-9 huntingtin Homo sapiens 43-46 32668197-3 2020 Here, we present analyses of the impact of polyQ length on the structure and function of HTT via an integrative structural and biochemical approach. polyglutamine 43-48 huntingtin Homo sapiens 89-92 32668197-4 2020 The cryo-EM analysis of normal (Q23) and disease (Q78) type HTTs shows that the structures of apo HTTs significantly differ from the structure of HTT in a HAP40 complex and that the polyQ expansion induces global structural changes in the relative movements among the HTT domains. polyglutamine 182-187 huntingtin Homo sapiens 60-63 32668197-5 2020 In addition, we show that the polyQ expansion alters the phosphorylation pattern across HTT and that Ser2116 phosphorylation in turn affects the global structure and function of HTT. polyglutamine 30-35 huntingtin Homo sapiens 88-91 32668197-5 2020 In addition, we show that the polyQ expansion alters the phosphorylation pattern across HTT and that Ser2116 phosphorylation in turn affects the global structure and function of HTT. polyglutamine 30-35 huntingtin Homo sapiens 178-181 32668197-6 2020 These results provide a molecular basis for the effect of the polyQ segment on HTT structure and activity, which may be important for HTT pathology. polyglutamine 62-67 huntingtin Homo sapiens 79-82 32662649-1 2020 Mutant huntingtin (mHTT) protein carrying the elongated N-terminal polyglutamine (polyQ) tract misfolds and forms protein aggregates characteristic of HD pathology. polyglutamine 82-87 huntingtin Homo sapiens 7-17 32747555-1 2020 Huntington disease (HD) is an ideal model for investigating selective neurodegeneration, as expanded polyQ repeats in the ubiquitously expressed huntingtin (HTT) cause the preferential neurodegeneration in the striatum of the HD patient brains. polyglutamine 101-106 huntingtin Homo sapiens 145-155 32747555-1 2020 Huntington disease (HD) is an ideal model for investigating selective neurodegeneration, as expanded polyQ repeats in the ubiquitously expressed huntingtin (HTT) cause the preferential neurodegeneration in the striatum of the HD patient brains. polyglutamine 101-106 huntingtin Homo sapiens 157-160 32857759-2 2020 Superficially these inclusions are similar to those formed by polyglutamine (polyQ)-expanded Huntingtin exon 1 (Httex1) in Huntington"s disease. polyglutamine 62-75 huntingtin Homo sapiens 93-103 32857759-2 2020 Superficially these inclusions are similar to those formed by polyglutamine (polyQ)-expanded Huntingtin exon 1 (Httex1) in Huntington"s disease. polyglutamine 77-82 huntingtin Homo sapiens 93-103 32581130-1 2020 Huntington disease (HD) is caused by an expansion mutation of the N-terminal polyglutamine of huntingtin (mHTT). polyglutamine 77-90 huntingtin Homo sapiens 94-104 32735619-1 2020 Mutations that cause Huntington"s Disease involve a polyglutamine (polyQ) sequence expansion beyond 35 repeats in exon 1 of Huntingtin. polyglutamine 52-65 huntingtin Homo sapiens 124-134 32735619-1 2020 Mutations that cause Huntington"s Disease involve a polyglutamine (polyQ) sequence expansion beyond 35 repeats in exon 1 of Huntingtin. polyglutamine 67-72 huntingtin Homo sapiens 124-134 32598938-1 2020 Huntington"s disease is a progressive neurodegenerative disease caused by expansion of the polyglutamine domain in the first exon of huntingtin (HttEx1). polyglutamine 91-104 huntingtin Homo sapiens 133-143 32402249-0 2020 Flanking Regions Determine the Structure of the Poly-Glutamine in Huntingtin through Mechanisms Common among Glutamine-Rich Human Proteins. polyglutamine 48-62 huntingtin Homo sapiens 66-76 32402249-1 2020 The causative agent of Huntington"s disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. polyglutamine 49-55 huntingtin Homo sapiens 96-106 32640252-2 2020 (2020a) combine site-specific isotope labeling and NMR spectroscopy to investigate opposing effects of flanking regions onto the conformation of the poly-Q region in Huntingtin. polyglutamine 149-155 huntingtin Homo sapiens 166-176 32611447-1 2020 Huntington"s disease (HD) is characterized by protein inclusions and loss of striatal neurons which result from expanded CAG repeats in the poly-glutamine (polyQ) region of the huntingtin (HTT) gene. polyglutamine 140-154 huntingtin Homo sapiens 177-187 32611447-1 2020 Huntington"s disease (HD) is characterized by protein inclusions and loss of striatal neurons which result from expanded CAG repeats in the poly-glutamine (polyQ) region of the huntingtin (HTT) gene. polyglutamine 140-154 huntingtin Homo sapiens 189-192 32611447-1 2020 Huntington"s disease (HD) is characterized by protein inclusions and loss of striatal neurons which result from expanded CAG repeats in the poly-glutamine (polyQ) region of the huntingtin (HTT) gene. polyglutamine 156-161 huntingtin Homo sapiens 177-187 32611447-1 2020 Huntington"s disease (HD) is characterized by protein inclusions and loss of striatal neurons which result from expanded CAG repeats in the poly-glutamine (polyQ) region of the huntingtin (HTT) gene. polyglutamine 156-161 huntingtin Homo sapiens 189-192 32560122-3 2020 The mutant huntingtin protein (HTT) exhibits an expansion of a polyglutamine repeat. polyglutamine 63-76 huntingtin Homo sapiens 11-21 32320524-0 2020 Stabilization of elongated polyglutamine tracts by a helical peptide derived from N-terminal huntingtin. polyglutamine 27-40 huntingtin Homo sapiens 93-103 32560122-3 2020 The mutant huntingtin protein (HTT) exhibits an expansion of a polyglutamine repeat. polyglutamine 63-76 huntingtin Homo sapiens 31-34 32560122-6 2020 The discovery and characterization of a panoply of PTMs in HTT aggregation and cellular events in HD will bring us closer to understanding how the expression of mutant polyglutamine-containing HTT affects cellular homeostasis that leads to the perturbation of cell functions, neurotoxicity, and finally, cell death. polyglutamine 168-181 huntingtin Homo sapiens 59-62 32329133-5 2020 We found that expression of exon 1 HTT fragments with longer polyQ tracts led to the formation of intra-nuclear inclusions in a polyQ length-dependent manner during neurogenesis. polyglutamine 61-66 huntingtin Homo sapiens 35-38 32596207-2 2020 The protein aggregates observed in Huntington"s Disease are caused by a polyglutamine expansion in the N-terminus of the huntingtin protein (Htt). polyglutamine 72-85 huntingtin Homo sapiens 121-131 32596207-2 2020 The protein aggregates observed in Huntington"s Disease are caused by a polyglutamine expansion in the N-terminus of the huntingtin protein (Htt). polyglutamine 72-85 huntingtin Homo sapiens 141-144 32329133-5 2020 We found that expression of exon 1 HTT fragments with longer polyQ tracts led to the formation of intra-nuclear inclusions in a polyQ length-dependent manner during neurogenesis. polyglutamine 128-133 huntingtin Homo sapiens 35-38 32127471-1 2020 Human profilin I reduces aggregation and concomitant toxicity of the polyglutamine-containing N-terminal region of the huntingtin protein encoded by exon 1 (httex1) and responsible for Huntington"s disease. polyglutamine 69-82 huntingtin Homo sapiens 119-129 32391325-0 2020 Length-Dependent Structural Transformations of Huntingtin PolyQ Domain Upon Binding to 2D-Nanomaterials. polyglutamine 58-63 huntingtin Homo sapiens 47-57 32235053-2 2021 A glutamine stretch (PolyQ) at the N-terminal of the Huntingtin protein is generated by the abnormal expansion of CAG trinucleotide repeats in exon 1 of the HTT gene. polyglutamine 21-26 huntingtin Homo sapiens 53-63 32235053-2 2021 A glutamine stretch (PolyQ) at the N-terminal of the Huntingtin protein is generated by the abnormal expansion of CAG trinucleotide repeats in exon 1 of the HTT gene. polyglutamine 21-26 huntingtin Homo sapiens 157-160 32341997-5 2020 First, through the enrichment of deuterated glutamine in the polyQ sequence of mutant Huntingtin (mHtt) exon1 proteins for Huntington"s disease, we achieved sensitive and specific stimulated Raman scattering (SRS) imaging of carbon-deuterium bonds (C-D) from aggregates without GFP labeling, which is commonly employed in fluorescence microscopy. polyglutamine 61-66 huntingtin Homo sapiens 86-96 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 huntingtin Homo sapiens 97-107 31943010-1 2020 Huntington"s Disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the Huntingtin protein (HTT) and is necessary to cause pathology and formation of HTT aggregates. polyglutamine 57-71 huntingtin Homo sapiens 95-105 31943010-1 2020 Huntington"s Disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the Huntingtin protein (HTT) and is necessary to cause pathology and formation of HTT aggregates. polyglutamine 57-71 huntingtin Homo sapiens 115-118 31943010-1 2020 Huntington"s Disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the Huntingtin protein (HTT) and is necessary to cause pathology and formation of HTT aggregates. polyglutamine 57-71 huntingtin Homo sapiens 173-176 31943010-1 2020 Huntington"s Disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the Huntingtin protein (HTT) and is necessary to cause pathology and formation of HTT aggregates. polyglutamine 73-78 huntingtin Homo sapiens 95-105 31943010-1 2020 Huntington"s Disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the Huntingtin protein (HTT) and is necessary to cause pathology and formation of HTT aggregates. polyglutamine 73-78 huntingtin Homo sapiens 115-118 31943010-1 2020 Huntington"s Disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the Huntingtin protein (HTT) and is necessary to cause pathology and formation of HTT aggregates. polyglutamine 73-78 huntingtin Homo sapiens 173-176 31943010-5 2020 Expanded polyQ alone is not sufficient to cause inclusion formation since full-length HTT and HTTex1 with expanded polyQ are both toxic although full-length HTT remains diffuse while HTTex1 forms inclusions. polyglutamine 115-120 huntingtin Homo sapiens 94-97 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 huntingtin Homo sapiens 97-107 31880908-1 2020 Huntington"s disease (HD), a genetic neurodegenerative disease, is caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin protein (htt). polyglutamine 89-102 huntingtin Homo sapiens 143-153 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 119-132 huntingtin Homo sapiens 76-86 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 119-132 huntingtin Homo sapiens 88-91 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 119-132 huntingtin Homo sapiens 158-168 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 119-132 huntingtin Homo sapiens 170-173 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 76-86 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 88-91 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 158-168 31715317-2 2020 The onset of HD has been linked to a pathogenic CAG repeat expansion in the huntingtin (HTT) gene that encodes for the polyglutamine (polyQ) stretches in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 170-173 31834602-1 2020 Huntington"s disease (HD) is a neurodegenerative late-onset genetic disorder caused by CAG expansions in the coding region of the Huntingtin (HTT) gene, resulting in a poly-glutamine (polyQ) expanded HTT protein. polyglutamine 168-182 huntingtin Homo sapiens 130-140 31834602-1 2020 Huntington"s disease (HD) is a neurodegenerative late-onset genetic disorder caused by CAG expansions in the coding region of the Huntingtin (HTT) gene, resulting in a poly-glutamine (polyQ) expanded HTT protein. polyglutamine 168-182 huntingtin Homo sapiens 142-145 31834602-1 2020 Huntington"s disease (HD) is a neurodegenerative late-onset genetic disorder caused by CAG expansions in the coding region of the Huntingtin (HTT) gene, resulting in a poly-glutamine (polyQ) expanded HTT protein. polyglutamine 168-182 huntingtin Homo sapiens 200-203 31834602-1 2020 Huntington"s disease (HD) is a neurodegenerative late-onset genetic disorder caused by CAG expansions in the coding region of the Huntingtin (HTT) gene, resulting in a poly-glutamine (polyQ) expanded HTT protein. polyglutamine 184-189 huntingtin Homo sapiens 130-140 31834602-1 2020 Huntington"s disease (HD) is a neurodegenerative late-onset genetic disorder caused by CAG expansions in the coding region of the Huntingtin (HTT) gene, resulting in a poly-glutamine (polyQ) expanded HTT protein. polyglutamine 184-189 huntingtin Homo sapiens 142-145 31834602-1 2020 Huntington"s disease (HD) is a neurodegenerative late-onset genetic disorder caused by CAG expansions in the coding region of the Huntingtin (HTT) gene, resulting in a poly-glutamine (polyQ) expanded HTT protein. polyglutamine 184-189 huntingtin Homo sapiens 200-203 32036391-1 2020 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by an increased and unstable CAG DNA expansion in the Huntingtin (HTT) gene, resulting in an elongated polyglutamine tract in huntingtin protein. polyglutamine 188-201 huntingtin Homo sapiens 139-149 32036391-1 2020 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by an increased and unstable CAG DNA expansion in the Huntingtin (HTT) gene, resulting in an elongated polyglutamine tract in huntingtin protein. polyglutamine 188-201 huntingtin Homo sapiens 151-154 32036391-1 2020 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by an increased and unstable CAG DNA expansion in the Huntingtin (HTT) gene, resulting in an elongated polyglutamine tract in huntingtin protein. polyglutamine 188-201 huntingtin Homo sapiens 211-221 32036391-7 2020 HMGB1 can inhibit mutant huntingtin aggregation, protecting against polyglutamine-induced neurotoxicity and acting as a chaperon-like molecule, possibly via autophagy regulation. polyglutamine 68-81 huntingtin Homo sapiens 25-35 31880908-1 2020 Huntington"s disease (HD), a genetic neurodegenerative disease, is caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin protein (htt). polyglutamine 89-102 huntingtin Homo sapiens 163-166 31880908-1 2020 Huntington"s disease (HD), a genetic neurodegenerative disease, is caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin protein (htt). polyglutamine 104-109 huntingtin Homo sapiens 143-153 31880908-1 2020 Huntington"s disease (HD), a genetic neurodegenerative disease, is caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin protein (htt). polyglutamine 104-109 huntingtin Homo sapiens 163-166 31745395-11 2019 The Ramachandran plot for HTT protein derived through online Rampage revealed the recurrent appearance of polyglutamine (Q) at the Phi (-55--65) and Psi (120-135) regions. polyglutamine 106-119 huntingtin Homo sapiens 26-29 31767406-2 2020 We previously developed a class of degradation-inducing agents targeting the beta-sheet-rich structure typical of such aggregates, and we showed that these agents dose-, time-, and proteasome-dependently decrease the intracellular level of mutant huntingtin with an extended polyglutamine tract, which correlates well with the severity of Huntington"s disease. polyglutamine 275-288 huntingtin Homo sapiens 247-257 31223078-4 2020 The mutation leads to the abnormal expansion of the production of the polyglutamine tract (polyQ) resulting in the form of an unstable Huntingtin protein commonly referred to as mutant Huntingtin. polyglutamine 91-96 huntingtin Homo sapiens 135-145 31223078-4 2020 The mutation leads to the abnormal expansion of the production of the polyglutamine tract (polyQ) resulting in the form of an unstable Huntingtin protein commonly referred to as mutant Huntingtin. polyglutamine 91-96 huntingtin Homo sapiens 185-195 31828084-1 2019 Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder, caused by a CAG/polyglutamine (polyQ) repeat expansion in the Huntingtin (HTT) gene. polyglutamine 107-120 huntingtin Homo sapiens 153-163 31828084-1 2019 Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder, caused by a CAG/polyglutamine (polyQ) repeat expansion in the Huntingtin (HTT) gene. polyglutamine 107-120 huntingtin Homo sapiens 165-168 31828084-1 2019 Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder, caused by a CAG/polyglutamine (polyQ) repeat expansion in the Huntingtin (HTT) gene. polyglutamine 122-127 huntingtin Homo sapiens 153-163 31828084-1 2019 Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder, caused by a CAG/polyglutamine (polyQ) repeat expansion in the Huntingtin (HTT) gene. polyglutamine 122-127 huntingtin Homo sapiens 165-168 31828084-2 2019 The polyQ tract is located in and transcribed from N-terminal HTT of exon 1. polyglutamine 4-9 huntingtin Homo sapiens 62-65 31428776-0 2019 Post-transcriptional negative feedback regulation of proteostasis through the Dis3 ribonuclease and its disruption by polyQ-expanded Huntingtin. polyglutamine 118-123 huntingtin Homo sapiens 133-143 31428776-6 2019 We further demonstrate that polyQ-expanded huntingtin delays Dis3 degradation during heat stress and thus hinders chaperone mRNA stabilization. polyglutamine 28-33 huntingtin Homo sapiens 43-53 31757420-2 2020 Here, we used the N&B method to characterize the unexpanded HTT protein oligomerization after the internalization of the mutant HTT (mHTT) which contains a CAG repeat extensions encoding for long polyglutamine (polyQ) proteins resulting in misfolding and aggregation. polyglutamine 200-213 huntingtin Homo sapiens 64-67 31757420-2 2020 Here, we used the N&B method to characterize the unexpanded HTT protein oligomerization after the internalization of the mutant HTT (mHTT) which contains a CAG repeat extensions encoding for long polyglutamine (polyQ) proteins resulting in misfolding and aggregation. polyglutamine 200-213 huntingtin Homo sapiens 132-135 31757420-2 2020 Here, we used the N&B method to characterize the unexpanded HTT protein oligomerization after the internalization of the mutant HTT (mHTT) which contains a CAG repeat extensions encoding for long polyglutamine (polyQ) proteins resulting in misfolding and aggregation. polyglutamine 215-220 huntingtin Homo sapiens 64-67 31757420-2 2020 Here, we used the N&B method to characterize the unexpanded HTT protein oligomerization after the internalization of the mutant HTT (mHTT) which contains a CAG repeat extensions encoding for long polyglutamine (polyQ) proteins resulting in misfolding and aggregation. polyglutamine 215-220 huntingtin Homo sapiens 132-135 31968243-1 2020 Huntington"s disease (HD) is caused by an autosomal dominant polyglutamine expansion mutation of Huntingtin (HTT). polyglutamine 61-74 huntingtin Homo sapiens 97-107 31968243-1 2020 Huntington"s disease (HD) is caused by an autosomal dominant polyglutamine expansion mutation of Huntingtin (HTT). polyglutamine 61-74 huntingtin Homo sapiens 109-112 30523767-3 2020 This HD variation is because of the development of a polyglutamine (CAG) repeats in the exon 1 of the Huntingtin protein. polyglutamine 53-66 huntingtin Homo sapiens 102-112 31638189-2 2019 It is caused by abnormal expansion of a CAG triplet in the gene encoding the huntingtin protein (Htt), with consequent expansion of a polyglutamine repeat in mutated Htt (mHtt). polyglutamine 134-147 huntingtin Homo sapiens 77-87 31638189-2 2019 It is caused by abnormal expansion of a CAG triplet in the gene encoding the huntingtin protein (Htt), with consequent expansion of a polyglutamine repeat in mutated Htt (mHtt). polyglutamine 134-147 huntingtin Homo sapiens 97-100 31638189-2 2019 It is caused by abnormal expansion of a CAG triplet in the gene encoding the huntingtin protein (Htt), with consequent expansion of a polyglutamine repeat in mutated Htt (mHtt). polyglutamine 134-147 huntingtin Homo sapiens 166-169 31304621-3 2019 Although the polyglutamine expansion within HTT is the causative factor in the pathogenesis of HD, the underlying mechanisms that provoke this expansion and the resulting neurodegeneration and clinical symptoms are not fully understood. polyglutamine 13-26 huntingtin Homo sapiens 44-47 31608620-4 2019 Specifically, HD is caused by the aggregation of the huntingtin (htt) protein that contains an expanded polyglutamine domain. polyglutamine 104-117 huntingtin Homo sapiens 53-63 31568752-4 2019 The Polyglutamine Binding Peptide 1 (QBP1), whose minimal active core is the octapeptide WGWWPGIF, strongly inhibits the aggregation of polyQ-containing amyloidogenic proteins such as Huntingtin. polyglutamine 4-17 huntingtin Homo sapiens 184-194 31568752-4 2019 The Polyglutamine Binding Peptide 1 (QBP1), whose minimal active core is the octapeptide WGWWPGIF, strongly inhibits the aggregation of polyQ-containing amyloidogenic proteins such as Huntingtin. polyglutamine 136-141 huntingtin Homo sapiens 184-194 31608620-4 2019 Specifically, HD is caused by the aggregation of the huntingtin (htt) protein that contains an expanded polyglutamine domain. polyglutamine 104-117 huntingtin Homo sapiens 65-68 31184975-1 2019 Huntington"s disease is a neurodegenerative disorder caused by a CAG repeat expansion in the first exon of huntingtin gene (HTT) encoding for a toxic polyglutamine protein. polyglutamine 150-163 huntingtin Homo sapiens 107-117 31717806-1 2019 Huntington"s disease (HD) is an inherited neurodegenerative disorder, caused by an abnormal polyglutamine (polyQ) expansion in the huntingtin protein (Htt). polyglutamine 92-105 huntingtin Homo sapiens 131-141 31717806-1 2019 Huntington"s disease (HD) is an inherited neurodegenerative disorder, caused by an abnormal polyglutamine (polyQ) expansion in the huntingtin protein (Htt). polyglutamine 92-105 huntingtin Homo sapiens 151-154 31717806-1 2019 Huntington"s disease (HD) is an inherited neurodegenerative disorder, caused by an abnormal polyglutamine (polyQ) expansion in the huntingtin protein (Htt). polyglutamine 107-112 huntingtin Homo sapiens 131-141 31717806-1 2019 Huntington"s disease (HD) is an inherited neurodegenerative disorder, caused by an abnormal polyglutamine (polyQ) expansion in the huntingtin protein (Htt). polyglutamine 107-112 huntingtin Homo sapiens 151-154 31717806-11 2019 Our data suggest that juvenile HD fibroblasts respond to mutant polyQ expansion of Htt with enhanced proteasome activity and faster turnover of specific UPS substrates to protect cells. polyglutamine 64-69 huntingtin Homo sapiens 83-86 31632982-1 2019 Huntington disease is a neurodegenerative disease characterized by a polymorphic tract of polyglutamine repeats in exon 1 of the huntingtin protein, which is thought to be responsible for protein aggregation and neuronal death. polyglutamine 90-103 huntingtin Homo sapiens 129-139 31184975-1 2019 Huntington"s disease is a neurodegenerative disorder caused by a CAG repeat expansion in the first exon of huntingtin gene (HTT) encoding for a toxic polyglutamine protein. polyglutamine 150-163 huntingtin Homo sapiens 124-127 31326748-1 2019 Huntington disease (HD) is an autosomal dominant, neurodegenerative disease caused by a CAG repeat expansion within the coding sequence of the HTT gene, resulting in a highly toxic protein with an expanded polyglutamine stretch that forms typical protein aggregates throughout the brain. polyglutamine 206-219 huntingtin Homo sapiens 143-146 31398342-1 2019 Variable, glutamine-encoding, CAA interruptions indicate that a property of the uninterrupted HTT CAG repeat sequence, distinct from the length of huntingtin"s polyglutamine segment, dictates the rate at which Huntington"s disease (HD) develops. polyglutamine 160-173 huntingtin Homo sapiens 147-157 31460743-1 2019 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in the huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminal part of huntingtin (Httex1). polyglutamine 117-130 huntingtin Homo sapiens 90-100 31460743-1 2019 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in the huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminal part of huntingtin (Httex1). polyglutamine 117-130 huntingtin Homo sapiens 175-185 31460743-1 2019 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in the huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminal part of huntingtin (Httex1). polyglutamine 132-137 huntingtin Homo sapiens 90-100 31460743-1 2019 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in the huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminal part of huntingtin (Httex1). polyglutamine 132-137 huntingtin Homo sapiens 175-185 31108174-1 2019 Huntington"s disease (HD) is a neurodegenerative disease caused by a CAG repeat expansion in the Huntingtin gene (HTT), translated into a Huntingtin protein with a polyglutamine expansion. polyglutamine 164-177 huntingtin Homo sapiens 97-107 31108174-1 2019 Huntington"s disease (HD) is a neurodegenerative disease caused by a CAG repeat expansion in the Huntingtin gene (HTT), translated into a Huntingtin protein with a polyglutamine expansion. polyglutamine 164-177 huntingtin Homo sapiens 114-117 31108174-1 2019 Huntington"s disease (HD) is a neurodegenerative disease caused by a CAG repeat expansion in the Huntingtin gene (HTT), translated into a Huntingtin protein with a polyglutamine expansion. polyglutamine 164-177 huntingtin Homo sapiens 138-148 31166067-1 2019 Huntington"s disease (HD) is classified as a protein-misfolding disease correlated with the mutant Huntingtin (mHtt) protein with abnormally expanded polyglutamine (polyQ) domains. polyglutamine 150-163 huntingtin Homo sapiens 99-109 31166067-1 2019 Huntington"s disease (HD) is classified as a protein-misfolding disease correlated with the mutant Huntingtin (mHtt) protein with abnormally expanded polyglutamine (polyQ) domains. polyglutamine 165-170 huntingtin Homo sapiens 99-109 31076452-2 2019 Here, we report, Rhes, a brain-enriched GTPase/SUMO E3-like protein, induces the biogenesis of TNT-like cellular protrusions, "Rhes tunnels," through which Rhes moves from cell to cell and transports Huntington disease (HD) protein, the poly-Q expanded mutant Huntingtin (mHTT). polyglutamine 237-243 huntingtin Homo sapiens 260-270 30863908-0 2019 Phosphorylated and aggregated TDP-43 with seeding properties are induced upon mutant Huntingtin (mHtt) polyglutamine expression in human cellular models. polyglutamine 103-116 huntingtin Homo sapiens 85-95 30924108-6 2019 Moreover, treatment of Dynasore significantly promotes the clearance of protein aggregates formed by mutant huntingtin protein containing expanded polyglutamine (polyQ), but not damaged mitochondria. polyglutamine 147-160 huntingtin Homo sapiens 108-118 30924108-6 2019 Moreover, treatment of Dynasore significantly promotes the clearance of protein aggregates formed by mutant huntingtin protein containing expanded polyglutamine (polyQ), but not damaged mitochondria. polyglutamine 162-167 huntingtin Homo sapiens 108-118 31249490-2 2019 HD is caused by a CAG repeat expansion within the first exon of the huntingtin (HTT) gene that produces a polyglutamine repeat that leads to protein misfolding, soluble aggregates, and inclusion bodies detected throughout the body. polyglutamine 106-119 huntingtin Homo sapiens 68-78 31249490-2 2019 HD is caused by a CAG repeat expansion within the first exon of the huntingtin (HTT) gene that produces a polyglutamine repeat that leads to protein misfolding, soluble aggregates, and inclusion bodies detected throughout the body. polyglutamine 106-119 huntingtin Homo sapiens 80-83 31250621-7 2019 Moreover, cellular toxicity was diminished with PCIII treatment for polyglutamine (PolyQ)-huntingtin expression and alpha-synuclein expression in conjunction with 6-hydroxydopamine (6-OHDA) treatment. polyglutamine 68-81 huntingtin Homo sapiens 90-100 31250621-7 2019 Moreover, cellular toxicity was diminished with PCIII treatment for polyglutamine (PolyQ)-huntingtin expression and alpha-synuclein expression in conjunction with 6-hydroxydopamine (6-OHDA) treatment. polyglutamine 83-88 huntingtin Homo sapiens 90-100 30672003-1 2019 Huntington disease is a neurodegenerative disorder caused by the expansion of polyglutamine (polyQ) at the N-terminal of the huntingtin exon 1 protein. polyglutamine 78-91 huntingtin Homo sapiens 125-135 30672003-1 2019 Huntington disease is a neurodegenerative disorder caused by the expansion of polyglutamine (polyQ) at the N-terminal of the huntingtin exon 1 protein. polyglutamine 93-98 huntingtin Homo sapiens 125-135 31063986-3 2019 We show that, in the presence of polyglutamine-expanded (polyQ-expanded) huntingtin (HTT), ADAM10 accumulates at the postsynaptic densities (PSDs) and causes excessive cleavage of the synaptic protein N-cadherin (N-CAD). polyglutamine 33-46 huntingtin Homo sapiens 85-88 30488434-0 2019 HNRNP Q suppresses polyglutamine huntingtin aggregation by post-transcriptional regulation of vaccinia-related kinase 2. polyglutamine 19-32 huntingtin Homo sapiens 33-43 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 116-129 huntingtin Homo sapiens 62-72 30711541-1 2019 Huntington"s disease (HD) is caused by an expanded CAG repeat in the huntingtin (HTT) gene, translating into an elongated polyglutamine stretch. polyglutamine 122-135 huntingtin Homo sapiens 69-79 30711541-1 2019 Huntington"s disease (HD) is caused by an expanded CAG repeat in the huntingtin (HTT) gene, translating into an elongated polyglutamine stretch. polyglutamine 122-135 huntingtin Homo sapiens 81-84 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 116-129 huntingtin Homo sapiens 74-77 30941013-1 2019 Huntington"s disease (HD) is a neurodegenerative disease triggered by expansion of polyglutamine repeats in the protein huntingtin. polyglutamine 83-96 huntingtin Homo sapiens 120-130 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 116-129 huntingtin Homo sapiens 85-89 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 116-129 huntingtin Homo sapiens 171-174 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 131-136 huntingtin Homo sapiens 62-72 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 131-136 huntingtin Homo sapiens 74-77 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 131-136 huntingtin Homo sapiens 85-89 30897183-2 2019 HD is caused by the expansion of CAG repeats in exon 1 of the huntingtin (HTT) gene, IT15, resulting in an expanded polyglutamine (polyQ) residue in the N-terminus of the HTT protein. polyglutamine 131-136 huntingtin Homo sapiens 171-174 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 huntingtin Homo sapiens 308-318 30837611-1 2019 Huntington"s disease is an autosomal dominant neurodegenerative disorder associated with progressive motor and cognitive impairments, and the expansion of a cysteine-adenine-guanine trinucleotide (polyglutamine) repeats in exon one of the human huntingtin gene. polyglutamine 197-210 huntingtin Homo sapiens 245-255 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 huntingtin Homo sapiens 320-323 30149694-1 2019 Huntington"s disease is a neurodegenerative disorder resulting from an expanded polyglutamine (polyQ) repeat of the Huntingtin (Htt) protein. polyglutamine 80-93 huntingtin Homo sapiens 116-126 30538129-1 2019 Huntington"s disease (HD) is a neurodegenerative, age-onset disorder caused by a CAG DNA expansion in exon 1 of the HTT gene, resulting in a polyglutamine expansion in the huntingtin protein. polyglutamine 141-154 huntingtin Homo sapiens 116-119 30538129-1 2019 Huntington"s disease (HD) is a neurodegenerative, age-onset disorder caused by a CAG DNA expansion in exon 1 of the HTT gene, resulting in a polyglutamine expansion in the huntingtin protein. polyglutamine 141-154 huntingtin Homo sapiens 172-182 30149694-1 2019 Huntington"s disease is a neurodegenerative disorder resulting from an expanded polyglutamine (polyQ) repeat of the Huntingtin (Htt) protein. polyglutamine 80-93 huntingtin Homo sapiens 128-131 30149694-1 2019 Huntington"s disease is a neurodegenerative disorder resulting from an expanded polyglutamine (polyQ) repeat of the Huntingtin (Htt) protein. polyglutamine 95-100 huntingtin Homo sapiens 116-126 30149694-1 2019 Huntington"s disease is a neurodegenerative disorder resulting from an expanded polyglutamine (polyQ) repeat of the Huntingtin (Htt) protein. polyglutamine 95-100 huntingtin Homo sapiens 128-131 30149694-3 2019 The N-terminal N17 domain proximal to the polyQ tract is key to enhance aggregation and modulate Htt toxicity. polyglutamine 42-47 huntingtin Homo sapiens 97-100 31322580-6 2019 The resulting expanded polyglutamine stretch in the huntingtin (HTT) protein induces its misfolding and aggregation, leading to neuronal dysfunction and death. polyglutamine 23-36 huntingtin Homo sapiens 52-62 31583595-2 2019 It is caused by a polyglutamine repeat expansion mutation in the widely expressed HTT protein. polyglutamine 18-31 huntingtin Homo sapiens 82-85 30540190-1 2019 Polyglutamine expansion within the N-terminal region of the huntingtin protein results in the formation of intracellular aggregates responsible for Huntington"s disease, a fatal neurodegenerative condition. polyglutamine 0-13 huntingtin Homo sapiens 60-70 30502498-1 2019 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a polyglutamine expansion mutation in the huntingtin protein. polyglutamine 90-103 huntingtin Homo sapiens 130-140 31322580-6 2019 The resulting expanded polyglutamine stretch in the huntingtin (HTT) protein induces its misfolding and aggregation, leading to neuronal dysfunction and death. polyglutamine 23-36 huntingtin Homo sapiens 64-67 30384997-6 2018 We then determined whether the mutations affected the ability of HSPA1A to prevent apoptosis caused by poly-glutamine carrying huntingtin proteins. polyglutamine 103-117 huntingtin Homo sapiens 127-137 30341614-3 2019 With the Huntington"s disease protein, polyglutamine-expanded mutant huntingtin, as an example, we provide sample preparation and imaging protocols for superresolution microscopy down to the ~30 nm-level. polyglutamine 39-52 huntingtin Homo sapiens 69-79 30315108-0 2018 The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. polyglutamine 68-81 huntingtin Homo sapiens 27-37 30315108-1 2018 Expansion of the polyglutamine (polyQ) tract in exon 1 of the huntingtin protein (Httex1) leads to Huntington"s disease resulting in fatal neurodegeneration. polyglutamine 17-30 huntingtin Homo sapiens 62-72 30315108-1 2018 Expansion of the polyglutamine (polyQ) tract in exon 1 of the huntingtin protein (Httex1) leads to Huntington"s disease resulting in fatal neurodegeneration. polyglutamine 32-37 huntingtin Homo sapiens 62-72 30156416-6 2018 The interaction of the N-terminal amphiphilic domain of huntingtin exon-1 with membrane surfaces promotes polyglutamine-mediated aggregation and, as such, is thought to play a role in the etiology of Huntington"s disease, an autosomal dominant fatal neurodegenerative condition. polyglutamine 106-119 huntingtin Homo sapiens 56-66 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 34-47 huntingtin Homo sapiens 100-110 30452683-0 2018 Mechanism suppressing H3K9 trimethylation in pluripotent stem cells and its demise by polyQ-expanded huntingtin mutations. polyglutamine 86-91 huntingtin Homo sapiens 101-111 30452683-7 2018 Notably, mutant expanded polyglutamine repeats in HTT diminish its interaction with ATF7IP-SETDB1 complex and trigger H3K9me3 in HD-iPSCs. polyglutamine 25-38 huntingtin Homo sapiens 50-53 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 34-47 huntingtin Homo sapiens 112-115 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 34-47 huntingtin Homo sapiens 164-167 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 49-54 huntingtin Homo sapiens 100-110 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 49-54 huntingtin Homo sapiens 112-115 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 49-54 huntingtin Homo sapiens 164-167 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 158-163 huntingtin Homo sapiens 100-110 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 158-163 huntingtin Homo sapiens 112-115 30486313-4 2018 In the case of HD, expansion of a polyglutamine (polyQ) stretch within the N-terminal domain of the Huntingtin (HTT) protein leads to nuclear accumulation of polyQ HTT (or mHTT) and a toxic gain-of-function phenotype resulting in neurodegeneration. polyglutamine 158-163 huntingtin Homo sapiens 164-167 30266909-1 2018 Huntington"s disease is a progressive neurodegenerative disorder caused by polyglutamine-expanded mutant huntingtin (mHTT). polyglutamine 75-88 huntingtin Homo sapiens 105-115 30143534-1 2018 PolyQ-expanded huntingtin (mHtt) variants form aggregates, termed inclusion bodies (IBs), in individuals with and models of Huntington"s disease (HD). polyglutamine 0-5 huntingtin Homo sapiens 15-25 30339373-1 2018 A pathological hallmark of Huntington"s disease (HD) is the formation of neuronal protein deposits containing mutant huntingtin fragments with expanded polyglutamine (polyQ) domains. polyglutamine 152-165 huntingtin Homo sapiens 117-127 30339373-1 2018 A pathological hallmark of Huntington"s disease (HD) is the formation of neuronal protein deposits containing mutant huntingtin fragments with expanded polyglutamine (polyQ) domains. polyglutamine 167-172 huntingtin Homo sapiens 117-127 30310861-1 2018 The neurodegenerative Huntington"s disease (HD) is caused by a polyglutamine (polyQ) amplification in the huntingtin protein (HTT). polyglutamine 63-76 huntingtin Homo sapiens 106-116 30310861-1 2018 The neurodegenerative Huntington"s disease (HD) is caused by a polyglutamine (polyQ) amplification in the huntingtin protein (HTT). polyglutamine 63-76 huntingtin Homo sapiens 126-129 30310861-1 2018 The neurodegenerative Huntington"s disease (HD) is caused by a polyglutamine (polyQ) amplification in the huntingtin protein (HTT). polyglutamine 78-83 huntingtin Homo sapiens 106-116 30310861-1 2018 The neurodegenerative Huntington"s disease (HD) is caused by a polyglutamine (polyQ) amplification in the huntingtin protein (HTT). polyglutamine 78-83 huntingtin Homo sapiens 126-129 29430620-5 2018 We found that Herp was able to bind to the overexpressed Htt N-terminal, and this interaction was enhanced by expansion of the polyQ fragment. polyglutamine 127-132 huntingtin Homo sapiens 57-60 30027901-1 2018 Huntington"s disease (HD) is caused due to an abnormal expansion of polyglutamine repeats in the first exon of huntingtin gene. polyglutamine 68-81 huntingtin Homo sapiens 111-121 30279700-10 2018 In summary, this study of STUbLs uncovers a conserved pathway that counteracts the accumulation of aggregating, transcriptionally active Htt (and possibly other poly-glutamine expanded proteins) on chromatin in both yeast and in mammalian cells. polyglutamine 161-175 huntingtin Homo sapiens 137-140 30134683-1 2018 Causative to the neurodegenerative Huntington"s disease (HD), a mutational huntingtin (HTT) protein consists of an unusual expansion on the poly-glutamine (polyQ) region in the first exon (exon-1) domain. polyglutamine 140-154 huntingtin Homo sapiens 75-85 30134683-1 2018 Causative to the neurodegenerative Huntington"s disease (HD), a mutational huntingtin (HTT) protein consists of an unusual expansion on the poly-glutamine (polyQ) region in the first exon (exon-1) domain. polyglutamine 140-154 huntingtin Homo sapiens 87-90 30134683-1 2018 Causative to the neurodegenerative Huntington"s disease (HD), a mutational huntingtin (HTT) protein consists of an unusual expansion on the poly-glutamine (polyQ) region in the first exon (exon-1) domain. polyglutamine 156-161 huntingtin Homo sapiens 75-85 30134683-1 2018 Causative to the neurodegenerative Huntington"s disease (HD), a mutational huntingtin (HTT) protein consists of an unusual expansion on the poly-glutamine (polyQ) region in the first exon (exon-1) domain. polyglutamine 156-161 huntingtin Homo sapiens 87-90 29979597-1 2018 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in Huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminus side of Huntingtin (Httex1) protein. polyglutamine 113-126 huntingtin Homo sapiens 86-96 29979597-1 2018 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in Huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminus side of Huntingtin (Httex1) protein. polyglutamine 113-126 huntingtin Homo sapiens 171-181 29979597-1 2018 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in Huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminus side of Huntingtin (Httex1) protein. polyglutamine 128-133 huntingtin Homo sapiens 86-96 29979597-1 2018 Huntington"s disease (HD) is a genetic disorder caused by a CAG expansion mutation in Huntingtin gene leading to polyglutamine (polyQ) expansion in the N-terminus side of Huntingtin (Httex1) protein. polyglutamine 128-133 huntingtin Homo sapiens 171-181 30038412-2 2018 As such, iPSCs suppress the aggregation of polyQ-expanded huntingtin (HTT), the mutant protein underlying Huntington"s disease (HD). polyglutamine 43-48 huntingtin Homo sapiens 58-68 30038412-2 2018 As such, iPSCs suppress the aggregation of polyQ-expanded huntingtin (HTT), the mutant protein underlying Huntington"s disease (HD). polyglutamine 43-48 huntingtin Homo sapiens 70-73 30038412-3 2018 Here we show that proteasome activity determines HTT levels, preventing polyQ-expanded aggregation in iPSCs from HD patients (HD-iPSCs). polyglutamine 72-77 huntingtin Homo sapiens 49-52 30472941-2 2018 HD is caused by expansion of CAG repeats in the HTT gene, which leads to pathological elongation of the polyglutamine tract within the respective protein - huntingtin. polyglutamine 104-117 huntingtin Homo sapiens 48-51 30472941-2 2018 HD is caused by expansion of CAG repeats in the HTT gene, which leads to pathological elongation of the polyglutamine tract within the respective protein - huntingtin. polyglutamine 104-117 huntingtin Homo sapiens 156-166 29789657-1 2018 Human huntingtin (Htt) contains 3144 amino acids and has an expanded polyglutamine region near the NH2-terminus in patients with Huntington"s disease. polyglutamine 69-82 huntingtin Homo sapiens 6-16 29858077-1 2018 The CAG repeat expansion that elongates the polyglutamine tract in huntingtin is the root genetic cause of Huntington"s disease (HD), a debilitating neurodegenerative disorder. polyglutamine 44-57 huntingtin Homo sapiens 67-77 29858077-4 2018 Aptamer binding to mutant huntingtin abrogated the enhanced polycomb repressive complex 2 (PRC2) stimulatory activity conferred by the expanded polyglutamine tract. polyglutamine 144-157 huntingtin Homo sapiens 26-36 30010666-1 2018 Huntington"s Disease (HD) is an inherited fatal neurodegenerative disease caused by a CAG expansion (>=36) in the first exon of the HD gene, resulting in the expression of the Huntingtin protein (Htt) or N-terminal fragments thereof with an expanded polyglutamine (polyQ) stretch. polyglutamine 250-263 huntingtin Homo sapiens 176-186 30010666-1 2018 Huntington"s Disease (HD) is an inherited fatal neurodegenerative disease caused by a CAG expansion (>=36) in the first exon of the HD gene, resulting in the expression of the Huntingtin protein (Htt) or N-terminal fragments thereof with an expanded polyglutamine (polyQ) stretch. polyglutamine 250-263 huntingtin Homo sapiens 196-199 30010666-1 2018 Huntington"s Disease (HD) is an inherited fatal neurodegenerative disease caused by a CAG expansion (>=36) in the first exon of the HD gene, resulting in the expression of the Huntingtin protein (Htt) or N-terminal fragments thereof with an expanded polyglutamine (polyQ) stretch. polyglutamine 265-270 huntingtin Homo sapiens 176-186 30010666-1 2018 Huntington"s Disease (HD) is an inherited fatal neurodegenerative disease caused by a CAG expansion (>=36) in the first exon of the HD gene, resulting in the expression of the Huntingtin protein (Htt) or N-terminal fragments thereof with an expanded polyglutamine (polyQ) stretch. polyglutamine 265-270 huntingtin Homo sapiens 196-199 29904030-3 2018 Mutant HTT (mHTT) harbors a CAG repeat extension which encodes an abnormally long polyglutamine (polyQ) repeat at HTT"s N-terminus. polyglutamine 82-95 huntingtin Homo sapiens 7-10 29904030-3 2018 Mutant HTT (mHTT) harbors a CAG repeat extension which encodes an abnormally long polyglutamine (polyQ) repeat at HTT"s N-terminus. polyglutamine 82-95 huntingtin Homo sapiens 13-16 29904030-3 2018 Mutant HTT (mHTT) harbors a CAG repeat extension which encodes an abnormally long polyglutamine (polyQ) repeat at HTT"s N-terminus. polyglutamine 97-102 huntingtin Homo sapiens 7-10 29904030-3 2018 Mutant HTT (mHTT) harbors a CAG repeat extension which encodes an abnormally long polyglutamine (polyQ) repeat at HTT"s N-terminus. polyglutamine 97-102 huntingtin Homo sapiens 13-16 29601786-1 2018 Huntingtin (HTT) fragments with extended polyglutamine tracts self-assemble into amyloid-like fibrillar aggregates. polyglutamine 41-54 huntingtin Homo sapiens 0-10 29601786-1 2018 Huntingtin (HTT) fragments with extended polyglutamine tracts self-assemble into amyloid-like fibrillar aggregates. polyglutamine 41-54 huntingtin Homo sapiens 12-15 29401586-0 2018 PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin. polyglutamine 0-5 huntingtin Homo sapiens 15-25 29401586-8 2018 PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin. polyglutamine 0-5 huntingtin Homo sapiens 15-25 29619771-2 2018 It is a polyglutamine (polyQ) disorder that is caused by an increase in the number of CAG repeats in the huntingtin (HTT) gene. polyglutamine 8-21 huntingtin Homo sapiens 105-115 29619771-2 2018 It is a polyglutamine (polyQ) disorder that is caused by an increase in the number of CAG repeats in the huntingtin (HTT) gene. polyglutamine 8-21 huntingtin Homo sapiens 117-120 29619771-2 2018 It is a polyglutamine (polyQ) disorder that is caused by an increase in the number of CAG repeats in the huntingtin (HTT) gene. polyglutamine 23-28 huntingtin Homo sapiens 105-115 29619771-2 2018 It is a polyglutamine (polyQ) disorder that is caused by an increase in the number of CAG repeats in the huntingtin (HTT) gene. polyglutamine 23-28 huntingtin Homo sapiens 117-120 29858077-7 2018 Therefore, DNA aptamers can preferentially target mutant huntingtin and modulate a gain of function endowed by the elongated polyglutamine segment. polyglutamine 125-138 huntingtin Homo sapiens 57-67 29754822-1 2018 Huntington"s disease is caused by an abnormally long polyglutamine tract in the huntingtin protein. polyglutamine 53-66 huntingtin Homo sapiens 80-90 29754822-4 2018 We found that huntingtin exon1 proteins can form reversible liquid-like assemblies, a process driven by huntingtin"s polyQ tract and proline-rich region. polyglutamine 117-122 huntingtin Homo sapiens 14-24 29754822-4 2018 We found that huntingtin exon1 proteins can form reversible liquid-like assemblies, a process driven by huntingtin"s polyQ tract and proline-rich region. polyglutamine 117-122 huntingtin Homo sapiens 104-114 29789657-1 2018 Human huntingtin (Htt) contains 3144 amino acids and has an expanded polyglutamine region near the NH2-terminus in patients with Huntington"s disease. polyglutamine 69-82 huntingtin Homo sapiens 18-21 29355642-2 2018 The polyglutamine-expanded disease protein huntingtin was shown to undergo proteolysis, which results in the accumulation of toxic and aggregation-prone fragments. polyglutamine 4-17 huntingtin Homo sapiens 43-53 29627459-0 2018 Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length. polyglutamine 126-139 huntingtin Homo sapiens 30-40 29381348-10 2018 A sliding interaction of the specific N-terminal segment of HYPK along the extended polyglutamine region of Huntingtin-exon1 is responsible for HYPK"s higher affinity for aggregation-prone Huntingtin than for its non-aggregating counterpart. polyglutamine 84-97 huntingtin Homo sapiens 108-118 29451775-2 2018 Expression of the mutant gene results in the production of a neurotoxic polyglutamine (polyQ)-expanded huntingtin (Htt) protein. polyglutamine 87-92 huntingtin Homo sapiens 103-113 29451775-2 2018 Expression of the mutant gene results in the production of a neurotoxic polyglutamine (polyQ)-expanded huntingtin (Htt) protein. polyglutamine 87-92 huntingtin Homo sapiens 115-118 29451775-3 2018 Clinical trials of knockdown therapy of mutant polyglutamine-encoding HTT mRNA in Huntington"s disease (HD) have begun. polyglutamine 47-60 huntingtin Homo sapiens 70-73 29381348-10 2018 A sliding interaction of the specific N-terminal segment of HYPK along the extended polyglutamine region of Huntingtin-exon1 is responsible for HYPK"s higher affinity for aggregation-prone Huntingtin than for its non-aggregating counterpart. polyglutamine 84-97 huntingtin Homo sapiens 189-199 29218782-3 2018 This extended CAG repeat results in production of HTT protein with an expanded polyglutamine tract, leading to pathogenic HTT protein conformers that are resistant to protein turnover, culminating in cellular toxicity and neurodegeneration. polyglutamine 79-92 huntingtin Homo sapiens 50-53 29218782-3 2018 This extended CAG repeat results in production of HTT protein with an expanded polyglutamine tract, leading to pathogenic HTT protein conformers that are resistant to protein turnover, culminating in cellular toxicity and neurodegeneration. polyglutamine 79-92 huntingtin Homo sapiens 122-125 29486399-3 2018 A human iPS cell line was generated from skin fibroblasts of a subject at the presymptomatic life stage, carrying a polyglutamine expansion in HTT gene codifying Huntingtin protein. polyglutamine 116-129 huntingtin Homo sapiens 143-146 28497201-1 2018 Huntington disease (HD) is a dominantly inherited disorder caused by a CAG expansion mutation in the huntingtin (HTT) gene, which results in the HTT protein that contains an expanded polyglutamine tract. polyglutamine 183-196 huntingtin Homo sapiens 101-111 28497201-1 2018 Huntington disease (HD) is a dominantly inherited disorder caused by a CAG expansion mutation in the huntingtin (HTT) gene, which results in the HTT protein that contains an expanded polyglutamine tract. polyglutamine 183-196 huntingtin Homo sapiens 113-116 28497201-1 2018 Huntington disease (HD) is a dominantly inherited disorder caused by a CAG expansion mutation in the huntingtin (HTT) gene, which results in the HTT protein that contains an expanded polyglutamine tract. polyglutamine 183-196 huntingtin Homo sapiens 145-148 29486399-3 2018 A human iPS cell line was generated from skin fibroblasts of a subject at the presymptomatic life stage, carrying a polyglutamine expansion in HTT gene codifying Huntingtin protein. polyglutamine 116-129 huntingtin Homo sapiens 162-172 29466333-3 2018 Furthermore, Huntington"s disease is caused by a mutation in the HTT gene, resulting in a pathogenic expansion of a polyglutamine repeat at the amino terminus of HTT. polyglutamine 116-129 huntingtin Homo sapiens 65-68 29359503-3 2018 Our method has enabled the NMR investigation of huntingtin exon1 with a 16-residue polyglutamine (poly-Q) tract, and the results indicate the presence of an N-terminal alpha-helix at near neutral pH that vanishes towards the end of the HR. polyglutamine 83-96 huntingtin Homo sapiens 48-58 29359503-3 2018 Our method has enabled the NMR investigation of huntingtin exon1 with a 16-residue polyglutamine (poly-Q) tract, and the results indicate the presence of an N-terminal alpha-helix at near neutral pH that vanishes towards the end of the HR. polyglutamine 98-104 huntingtin Homo sapiens 48-58 29358329-1 2018 Huntingtin N-terminal fragments (Htt-NTFs) with expanded polyglutamine tracts form a range of neurotoxic aggregates that are associated with Huntington"s disease. polyglutamine 57-70 huntingtin Homo sapiens 0-10 29358329-1 2018 Huntingtin N-terminal fragments (Htt-NTFs) with expanded polyglutamine tracts form a range of neurotoxic aggregates that are associated with Huntington"s disease. polyglutamine 57-70 huntingtin Homo sapiens 33-36 29358329-7 2018 Our experiments, aided by coarse-grained computer simulations and theoretical analysis, suggest that preferential binding of profilin to the M-phase species of Htt-NTFs is enhanced through a combination of specific interactions between profilin and polyproline segments and auxiliary interactions between profilin and polyglutamine tracts. polyglutamine 318-331 huntingtin Homo sapiens 160-163 29466333-3 2018 Furthermore, Huntington"s disease is caused by a mutation in the HTT gene, resulting in a pathogenic expansion of a polyglutamine repeat at the amino terminus of HTT. polyglutamine 116-129 huntingtin Homo sapiens 162-165 29232946-3 2018 Then we expressed Huntingtin protein fragments that contained polyglutamine (polyQ) sequences (Htt-polyQ), a hallmark of Huntington"s disease. polyglutamine 62-75 huntingtin Homo sapiens 18-28 29427096-3 2018 The causative genetic mutation is an expanded CAG trinucleotide repeat in the gene encoding the Huntingtin protein, which leads to a prolonged polyglutamine stretch at the N-terminus of the protein. polyglutamine 143-156 huntingtin Homo sapiens 96-106 29459817-2 2017 HD is caused by a CAG repeat expansion encoding a stretch of polyglutamine residues in the N-terminus of mutant huntingtin (mHTT) protein. polyglutamine 61-74 huntingtin Homo sapiens 112-122 29362455-3 2018 In this study, we examine recruitment of ubiquitin to IBs of polyglutamine-expanded huntingtin fragments (mHtt) by using synthesized TAMRA-labeled ubiquitin moieties. polyglutamine 61-74 huntingtin Homo sapiens 84-94 29399649-1 2018 Huntington disease (HD) is an inherited neurodegenerative disease caused by the expansion beyond a critical threshold of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 123-136 huntingtin Homo sapiens 178-188 29399649-1 2018 Huntington disease (HD) is an inherited neurodegenerative disease caused by the expansion beyond a critical threshold of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 123-136 huntingtin Homo sapiens 190-193 29399649-1 2018 Huntington disease (HD) is an inherited neurodegenerative disease caused by the expansion beyond a critical threshold of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 138-143 huntingtin Homo sapiens 178-188 29399649-1 2018 Huntington disease (HD) is an inherited neurodegenerative disease caused by the expansion beyond a critical threshold of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 138-143 huntingtin Homo sapiens 190-193 29399649-2 2018 Expanded polyQ promotes the formation of a variety of oligomeric and fibrillar aggregates of htt that accumulate into the hallmark proteinaceous inclusion bodies associated with HD. polyglutamine 9-14 huntingtin Homo sapiens 93-96 29308690-2 2018 Other neurodegenerative diseases are also characterized by neuronal protein aggregates, e.g. Huntington"s disease, associated with polyglutamine (polyQ) expansions in the protein huntingtin. polyglutamine 131-144 huntingtin Homo sapiens 179-189 29308690-2 2018 Other neurodegenerative diseases are also characterized by neuronal protein aggregates, e.g. Huntington"s disease, associated with polyglutamine (polyQ) expansions in the protein huntingtin. polyglutamine 146-151 huntingtin Homo sapiens 179-189 29413175-4 2018 The disease is a consequence of a CAG repeat extension leading to an abnormally long polyglutamine (Q) stretch at HTT"s N-terminus, which likely confers a toxic gain of function to the mutant polypeptide. polyglutamine 85-98 huntingtin Homo sapiens 114-117 29865084-1 2018 Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by a mutation that expands the polyglutamine (CAG) repeat in exon 1 of the huntingtin (HTT) gene. polyglutamine 107-120 huntingtin Homo sapiens 151-161 29865084-1 2018 Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by a mutation that expands the polyglutamine (CAG) repeat in exon 1 of the huntingtin (HTT) gene. polyglutamine 107-120 huntingtin Homo sapiens 163-166 30452421-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide expansion in the HTT gene, which encodes for an abnormal polyglutamine tract in the huntingtin protein (HTT). polyglutamine 165-178 huntingtin Homo sapiens 125-128 30452421-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide expansion in the HTT gene, which encodes for an abnormal polyglutamine tract in the huntingtin protein (HTT). polyglutamine 165-178 huntingtin Homo sapiens 192-202 30452421-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide expansion in the HTT gene, which encodes for an abnormal polyglutamine tract in the huntingtin protein (HTT). polyglutamine 165-178 huntingtin Homo sapiens 212-215 29856013-1 2018 N-terminal mutant huntingtin (mHTT) fragments with pathogenic polyglutamine (polyQ) tracts spontaneously form stable, amyloidogenic protein aggregates with a fibrillar morphology. polyglutamine 62-75 huntingtin Homo sapiens 18-28 29856013-1 2018 N-terminal mutant huntingtin (mHTT) fragments with pathogenic polyglutamine (polyQ) tracts spontaneously form stable, amyloidogenic protein aggregates with a fibrillar morphology. polyglutamine 77-82 huntingtin Homo sapiens 18-28 29856014-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by expanded polyglutamine (polyQ)-encoding repeats in the Huntingtin (HTT) gene. polyglutamine 97-110 huntingtin Homo sapiens 143-153 29856014-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by expanded polyglutamine (polyQ)-encoding repeats in the Huntingtin (HTT) gene. polyglutamine 97-110 huntingtin Homo sapiens 155-158 29856014-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by expanded polyglutamine (polyQ)-encoding repeats in the Huntingtin (HTT) gene. polyglutamine 112-117 huntingtin Homo sapiens 143-153 29856014-1 2018 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by expanded polyglutamine (polyQ)-encoding repeats in the Huntingtin (HTT) gene. polyglutamine 112-117 huntingtin Homo sapiens 155-158 29856014-2 2018 Traditionally, HD cellular models consisted of either patient cells not affected by disease or rodent neurons expressing expanded polyQ repeats in HTT. polyglutamine 130-135 huntingtin Homo sapiens 147-150 29870995-1 2018 BACKGROUND: Huntington disease (HD) is an incurable neurodegenerative disease caused by the expansion of a polyglutamine sequence in a gene encoding the huntingtin (Htt) protein, which is expressed in almost all cells of the body. polyglutamine 107-120 huntingtin Homo sapiens 153-163 29870995-1 2018 BACKGROUND: Huntington disease (HD) is an incurable neurodegenerative disease caused by the expansion of a polyglutamine sequence in a gene encoding the huntingtin (Htt) protein, which is expressed in almost all cells of the body. polyglutamine 107-120 huntingtin Homo sapiens 165-168 28972180-1 2017 Huntington"s disease (HD) is caused in large part by a polyglutamine expansion within the huntingtin (Htt) protein. polyglutamine 55-68 huntingtin Homo sapiens 90-100 28972180-1 2017 Huntington"s disease (HD) is caused in large part by a polyglutamine expansion within the huntingtin (Htt) protein. polyglutamine 55-68 huntingtin Homo sapiens 102-105 28869595-2 2017 The HD-causing mutant huntingtin protein (mHTT) has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, and the most toxic of these is the one recognized by antibody 3B5H10. polyglutamine 64-77 huntingtin Homo sapiens 22-32 28832564-1 2017 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by expansion of a CAG trinucleotide repeat in HTT, resulting in an extended polyglutamine tract in huntingtin. polyglutamine 160-173 huntingtin Homo sapiens 130-133 28832564-1 2017 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by expansion of a CAG trinucleotide repeat in HTT, resulting in an extended polyglutamine tract in huntingtin. polyglutamine 160-173 huntingtin Homo sapiens 183-193 27815841-1 2017 Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an N-terminal expansion of polyglutamine stretch (polyQ) of huntingtin (Htt) protein. polyglutamine 107-120 huntingtin Homo sapiens 140-150 27815841-1 2017 Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an N-terminal expansion of polyglutamine stretch (polyQ) of huntingtin (Htt) protein. polyglutamine 107-120 huntingtin Homo sapiens 152-155 28869595-2 2017 The HD-causing mutant huntingtin protein (mHTT) has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, and the most toxic of these is the one recognized by antibody 3B5H10. polyglutamine 79-84 huntingtin Homo sapiens 22-32 28937758-0 2017 Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths. polyglutamine 99-112 huntingtin Homo sapiens 10-20 29093475-1 2017 Huntington"s disease (HD) is caused by aberrant expansion of polyglutamine (polyQ) in the N-terminus of huntingtin (Htt). polyglutamine 61-74 huntingtin Homo sapiens 104-114 29093475-1 2017 Huntington"s disease (HD) is caused by aberrant expansion of polyglutamine (polyQ) in the N-terminus of huntingtin (Htt). polyglutamine 61-74 huntingtin Homo sapiens 116-119 29093475-1 2017 Huntington"s disease (HD) is caused by aberrant expansion of polyglutamine (polyQ) in the N-terminus of huntingtin (Htt). polyglutamine 76-81 huntingtin Homo sapiens 104-114 29093475-1 2017 Huntington"s disease (HD) is caused by aberrant expansion of polyglutamine (polyQ) in the N-terminus of huntingtin (Htt). polyglutamine 76-81 huntingtin Homo sapiens 116-119 29093475-4 2017 Our results showed that HSP90 binds to the N-terminal extreme of Htt-N in a sequence just ahead of the polyQ tract. polyglutamine 103-108 huntingtin Homo sapiens 65-70 28937758-1 2017 Huntington"s disease is caused by expansion of a polyglutamine (polyQ) domain within exon 1 of the huntingtin gene (Httex1). polyglutamine 49-62 huntingtin Homo sapiens 99-109 28937758-1 2017 Huntington"s disease is caused by expansion of a polyglutamine (polyQ) domain within exon 1 of the huntingtin gene (Httex1). polyglutamine 64-69 huntingtin Homo sapiens 99-109 29066943-1 2017 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in exon 1 of the Huntingtin (HTT) gene. polyglutamine 82-95 huntingtin Homo sapiens 131-141 29066943-1 2017 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in exon 1 of the Huntingtin (HTT) gene. polyglutamine 82-95 huntingtin Homo sapiens 143-146 29066943-1 2017 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in exon 1 of the Huntingtin (HTT) gene. polyglutamine 97-102 huntingtin Homo sapiens 131-141 29066943-1 2017 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in exon 1 of the Huntingtin (HTT) gene. polyglutamine 97-102 huntingtin Homo sapiens 143-146 28527044-6 2017 The ability to induce vesicle rupture was not specific to alpha-syn, as amyloid assemblies of tau and huntingtin Exon1 with pathologic polyglutamine repeats also exhibited the ability to induce vesicle rupture. polyglutamine 135-148 huntingtin Homo sapiens 102-112 28920088-1 2017 Huntington"s Disease (HD) is a neurodegenerative disorder caused by an expansion in a CAG-tri-nucleotide repeat that introduces a poly-glutamine stretch into the huntingtin protein (mHTT). polyglutamine 130-144 huntingtin Homo sapiens 162-172 28934390-1 2017 Huntington"s disease is neurodegenerative disorder caused by a polyglutamine expansion in the N-terminal region of the huntingtin protein (N17). polyglutamine 63-76 huntingtin Homo sapiens 119-129 28890085-2 2017 To gain insight into the role of inclusions in pathology and the in situ structure of protein aggregates inside cells, we employ advanced cryo-electron tomography methods to analyze the structure of inclusions formed by polyglutamine (polyQ)-expanded huntingtin exon 1 within their intact cellular context. polyglutamine 235-240 huntingtin Homo sapiens 251-261 28609090-1 2017 There exists strong correlation between the extended polyglutamines (polyQ) within exon-1 of Huntingtin protein (Htt) and age onset of Huntington"s disease (HD); however, the underlying molecular mechanism is still poorly understood. polyglutamine 53-67 huntingtin Homo sapiens 93-103 28841744-4 2017 The mutation induces a polyglutamine expansion in the huntingtin protein (HTT). polyglutamine 23-36 huntingtin Homo sapiens 54-64 28841744-4 2017 The mutation induces a polyglutamine expansion in the huntingtin protein (HTT). polyglutamine 23-36 huntingtin Homo sapiens 74-77 28550168-1 2017 Huntington"s disease (HD) is an inherited neurodegenerative disease caused by a polyglutamine expansion in the huntington protein (htt). polyglutamine 80-93 huntingtin Homo sapiens 111-129 28550168-1 2017 Huntington"s disease (HD) is an inherited neurodegenerative disease caused by a polyglutamine expansion in the huntington protein (htt). polyglutamine 80-93 huntingtin Homo sapiens 131-134 28848389-1 2017 Huntington disease (HD) is an incurable neurodegenerative disorder caused by expansion of CAG repeats in huntingtin (HTT) gene, resulting in expanded polyglutamine tract in HTT protein. polyglutamine 150-163 huntingtin Homo sapiens 105-115 28848389-1 2017 Huntington disease (HD) is an incurable neurodegenerative disorder caused by expansion of CAG repeats in huntingtin (HTT) gene, resulting in expanded polyglutamine tract in HTT protein. polyglutamine 150-163 huntingtin Homo sapiens 117-120 28848389-1 2017 Huntington disease (HD) is an incurable neurodegenerative disorder caused by expansion of CAG repeats in huntingtin (HTT) gene, resulting in expanded polyglutamine tract in HTT protein. polyglutamine 150-163 huntingtin Homo sapiens 173-176 28753941-2 2017 HD is caused by mutations in the Huntingtin (HTT) gene, resulting in the expansion of polyglutamine (polyQ) repeats in the HTT protein. polyglutamine 86-99 huntingtin Homo sapiens 33-43 28753941-2 2017 HD is caused by mutations in the Huntingtin (HTT) gene, resulting in the expansion of polyglutamine (polyQ) repeats in the HTT protein. polyglutamine 86-99 huntingtin Homo sapiens 45-48 28753941-2 2017 HD is caused by mutations in the Huntingtin (HTT) gene, resulting in the expansion of polyglutamine (polyQ) repeats in the HTT protein. polyglutamine 86-99 huntingtin Homo sapiens 123-126 28753941-2 2017 HD is caused by mutations in the Huntingtin (HTT) gene, resulting in the expansion of polyglutamine (polyQ) repeats in the HTT protein. polyglutamine 101-106 huntingtin Homo sapiens 33-43 28753941-2 2017 HD is caused by mutations in the Huntingtin (HTT) gene, resulting in the expansion of polyglutamine (polyQ) repeats in the HTT protein. polyglutamine 101-106 huntingtin Homo sapiens 45-48 28753941-2 2017 HD is caused by mutations in the Huntingtin (HTT) gene, resulting in the expansion of polyglutamine (polyQ) repeats in the HTT protein. polyglutamine 101-106 huntingtin Homo sapiens 123-126 28753941-3 2017 Mutant HTT is prone to aggregation, and the accumulation of polyQ-expanded fibrils as well as intermediate oligomers formed during the aggregation process contribute to neurodegeneration. polyglutamine 60-65 huntingtin Homo sapiens 7-10 28753941-5 2017 Moreover, polyQ-expanded HTT fibrils and oligomers can lead to a global collapse in neuronal proteostasis, a process that contributes to neurodegeneration. polyglutamine 10-15 huntingtin Homo sapiens 25-28 28698602-0 2017 Polyglutamine expansion affects huntingtin conformation in multiple Huntington"s disease models. polyglutamine 0-13 huntingtin Homo sapiens 32-42 28698602-2 2017 Using immunoassays and biophysical approaches, we and others have recently reported that polyglutamine expansion in purified or recombinantly expressed huntingtin (HTT) proteins affects their conformational properties in a manner dependent on both polyglutamine repeat length and temperature but independent of HTT protein fragment length. polyglutamine 89-102 huntingtin Homo sapiens 152-162 28698602-2 2017 Using immunoassays and biophysical approaches, we and others have recently reported that polyglutamine expansion in purified or recombinantly expressed huntingtin (HTT) proteins affects their conformational properties in a manner dependent on both polyglutamine repeat length and temperature but independent of HTT protein fragment length. polyglutamine 89-102 huntingtin Homo sapiens 164-167 28698602-2 2017 Using immunoassays and biophysical approaches, we and others have recently reported that polyglutamine expansion in purified or recombinantly expressed huntingtin (HTT) proteins affects their conformational properties in a manner dependent on both polyglutamine repeat length and temperature but independent of HTT protein fragment length. polyglutamine 89-102 huntingtin Homo sapiens 311-314 28698602-2 2017 Using immunoassays and biophysical approaches, we and others have recently reported that polyglutamine expansion in purified or recombinantly expressed huntingtin (HTT) proteins affects their conformational properties in a manner dependent on both polyglutamine repeat length and temperature but independent of HTT protein fragment length. polyglutamine 248-261 huntingtin Homo sapiens 152-162 28698602-2 2017 Using immunoassays and biophysical approaches, we and others have recently reported that polyglutamine expansion in purified or recombinantly expressed huntingtin (HTT) proteins affects their conformational properties in a manner dependent on both polyglutamine repeat length and temperature but independent of HTT protein fragment length. polyglutamine 248-261 huntingtin Homo sapiens 164-167 28698602-4 2017 We now report that the same conformational TR-FRET based immunoassay detects polyglutamine- and temperature-dependent changes on the endogenously expressed HTT protein in peripheral tissues and post-mortem HD brain tissue, as well as in tissues from HD animal models. polyglutamine 77-90 huntingtin Homo sapiens 156-159 28609090-1 2017 There exists strong correlation between the extended polyglutamines (polyQ) within exon-1 of Huntingtin protein (Htt) and age onset of Huntington"s disease (HD); however, the underlying molecular mechanism is still poorly understood. polyglutamine 53-67 huntingtin Homo sapiens 113-116 28609090-1 2017 There exists strong correlation between the extended polyglutamines (polyQ) within exon-1 of Huntingtin protein (Htt) and age onset of Huntington"s disease (HD); however, the underlying molecular mechanism is still poorly understood. polyglutamine 69-74 huntingtin Homo sapiens 93-103 28609090-1 2017 There exists strong correlation between the extended polyglutamines (polyQ) within exon-1 of Huntingtin protein (Htt) and age onset of Huntington"s disease (HD); however, the underlying molecular mechanism is still poorly understood. polyglutamine 69-74 huntingtin Homo sapiens 113-116 28609090-2 2017 Here we apply extensive molecular dynamics simulations to study the folding of Htt-exon-1 across five different polyQ-lengths. polyglutamine 112-117 huntingtin Homo sapiens 79-82 28900094-2 2017 Huntington"s disease (HD) results from pathological expansion of a polyglutamine stretch in the HTT molecule, being probably associated with aberrant protein-protein interactions. polyglutamine 67-80 huntingtin Homo sapiens 96-99 28406522-0 2017 Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington"s disease. polyglutamine 14-27 huntingtin Homo sapiens 51-61 28406522-1 2017 The mutant huntingtin protein (mHtt) fragments with expanded polyglutamine sequence forms microscopically visible aggregates in neurons, a hallmark of Huntington"s disease (HD). polyglutamine 61-74 huntingtin Homo sapiens 11-21 28900094-8 2017 It was assumed that polyQ-HTT may compete with postsynaptic density proteins and proteins regulating cytoskeleton remodeling. polyglutamine 20-25 huntingtin Homo sapiens 26-29 28539049-6 2017 In this study, the authors analyze the aggregation propensity of Huntingtin headpiece (httNT), which is known to facilitate the polyQ aggregation, in relation to the helix mediated aggregation mechanism proposed by the Wetzel group. polyglutamine 128-133 huntingtin Homo sapiens 65-75 28662109-7 2017 Since impaired proteasome function has been linked to the aggregation of toxic proteins including the Huntington"s disease (HD) related huntingtin (Htt) protein with expanded polyglutamine repeats, we evaluated the extent of Htt aggregation in our phospho-dead (rpt6-S119A) and phospho-mimetic (rpt6-S119D) mutants. polyglutamine 175-188 huntingtin Homo sapiens 148-151 28027448-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an expansion of CAG trinucleotide repeat (polyglutamine [polyQ]) in the huntingtin ( HTT) gene, which leads to the formation of mutant HTT (mHTT) protein aggregates. polyglutamine 109-122 huntingtin Homo sapiens 139-149 28027448-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an expansion of CAG trinucleotide repeat (polyglutamine [polyQ]) in the huntingtin ( HTT) gene, which leads to the formation of mutant HTT (mHTT) protein aggregates. polyglutamine 109-122 huntingtin Homo sapiens 152-155 28027448-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an expansion of CAG trinucleotide repeat (polyglutamine [polyQ]) in the huntingtin ( HTT) gene, which leads to the formation of mutant HTT (mHTT) protein aggregates. polyglutamine 109-122 huntingtin Homo sapiens 202-205 28027448-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an expansion of CAG trinucleotide repeat (polyglutamine [polyQ]) in the huntingtin ( HTT) gene, which leads to the formation of mutant HTT (mHTT) protein aggregates. polyglutamine 124-129 huntingtin Homo sapiens 139-149 28027448-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an expansion of CAG trinucleotide repeat (polyglutamine [polyQ]) in the huntingtin ( HTT) gene, which leads to the formation of mutant HTT (mHTT) protein aggregates. polyglutamine 124-129 huntingtin Homo sapiens 152-155 28027448-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an expansion of CAG trinucleotide repeat (polyglutamine [polyQ]) in the huntingtin ( HTT) gene, which leads to the formation of mutant HTT (mHTT) protein aggregates. polyglutamine 124-129 huntingtin Homo sapiens 202-205 28603746-1 2017 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder resulting from a polyglutamine expansion in the huntingtin (HTT) protein. polyglutamine 95-108 huntingtin Homo sapiens 126-136 28398721-1 2017 R6/2 mice contain an N-terminal fragment of human huntingtin with an expanded polyQ and develop a neurological disease resembling Huntington disease. polyglutamine 78-83 huntingtin Homo sapiens 50-60 28603746-1 2017 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder resulting from a polyglutamine expansion in the huntingtin (HTT) protein. polyglutamine 95-108 huntingtin Homo sapiens 138-141 28740725-3 2017 The mutation results in an expanded polyglutamine tract at the N-terminus of the huntingtin protein, causing the neurodegenerative pathology. polyglutamine 36-49 huntingtin Homo sapiens 81-91 28400517-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an abnormal expansion in the polyglutamine (polyQ) track of the Huntingtin (HTT) protein. polyglutamine 96-109 huntingtin Homo sapiens 131-141 28400517-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an abnormal expansion in the polyglutamine (polyQ) track of the Huntingtin (HTT) protein. polyglutamine 96-109 huntingtin Homo sapiens 143-146 28400517-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an abnormal expansion in the polyglutamine (polyQ) track of the Huntingtin (HTT) protein. polyglutamine 111-116 huntingtin Homo sapiens 131-141 28400517-1 2017 Huntington"s disease (HD) is a neurodegenerative disease caused by an abnormal expansion in the polyglutamine (polyQ) track of the Huntingtin (HTT) protein. polyglutamine 111-116 huntingtin Homo sapiens 143-146 28406616-1 2017 Huntington"s disease is a neurodegenerative disorder associated with the expansion of the polyglutamine tract in the exon-1 domain of the huntingtin protein (htte1). polyglutamine 90-103 huntingtin Homo sapiens 138-148 28263187-4 2017 We observed pathological cross-seeding between DISC1 and mutant HTT aggregates in the brains of HD patients as well as in a murine model that recapitulates the polyQ pathology of HD (R6/2 mice). polyglutamine 160-165 huntingtin Homo sapiens 64-67 28282438-2 2017 One such disorder is Huntington"s Disease (HD) that is caused by a polyglutamine expansion in the human huntingtin protein (htt). polyglutamine 67-80 huntingtin Homo sapiens 104-122 28282438-2 2017 One such disorder is Huntington"s Disease (HD) that is caused by a polyglutamine expansion in the human huntingtin protein (htt). polyglutamine 67-80 huntingtin Homo sapiens 124-127 28282438-3 2017 The polyglutamine expansion destabilizes htt leading to protein misfolding, which in turn triggers neurodegeneration and the disruption of energy metabolism in muscle cells. polyglutamine 4-17 huntingtin Homo sapiens 41-44 28282438-6 2017 We show that this htt fragment aggregates in C. elegans in a polyglutamine length-dependent manner and is toxic. polyglutamine 61-74 huntingtin Homo sapiens 18-21 27840125-1 2016 Neuronal cell death in Huntington"s Disease (HD) is associated with the abnormal expansions of a polyglutamine (polyQ) tract in the huntingtin protein (Htt) at the N-terminus that causes the misfolding and aggregation of the mutated protein (mHtt). polyglutamine 97-110 huntingtin Homo sapiens 132-142 27639641-6 2017 This mutation leads to the expression of a poly-glutamine stretch that changes the biological functions of mutant Htt (mHtt). polyglutamine 43-57 huntingtin Homo sapiens 114-117 26459990-1 2017 Huntington s Disease (HD) is a fatal neurodegenerative disorder caused by expanded polyglutamine repeats in the Huntingtin (HTT) gene. polyglutamine 83-96 huntingtin Homo sapiens 112-122 26459990-1 2017 Huntington s Disease (HD) is a fatal neurodegenerative disorder caused by expanded polyglutamine repeats in the Huntingtin (HTT) gene. polyglutamine 83-96 huntingtin Homo sapiens 124-127 28971465-2 2017 Most of the neurodegenerative diseases share same or similar cell dysfunctions and huntingtin seems to associate in an polyglutamine-length dependent manner with components of the mechanisms that can go impaired. polyglutamine 119-132 huntingtin Homo sapiens 83-93 28956337-4 2017 Indeed, huntingtin has a CAG/polyglutamine expansion in the range of 6-39 units in normal individuals, whereas it reaches 39-180 units in HD patients. polyglutamine 29-42 huntingtin Homo sapiens 8-18 28674979-4 2017 This polyglutamine expansion appears to induce a "change of function", possibly a "gain of function", in the huntingtin protein, which leads to various molecular and cellular cascades of pathogenesis. polyglutamine 5-18 huntingtin Homo sapiens 109-119 28947126-1 2017 Huntington disease (HD) is an autosomal-dominant disorder resulting from CAG triplet repeats, which leads to an expanded polyglutamine sequence in the HTT (Huntingtin) protein. polyglutamine 121-134 huntingtin Homo sapiens 151-154 28947126-1 2017 Huntington disease (HD) is an autosomal-dominant disorder resulting from CAG triplet repeats, which leads to an expanded polyglutamine sequence in the HTT (Huntingtin) protein. polyglutamine 121-134 huntingtin Homo sapiens 156-166 27840155-1 2017 Increased poly glutamine (polyQ) stretch at N-terminal of Huntingtin (HTT) causes Huntington"s disease. polyglutamine 10-24 huntingtin Homo sapiens 58-68 27840155-1 2017 Increased poly glutamine (polyQ) stretch at N-terminal of Huntingtin (HTT) causes Huntington"s disease. polyglutamine 10-24 huntingtin Homo sapiens 70-73 27840155-1 2017 Increased poly glutamine (polyQ) stretch at N-terminal of Huntingtin (HTT) causes Huntington"s disease. polyglutamine 26-31 huntingtin Homo sapiens 58-68 27840155-1 2017 Increased poly glutamine (polyQ) stretch at N-terminal of Huntingtin (HTT) causes Huntington"s disease. polyglutamine 26-31 huntingtin Homo sapiens 70-73 28339398-0 2017 N-Terminal Fragments of Huntingtin Longer than Residue 170 form Visible Aggregates Independently to Polyglutamine Expansion. polyglutamine 100-113 huntingtin Homo sapiens 24-34 28339398-1 2017 BACKGROUND: A hallmark of Huntington"s disease is the progressive aggregation of full length and N-terminal fragments of polyglutamine (polyQ)-expanded Huntingtin (Htt) into intracellular inclusions. polyglutamine 121-134 huntingtin Homo sapiens 152-162 28339398-1 2017 BACKGROUND: A hallmark of Huntington"s disease is the progressive aggregation of full length and N-terminal fragments of polyglutamine (polyQ)-expanded Huntingtin (Htt) into intracellular inclusions. polyglutamine 121-134 huntingtin Homo sapiens 164-167 28339398-1 2017 BACKGROUND: A hallmark of Huntington"s disease is the progressive aggregation of full length and N-terminal fragments of polyglutamine (polyQ)-expanded Huntingtin (Htt) into intracellular inclusions. polyglutamine 136-141 huntingtin Homo sapiens 152-162 28339398-1 2017 BACKGROUND: A hallmark of Huntington"s disease is the progressive aggregation of full length and N-terminal fragments of polyglutamine (polyQ)-expanded Huntingtin (Htt) into intracellular inclusions. polyglutamine 136-141 huntingtin Homo sapiens 164-167 28339398-4 2017 We investigated the fundamental intracellular aggregation process of eight different-length N-terminal fragments of Htt in both short (25Q) and long polyQ (97Q). polyglutamine 149-154 huntingtin Homo sapiens 116-119 27840125-1 2016 Neuronal cell death in Huntington"s Disease (HD) is associated with the abnormal expansions of a polyglutamine (polyQ) tract in the huntingtin protein (Htt) at the N-terminus that causes the misfolding and aggregation of the mutated protein (mHtt). polyglutamine 97-110 huntingtin Homo sapiens 152-155 27840125-1 2016 Neuronal cell death in Huntington"s Disease (HD) is associated with the abnormal expansions of a polyglutamine (polyQ) tract in the huntingtin protein (Htt) at the N-terminus that causes the misfolding and aggregation of the mutated protein (mHtt). polyglutamine 112-117 huntingtin Homo sapiens 132-142 27840125-1 2016 Neuronal cell death in Huntington"s Disease (HD) is associated with the abnormal expansions of a polyglutamine (polyQ) tract in the huntingtin protein (Htt) at the N-terminus that causes the misfolding and aggregation of the mutated protein (mHtt). polyglutamine 112-117 huntingtin Homo sapiens 152-155 27840125-5 2016 Here we show that the hyper-expression of mutant (>113/150) polyQ Htt is per se toxic to dopaminergic human neuroblastoma SH-SY5Y cells, and that DA exacerbates this toxicity leading to apoptosis and secondary necrosis. polyglutamine 60-65 huntingtin Homo sapiens 66-69 27713486-1 2016 Huntington disease (HD) is an autosomal neurodegenerative disorder caused by the expansion of Polyglutamine (polyQ) in exon 1 of the Huntingtin protein. polyglutamine 94-107 huntingtin Homo sapiens 133-143 27529325-1 2016 Huntington"s disease (HD) belongs to the group of inherited polyglutamine (PolyQ) diseases caused by an expanded CAG repeat in the coding region of the Huntingtin (HTT) gene that results in an elongated polyQ stretch. polyglutamine 60-73 huntingtin Homo sapiens 152-162 27529325-1 2016 Huntington"s disease (HD) belongs to the group of inherited polyglutamine (PolyQ) diseases caused by an expanded CAG repeat in the coding region of the Huntingtin (HTT) gene that results in an elongated polyQ stretch. polyglutamine 60-73 huntingtin Homo sapiens 164-167 27529325-1 2016 Huntington"s disease (HD) belongs to the group of inherited polyglutamine (PolyQ) diseases caused by an expanded CAG repeat in the coding region of the Huntingtin (HTT) gene that results in an elongated polyQ stretch. polyglutamine 75-80 huntingtin Homo sapiens 152-162 27529325-1 2016 Huntington"s disease (HD) belongs to the group of inherited polyglutamine (PolyQ) diseases caused by an expanded CAG repeat in the coding region of the Huntingtin (HTT) gene that results in an elongated polyQ stretch. polyglutamine 75-80 huntingtin Homo sapiens 164-167 27529325-1 2016 Huntington"s disease (HD) belongs to the group of inherited polyglutamine (PolyQ) diseases caused by an expanded CAG repeat in the coding region of the Huntingtin (HTT) gene that results in an elongated polyQ stretch. polyglutamine 203-208 huntingtin Homo sapiens 152-162 27529325-1 2016 Huntington"s disease (HD) belongs to the group of inherited polyglutamine (PolyQ) diseases caused by an expanded CAG repeat in the coding region of the Huntingtin (HTT) gene that results in an elongated polyQ stretch. polyglutamine 203-208 huntingtin Homo sapiens 164-167 27713486-1 2016 Huntington disease (HD) is an autosomal neurodegenerative disorder caused by the expansion of Polyglutamine (polyQ) in exon 1 of the Huntingtin protein. polyglutamine 109-114 huntingtin Homo sapiens 133-143 29963642-1 2016 Huntington"s disease (HD) is a rare, inherited, progressive, and fatal neurological disorder resulting from expanded polyglutamine repeats in the huntingtin protein. polyglutamine 117-130 huntingtin Homo sapiens 146-156 27698679-3 2016 An increase in the number of CAG repeats within the HTT gene, which lead to an expansion of polyglutamine tract in the resulting mutated HTT protein, which is toxic, is the causative factor of HD. polyglutamine 92-105 huntingtin Homo sapiens 52-55 27698679-3 2016 An increase in the number of CAG repeats within the HTT gene, which lead to an expansion of polyglutamine tract in the resulting mutated HTT protein, which is toxic, is the causative factor of HD. polyglutamine 92-105 huntingtin Homo sapiens 137-140 27677791-5 2016 Surprisingly, despite the presence of polyQ Htt aggregates in both the cytoplasm and nucleus, no significant growth defect was observed in S. pombe cells. polyglutamine 38-43 huntingtin Homo sapiens 44-47 27677791-10 2016 To study how distinct cellular environments modulate polyQ aggregation and toxicity, we expressed CAG-expanded huntingtin fragments in Schizosaccharomyces pombe In stark contrast to many other eukaryotes, S. pombe is uniquely devoid of proteins containing long polyQ tracts. polyglutamine 53-58 huntingtin Homo sapiens 111-121 27520369-1 2016 We have previously reported TR-FRET based immunoassays to detect a conformational change imparted on huntingtin protein by the polyglutamine expansion, which we confirmed using biophysical methodologies. polyglutamine 127-140 huntingtin Homo sapiens 101-111 27267344-1 2016 Huntington"s disease (HD) is a genetically-mediated neurodegenerative disorder wherein the aetiological defect is a mutation in the Huntington"s gene (HTT), which alters the structure of the huntingtin protein (Htt) through lengthening of its polyglutamine tract, thus initiating a cascade that ultimately leads to premature death. polyglutamine 243-256 huntingtin Homo sapiens 151-154 27267344-1 2016 Huntington"s disease (HD) is a genetically-mediated neurodegenerative disorder wherein the aetiological defect is a mutation in the Huntington"s gene (HTT), which alters the structure of the huntingtin protein (Htt) through lengthening of its polyglutamine tract, thus initiating a cascade that ultimately leads to premature death. polyglutamine 243-256 huntingtin Homo sapiens 191-201 27267344-1 2016 Huntington"s disease (HD) is a genetically-mediated neurodegenerative disorder wherein the aetiological defect is a mutation in the Huntington"s gene (HTT), which alters the structure of the huntingtin protein (Htt) through lengthening of its polyglutamine tract, thus initiating a cascade that ultimately leads to premature death. polyglutamine 243-256 huntingtin Homo sapiens 211-214 27133377-1 2016 The expansion of a polyglutamine repeat in huntingtin (HTT) causes Huntington disease (HD). polyglutamine 19-32 huntingtin Homo sapiens 43-53 27133377-1 2016 The expansion of a polyglutamine repeat in huntingtin (HTT) causes Huntington disease (HD). polyglutamine 19-32 huntingtin Homo sapiens 55-58 27040914-2 2016 In HD, expansion of a polyglutamine stretch within the first exon of the Huntingtin protein (Htt) leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms. polyglutamine 22-35 huntingtin Homo sapiens 73-83 27040914-2 2016 In HD, expansion of a polyglutamine stretch within the first exon of the Huntingtin protein (Htt) leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms. polyglutamine 22-35 huntingtin Homo sapiens 93-96 27040914-2 2016 In HD, expansion of a polyglutamine stretch within the first exon of the Huntingtin protein (Htt) leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms. polyglutamine 22-35 huntingtin Homo sapiens 107-110 27658206-0 2016 Polyglutamine Tract Expansion Increases S-Nitrosylation of Huntingtin and Ataxin-1. polyglutamine 0-13 huntingtin Homo sapiens 59-69 27658206-1 2016 Expansion of the polyglutamine (polyQ) tract in the huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited movement disorder linked to neurodegeneration in the striatum and cortex. polyglutamine 17-30 huntingtin Homo sapiens 52-62 27658206-1 2016 Expansion of the polyglutamine (polyQ) tract in the huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited movement disorder linked to neurodegeneration in the striatum and cortex. polyglutamine 17-30 huntingtin Homo sapiens 64-67 27658206-1 2016 Expansion of the polyglutamine (polyQ) tract in the huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited movement disorder linked to neurodegeneration in the striatum and cortex. polyglutamine 32-37 huntingtin Homo sapiens 52-62 27658206-1 2016 Expansion of the polyglutamine (polyQ) tract in the huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited movement disorder linked to neurodegeneration in the striatum and cortex. polyglutamine 32-37 huntingtin Homo sapiens 64-67 27658206-8 2016 Taken together with the evidence that S-nitrosylation of Htt is widespread and parallels polyQ expansion, these subcellular changes show that S-nitrosylation affects the biology of this protein in vivo. polyglutamine 89-94 huntingtin Homo sapiens 57-60 27033979-1 2016 Huntington"s Disease (HD) is an inherited neurodegenerative disease caused by a polyglutamine expansion in the huntingtin protein. polyglutamine 80-93 huntingtin Homo sapiens 111-121 27436896-2 2016 HD is triggered by an expansion of polyglutamine repeats in the protein huntingtin (Htt), impacting diverse cellular processes, ranging from transcriptional regulation to cognitive and motor functions. polyglutamine 35-48 huntingtin Homo sapiens 72-82 27436896-2 2016 HD is triggered by an expansion of polyglutamine repeats in the protein huntingtin (Htt), impacting diverse cellular processes, ranging from transcriptional regulation to cognitive and motor functions. polyglutamine 35-48 huntingtin Homo sapiens 84-87 27463137-1 2016 Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the huntingtin (htt) protein. polyglutamine 88-101 huntingtin Homo sapiens 144-154 27463137-1 2016 Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the huntingtin (htt) protein. polyglutamine 88-101 huntingtin Homo sapiens 156-159 27463137-1 2016 Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the huntingtin (htt) protein. polyglutamine 103-108 huntingtin Homo sapiens 144-154 27463137-1 2016 Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the huntingtin (htt) protein. polyglutamine 103-108 huntingtin Homo sapiens 156-159 27463137-2 2016 Expanded polyQ leads to htt aggregation. polyglutamine 9-14 huntingtin Homo sapiens 24-27 27377031-1 2016 Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormal expansion of polyglutamine repeats in the N-terminal of huntingtin. polyglutamine 93-106 huntingtin Homo sapiens 136-146 27170182-3 2016 Here we used a misfolded huntingtin exon I containing a 103-polyglutamine expansion (Htt103QP) as a model substrate for the functional study of ubiquilin proteins. polyglutamine 60-73 huntingtin Homo sapiens 25-35 26388396-1 2016 Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by polyglutamine expansion mutations in the huntingtin protein. polyglutamine 79-92 huntingtin Homo sapiens 120-130 27094178-0 2016 Biophysical Aspect of Huntingtin Protein During polyQ: An In Silico Insight. polyglutamine 48-53 huntingtin Homo sapiens 22-32 27094178-1 2016 Huntington"s disease (HD) is a neurodegenerative disorder that is caused by an abnormal elongation of the polyglutamine (polyQ) chain in the Huntington (Htt) protein. polyglutamine 106-119 huntingtin Homo sapiens 153-156 27094178-1 2016 Huntington"s disease (HD) is a neurodegenerative disorder that is caused by an abnormal elongation of the polyglutamine (polyQ) chain in the Huntington (Htt) protein. polyglutamine 121-126 huntingtin Homo sapiens 153-156 27094178-2 2016 At present, the normal function of Htt of neurons as well as the mechanism by which selective neurodegeneration is caused by the expanded polyQ chain in Htt remains ambiguous. polyglutamine 138-143 huntingtin Homo sapiens 153-156 27094178-3 2016 A gain of function as a result of the elongated polyQ chain can lead to abnormal interaction of the Htt protein with its interacting partners, thereby resulting in the neuropathological changes seen in the Huntington"s disease. polyglutamine 48-53 huntingtin Homo sapiens 100-103 27094178-10 2016 Our investigation of native and mutant Htt clearly shows that the structural and functional consequences of the polyQ elongation cause HD. polyglutamine 112-117 huntingtin Homo sapiens 39-42 27147961-1 2016 Huntington"s disease (HD) is an autosomal dominant, progressive neurodegenerative disease caused by an expanded polyglutamine (polyQ) tract in the N-terminal region of mutant huntingtin (mHtt). polyglutamine 112-125 huntingtin Homo sapiens 175-185 27147961-1 2016 Huntington"s disease (HD) is an autosomal dominant, progressive neurodegenerative disease caused by an expanded polyglutamine (polyQ) tract in the N-terminal region of mutant huntingtin (mHtt). polyglutamine 127-132 huntingtin Homo sapiens 175-185 26951563-1 2016 In Huntington"s disease (HD) the imperfect expanded CAG repeat in the first exon of the HTT gene leads to the generation of a polyglutamine (polyQ) protein, which has some neuronal toxicity, potentially mollified by formation of aggregates. polyglutamine 126-139 huntingtin Homo sapiens 88-91 26951563-1 2016 In Huntington"s disease (HD) the imperfect expanded CAG repeat in the first exon of the HTT gene leads to the generation of a polyglutamine (polyQ) protein, which has some neuronal toxicity, potentially mollified by formation of aggregates. polyglutamine 141-146 huntingtin Homo sapiens 88-91 26984770-4 2016 It is caused by an expanded CAG repeat in the first exon of the Huntingtin (HTT) gene, leading to an abnormal form of the Huntingtin protein (Htt) (polyQHtt), containing N-terminus, enlarged polyglutamine strands of variable length that stick together to form aggregates and nuclear inclusions in the damaged brain cells. polyglutamine 191-204 huntingtin Homo sapiens 64-74 27003594-0 2016 Huntingtin"s spherical solenoid structure enables polyglutamine tract-dependent modulation of its structure and function. polyglutamine 50-63 huntingtin Homo sapiens 0-10 27003594-1 2016 The polyglutamine expansion in huntingtin protein causes Huntington"s disease. polyglutamine 4-17 huntingtin Homo sapiens 31-41 27003594-4 2016 Interestingly, we showed that the polyglutamine expansion increases alpha-helical properties of huntingtin and affects the intramolecular interactions among the domains. polyglutamine 34-47 huntingtin Homo sapiens 96-106 27003594-5 2016 Our work delineates the structural characteristics of full-length huntingtin, which are affected by the polyglutamine expansion, and provides an elegant solution to the apparent conundrum of how the extreme amino-terminal polyglutamine tract confers a novel property on huntingtin, causing the disease. polyglutamine 104-117 huntingtin Homo sapiens 66-76 27003594-5 2016 Our work delineates the structural characteristics of full-length huntingtin, which are affected by the polyglutamine expansion, and provides an elegant solution to the apparent conundrum of how the extreme amino-terminal polyglutamine tract confers a novel property on huntingtin, causing the disease. polyglutamine 222-235 huntingtin Homo sapiens 66-76 27003594-5 2016 Our work delineates the structural characteristics of full-length huntingtin, which are affected by the polyglutamine expansion, and provides an elegant solution to the apparent conundrum of how the extreme amino-terminal polyglutamine tract confers a novel property on huntingtin, causing the disease. polyglutamine 222-235 huntingtin Homo sapiens 270-280 26984770-4 2016 It is caused by an expanded CAG repeat in the first exon of the Huntingtin (HTT) gene, leading to an abnormal form of the Huntingtin protein (Htt) (polyQHtt), containing N-terminus, enlarged polyglutamine strands of variable length that stick together to form aggregates and nuclear inclusions in the damaged brain cells. polyglutamine 191-204 huntingtin Homo sapiens 76-79 26984770-4 2016 It is caused by an expanded CAG repeat in the first exon of the Huntingtin (HTT) gene, leading to an abnormal form of the Huntingtin protein (Htt) (polyQHtt), containing N-terminus, enlarged polyglutamine strands of variable length that stick together to form aggregates and nuclear inclusions in the damaged brain cells. polyglutamine 191-204 huntingtin Homo sapiens 122-132 26984770-4 2016 It is caused by an expanded CAG repeat in the first exon of the Huntingtin (HTT) gene, leading to an abnormal form of the Huntingtin protein (Htt) (polyQHtt), containing N-terminus, enlarged polyglutamine strands of variable length that stick together to form aggregates and nuclear inclusions in the damaged brain cells. polyglutamine 191-204 huntingtin Homo sapiens 142-145 26652744-2 2016 Expanded polyQ domains are directly correlated to disease-related htt aggregation. polyglutamine 9-14 huntingtin Homo sapiens 66-69 26938440-1 2016 Huntingtin (HTT) is now a famous protein because an abnormal expansion of a glutamine stretch (polyQ) in its N-terminal sequence leads to the devastating neurodegenerative disorder Huntington"s disease (HD). polyglutamine 95-100 huntingtin Homo sapiens 0-10 26938440-1 2016 Huntingtin (HTT) is now a famous protein because an abnormal expansion of a glutamine stretch (polyQ) in its N-terminal sequence leads to the devastating neurodegenerative disorder Huntington"s disease (HD). polyglutamine 95-100 huntingtin Homo sapiens 12-15 26938440-3 2016 Subsequently, in the hope of finding a cure for HD, there has been intense research aimed at understanding the molecular mechanisms underlying the deleterious effects of the presence of the abnormal polyQ expansion in HTT. polyglutamine 199-204 huntingtin Homo sapiens 218-221 26831073-0 2016 Huntingtin exon 1 fibrils feature an interdigitated beta-hairpin-based polyglutamine core. polyglutamine 71-84 huntingtin Homo sapiens 0-10 26831073-1 2016 Polyglutamine expansion within the exon1 of huntingtin leads to protein misfolding, aggregation, and cytotoxicity in Huntington"s disease. polyglutamine 0-13 huntingtin Homo sapiens 44-54 26831073-10 2016 We show that the aggregation of mutant huntingtin exon1 proceeds via an intramolecular collapse of the expanded polyglutamine domain and discuss the implications of this observation for our understanding of its misfolding and aggregation mechanisms. polyglutamine 112-125 huntingtin Homo sapiens 39-49 27347427-2 2016 Here, we used Caenorhabdits elegans to investigate how the expression of proteotoxic triggers, such as polyglutamine (polyQ)-expanded huntingtin and silencing of proteostasis regulators, such as the ubiquitin-proteasome system (UPS) and protein clearance components, may impact the morphological remodeling of individual neurons as animals age. polyglutamine 103-116 huntingtin Homo sapiens 134-144 26850319-2 2016 Although pathogenesis has been attributed to this polyglutamine expansion, the underlying mechanisms through which the huntingtin protein functions have yet to be elucidated. polyglutamine 50-63 huntingtin Homo sapiens 119-129 28096892-6 2016 We investigate the mutation landscape of the Htt-N-terminal region and explore amino acid residue mutations that affect its structural stability and hydrophobic interactions with the polyQ domain. polyglutamine 183-188 huntingtin Homo sapiens 45-48 26819834-1 2016 Huntington disease (HD) is caused by the CAG (Q) expansion in exon 1 of the IT15 gene encoding a polyglutamine (poly-Q) stretch of the Huntingtin protein (Htt). polyglutamine 97-110 huntingtin Homo sapiens 76-80 26819834-1 2016 Huntington disease (HD) is caused by the CAG (Q) expansion in exon 1 of the IT15 gene encoding a polyglutamine (poly-Q) stretch of the Huntingtin protein (Htt). polyglutamine 97-110 huntingtin Homo sapiens 135-145 26819834-1 2016 Huntington disease (HD) is caused by the CAG (Q) expansion in exon 1 of the IT15 gene encoding a polyglutamine (poly-Q) stretch of the Huntingtin protein (Htt). polyglutamine 97-110 huntingtin Homo sapiens 155-158 27347427-2 2016 Here, we used Caenorhabdits elegans to investigate how the expression of proteotoxic triggers, such as polyglutamine (polyQ)-expanded huntingtin and silencing of proteostasis regulators, such as the ubiquitin-proteasome system (UPS) and protein clearance components, may impact the morphological remodeling of individual neurons as animals age. polyglutamine 118-123 huntingtin Homo sapiens 134-144 27347427-5 2016 The age-associated branching of PLM neurons is suppressed by N-ter polyQ-expanded Htt expression, whereas ALM neurons with polyQ-expanded Htt accumulate extended outgrowths and other soma abnormalities. polyglutamine 67-72 huntingtin Homo sapiens 82-85 27347427-5 2016 The age-associated branching of PLM neurons is suppressed by N-ter polyQ-expanded Htt expression, whereas ALM neurons with polyQ-expanded Htt accumulate extended outgrowths and other soma abnormalities. polyglutamine 123-128 huntingtin Homo sapiens 138-141 26660732-1 2015 Huntington"s disease is a neurodegenerative disorder characterised primarily by motor abnormalities, and is caused by an expanded polyglutamine repeat in the huntingtin protein. polyglutamine 130-143 huntingtin Homo sapiens 158-168 26350150-2 2016 In HD, expansion of the CAG-repeat-encoded polyglutamine (polyQ) stretch beyond ~40 glutamines in huntingtin (Htt) and its N-terminal fragments leads to the formation of large (up to several mum) globular neuronal inclusion bodies (IBs) over time. polyglutamine 43-56 huntingtin Homo sapiens 98-108 26350150-2 2016 In HD, expansion of the CAG-repeat-encoded polyglutamine (polyQ) stretch beyond ~40 glutamines in huntingtin (Htt) and its N-terminal fragments leads to the formation of large (up to several mum) globular neuronal inclusion bodies (IBs) over time. polyglutamine 43-56 huntingtin Homo sapiens 110-113 26350150-2 2016 In HD, expansion of the CAG-repeat-encoded polyglutamine (polyQ) stretch beyond ~40 glutamines in huntingtin (Htt) and its N-terminal fragments leads to the formation of large (up to several mum) globular neuronal inclusion bodies (IBs) over time. polyglutamine 58-63 huntingtin Homo sapiens 98-108 26350150-2 2016 In HD, expansion of the CAG-repeat-encoded polyglutamine (polyQ) stretch beyond ~40 glutamines in huntingtin (Htt) and its N-terminal fragments leads to the formation of large (up to several mum) globular neuronal inclusion bodies (IBs) over time. polyglutamine 58-63 huntingtin Homo sapiens 110-113 26522227-1 2015 Huntington"s disease (HD) is a neurodegenerative disorder wherein the aetiological defect is a mutation in the Huntington"s gene (HTT), which alters the structure of the huntingtin protein through the lengthening of a polyglutamine tract and initiates a cascade that ultimately leads to dementia and premature death. polyglutamine 218-231 huntingtin Homo sapiens 130-133 26522227-1 2015 Huntington"s disease (HD) is a neurodegenerative disorder wherein the aetiological defect is a mutation in the Huntington"s gene (HTT), which alters the structure of the huntingtin protein through the lengthening of a polyglutamine tract and initiates a cascade that ultimately leads to dementia and premature death. polyglutamine 218-231 huntingtin Homo sapiens 170-180 26163995-4 2015 Huntington"s disease (HD) is a neurodegenerative disorder linked to expression of polyglutamine-expanded huntingtin (HTT) protein for which there is still no disease-reversing treatment. polyglutamine 82-95 huntingtin Homo sapiens 105-115 25336039-2 2015 The mutational expansion of polyglutamine beyond a critical length produces a toxic gain of function in huntingtin and results in neuronal death. polyglutamine 28-41 huntingtin Homo sapiens 104-114 26307082-2 2015 Huntington"s disease (HD), an autosomal dominant disorder triggered by misfolding of huntingtin (HTT) protein with an expanded polyglutamine tract, could also benefit from this approach. polyglutamine 127-140 huntingtin Homo sapiens 85-95 26307082-2 2015 Huntington"s disease (HD), an autosomal dominant disorder triggered by misfolding of huntingtin (HTT) protein with an expanded polyglutamine tract, could also benefit from this approach. polyglutamine 127-140 huntingtin Homo sapiens 97-100 26100538-1 2015 Huntington"s disease (HD), a progressive neurodegenerative disease, is caused by an expanded CAG triplet repeat producing a mutant huntingtin protein (mHTT) with a polyglutamine-repeat expansion. polyglutamine 164-177 huntingtin Homo sapiens 131-141 26100538-3 2015 We report that synthetic polyglutamine oligomers and cerebrospinal fluid (CSF) from BACHD transgenic rats and from human HD subjects can seed mutant huntingtin aggregation in a cell model and its cell lysate. polyglutamine 25-38 huntingtin Homo sapiens 149-159 26495838-3 2015 Among them, a polyglutamine region that is present in huntingtin is known to exhibit a correlation between the length of the chain and the severity as well as the earliness of the onset of Huntington disease. polyglutamine 14-27 huntingtin Homo sapiens 54-64 26450664-0 2015 Conformational switch of polyglutamine-expanded huntingtin into benign aggregates leads to neuroprotective effect. polyglutamine 25-38 huntingtin Homo sapiens 48-58 26163995-4 2015 Huntington"s disease (HD) is a neurodegenerative disorder linked to expression of polyglutamine-expanded huntingtin (HTT) protein for which there is still no disease-reversing treatment. polyglutamine 82-95 huntingtin Homo sapiens 117-120 26351672-3 2015 Here we use a polyglutamine-expanded form of human huntingtin (Htt) with a fluorescent tag to monitor the spreading of aggregates in the Drosophila brain in a model of Huntington"s disease. polyglutamine 14-27 huntingtin Homo sapiens 51-61 26351672-3 2015 Here we use a polyglutamine-expanded form of human huntingtin (Htt) with a fluorescent tag to monitor the spreading of aggregates in the Drosophila brain in a model of Huntington"s disease. polyglutamine 14-27 huntingtin Homo sapiens 63-66 26160070-7 2015 In addition, because polyQ-HTT also accumulates in primary cilia, the possibility exists that primary cilia might play additional roles in HD: perhaps by disrupting signaling pathways or acting as a reservoir for secretion and propagation of toxic, misfolded polyQ-HTT fragments. polyglutamine 21-26 huntingtin Homo sapiens 27-30 26165689-0 2015 Huntingtin proteolysis releases non-polyQ fragments that cause toxicity through dynamin 1 dysregulation. polyglutamine 36-41 huntingtin Homo sapiens 0-10 28031871-4 2015 Huntington"s disease is an inherited neurodegenerative disease caused by the misfolding of an abnormally expanded polyglutamine (polyQ) region in the protein huntingtin (Htt), polyQHtt. polyglutamine 114-127 huntingtin Homo sapiens 158-168 28031871-4 2015 Huntington"s disease is an inherited neurodegenerative disease caused by the misfolding of an abnormally expanded polyglutamine (polyQ) region in the protein huntingtin (Htt), polyQHtt. polyglutamine 114-127 huntingtin Homo sapiens 170-173 28031871-4 2015 Huntington"s disease is an inherited neurodegenerative disease caused by the misfolding of an abnormally expanded polyglutamine (polyQ) region in the protein huntingtin (Htt), polyQHtt. polyglutamine 129-134 huntingtin Homo sapiens 158-168 28031871-4 2015 Huntington"s disease is an inherited neurodegenerative disease caused by the misfolding of an abnormally expanded polyglutamine (polyQ) region in the protein huntingtin (Htt), polyQHtt. polyglutamine 129-134 huntingtin Homo sapiens 170-173 26025364-1 2015 The cascade of events that lead to cognitive decline, motor deficits, and psychiatric symptoms in patients with Huntington disease (HD) is triggered by a polyglutamine expansion in the N-terminal region of the huntingtin (HTT) protein. polyglutamine 154-167 huntingtin Homo sapiens 210-220 26300964-4 2015 HD is caused by an expanded polyglutamine stretch in the N-terminal part of a 350 kDa protein called huntingtin (HTT). polyglutamine 28-41 huntingtin Homo sapiens 101-111 26300964-4 2015 HD is caused by an expanded polyglutamine stretch in the N-terminal part of a 350 kDa protein called huntingtin (HTT). polyglutamine 28-41 huntingtin Homo sapiens 113-116 26047735-1 2015 Huntington"s disease is caused by expansion of a polyglutamine (polyQ) repeat in the huntingtin protein. polyglutamine 49-62 huntingtin Homo sapiens 85-95 26047735-1 2015 Huntington"s disease is caused by expansion of a polyglutamine (polyQ) repeat in the huntingtin protein. polyglutamine 64-69 huntingtin Homo sapiens 85-95 26047735-9 2015 First, both antibodies bound to normal, as well as expanded, polyQ in huntingtin exon 1 fusion proteins. polyglutamine 61-66 huntingtin Homo sapiens 70-80 26317359-2 2015 Aggregates formed by polyglutamine (polyQ)-expanded proteins, such as Huntingtin, adopt amyloid-like structures that are resistant to denaturation. polyglutamine 21-34 huntingtin Homo sapiens 70-80 26317359-2 2015 Aggregates formed by polyglutamine (polyQ)-expanded proteins, such as Huntingtin, adopt amyloid-like structures that are resistant to denaturation. polyglutamine 36-41 huntingtin Homo sapiens 70-80 26106822-1 2015 Expansion of a CAG triplet repeat within the first exon of the HUNTINGTIN gene encoding for a polyglutamine tract is the cause of a progressive neurodegenerative disorder known as Huntington"s disease. polyglutamine 94-107 huntingtin Homo sapiens 63-73 26106822-3 2015 The biological and biophysical properties of the polyglutamine expansion within these huntingtin fragments are influenced by neighboring domains, in particular by the first 17 amino acids of huntingtin (N17), which precede the polyglutamine expansion. polyglutamine 49-62 huntingtin Homo sapiens 86-96 26106822-3 2015 The biological and biophysical properties of the polyglutamine expansion within these huntingtin fragments are influenced by neighboring domains, in particular by the first 17 amino acids of huntingtin (N17), which precede the polyglutamine expansion. polyglutamine 49-62 huntingtin Homo sapiens 191-201 26106822-3 2015 The biological and biophysical properties of the polyglutamine expansion within these huntingtin fragments are influenced by neighboring domains, in particular by the first 17 amino acids of huntingtin (N17), which precede the polyglutamine expansion. polyglutamine 227-240 huntingtin Homo sapiens 86-96 26106822-3 2015 The biological and biophysical properties of the polyglutamine expansion within these huntingtin fragments are influenced by neighboring domains, in particular by the first 17 amino acids of huntingtin (N17), which precede the polyglutamine expansion. polyglutamine 227-240 huntingtin Homo sapiens 191-201 26025364-1 2015 The cascade of events that lead to cognitive decline, motor deficits, and psychiatric symptoms in patients with Huntington disease (HD) is triggered by a polyglutamine expansion in the N-terminal region of the huntingtin (HTT) protein. polyglutamine 154-167 huntingtin Homo sapiens 222-225 25861763-1 2015 Huntington"s disease is triggered by misfolding of fragments of mutant forms of the huntingtin protein (mHTT) with aberrant polyglutamine expansions. polyglutamine 124-137 huntingtin Homo sapiens 84-94 25995452-2 2015 This DNA sequence translates to a polyglutamine repeat in the protein product, leading to mutant huntingtin (mHTT) protein aggregation. polyglutamine 34-47 huntingtin Homo sapiens 97-107 26037141-3 2015 Here we show that prefibrillar huntingtin (HTT) oligomers, isolated from Huntington"s disease (HD) affected human brain samples or mouse models, stimulate polyglutamine amyloid formation. polyglutamine 155-168 huntingtin Homo sapiens 31-41 26037141-3 2015 Here we show that prefibrillar huntingtin (HTT) oligomers, isolated from Huntington"s disease (HD) affected human brain samples or mouse models, stimulate polyglutamine amyloid formation. polyglutamine 155-168 huntingtin Homo sapiens 43-46 25740845-1 2015 Huntington"s disease (HD) is a fatal neurodegenerative disease, caused by expansion of polyglutamine repeats in the Huntingtin gene, with longer expansions leading to earlier ages of onset. polyglutamine 87-100 huntingtin Homo sapiens 116-126 26039312-0 2015 Correction: polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy. polyglutamine 12-25 huntingtin Homo sapiens 87-97 26010866-1 2015 Huntington"s disease (HD) is a devastating neurological disorder that is caused by an expansion of the poly-Q tract in exon 1 of the Huntingtin gene (HTT). polyglutamine 103-109 huntingtin Homo sapiens 133-143 26010866-1 2015 Huntington"s disease (HD) is a devastating neurological disorder that is caused by an expansion of the poly-Q tract in exon 1 of the Huntingtin gene (HTT). polyglutamine 103-109 huntingtin Homo sapiens 150-153 25741791-1 2015 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) domain that is expanded beyond a critical threshold near the N-terminus of the huntingtin (htt) protein, directly leading to htt aggregation. polyglutamine 56-61 huntingtin Homo sapiens 154-157 25993131-1 2015 Huntington disease (HD; OMIM 143100), a progressive neurodegenerative disorder, is caused by an expanded trinucleotide CAG (polyQ) motif in the HTT gene. polyglutamine 124-129 huntingtin Homo sapiens 144-147 25908449-1 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington"s disease (HD). polyglutamine 55-68 huntingtin Homo sapiens 14-24 25908449-1 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington"s disease (HD). polyglutamine 55-68 huntingtin Homo sapiens 26-29 25908449-1 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington"s disease (HD). polyglutamine 70-75 huntingtin Homo sapiens 14-24 25908449-1 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington"s disease (HD). polyglutamine 70-75 huntingtin Homo sapiens 26-29 25928884-2 2015 HD is caused by a CAG repeat expansion in the first exon of the HTT gene, resulting in an expanded polyglutamine tract at the N-terminus of the huntingtin protein. polyglutamine 99-112 huntingtin Homo sapiens 64-67 25928884-2 2015 HD is caused by a CAG repeat expansion in the first exon of the HTT gene, resulting in an expanded polyglutamine tract at the N-terminus of the huntingtin protein. polyglutamine 99-112 huntingtin Homo sapiens 144-154 25738228-2 2015 It is mainly caused by cytotoxicity of the mutant huntingtin protein (Htt) with an expanded polyQ stretch. polyglutamine 92-97 huntingtin Homo sapiens 50-60 25738228-2 2015 It is mainly caused by cytotoxicity of the mutant huntingtin protein (Htt) with an expanded polyQ stretch. polyglutamine 92-97 huntingtin Homo sapiens 70-73 27188817-3 2015 In mutation carriers, huntingtin is produced with abnormally long polyglutamine sequences that confer toxic gains of function and predispose the protein to fragmentation, resulting in neuronal dysfunction and death. polyglutamine 66-79 huntingtin Homo sapiens 22-32 25799558-2 2015 Huntington"s disease (HD) is caused by a CAG triplet amplification in exon 1 of the corresponding gene resulting in a polyglutamine (polyQ) expansion at the N-terminus of Htt. polyglutamine 118-131 huntingtin Homo sapiens 171-174 25799558-2 2015 Huntington"s disease (HD) is caused by a CAG triplet amplification in exon 1 of the corresponding gene resulting in a polyglutamine (polyQ) expansion at the N-terminus of Htt. polyglutamine 133-138 huntingtin Homo sapiens 171-174 25741791-1 2015 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) domain that is expanded beyond a critical threshold near the N-terminus of the huntingtin (htt) protein, directly leading to htt aggregation. polyglutamine 56-61 huntingtin Homo sapiens 142-152 25741791-1 2015 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) domain that is expanded beyond a critical threshold near the N-terminus of the huntingtin (htt) protein, directly leading to htt aggregation. polyglutamine 56-61 huntingtin Homo sapiens 188-191 25741791-3 2015 It is clear that polyQ length is a key determinant of htt aggregation and toxicity. polyglutamine 17-22 huntingtin Homo sapiens 54-57 24841383-1 2015 Huntington"s disease (HD) is an inherited neurodegenerative disease caused by a polyglutamine repeat expansion in the huntingtin protein. polyglutamine 80-93 huntingtin Homo sapiens 118-128 25294428-1 2015 Huntington disease is caused by expansion of a CAG repeat in the huntingtin gene that is translated into an elongated polyglutamine stretch within the N-terminal domain of the huntingtin protein. polyglutamine 118-131 huntingtin Homo sapiens 65-75 25294428-1 2015 Huntington disease is caused by expansion of a CAG repeat in the huntingtin gene that is translated into an elongated polyglutamine stretch within the N-terminal domain of the huntingtin protein. polyglutamine 118-131 huntingtin Homo sapiens 176-186 25723488-5 2015 Here we report that proteotoxic stress imposed by the proteasome inhibition or expression of polyglutamine expanded huntingtin (polyQ-Htt) induces p62 phosphorylation at its ubiquitin-association (UBA) domain that regulates its binding to ubiquitinated proteins. polyglutamine 93-106 huntingtin Homo sapiens 116-126 24841383-8 2015 Indeed, constitutive phosphorylation of huntingtin was able to restore the Deltapsim in lymphoblasts expressing an abnormal expansion of polyglutamines. polyglutamine 137-151 huntingtin Homo sapiens 40-50 25927346-1 2015 Abnormal protein interactions of mutant huntingtin (Htt) triggered by polyglutamine expansion are thought to mediate Huntington"s disease (HD) pathogenesis. polyglutamine 70-83 huntingtin Homo sapiens 40-50 25290828-1 2015 Huntington"s disease (HD) is the most common inherited neurodegenerative disorder among polyglutamine (polyQ) diseases caused by cytosine-adenine-guanine repeat expansion in exon 1 of the huntingtin gene whose translation results in polyQ stretch in the N-terminus of the huntingtin protein (HD protein). polyglutamine 88-101 huntingtin Homo sapiens 188-198 25290828-1 2015 Huntington"s disease (HD) is the most common inherited neurodegenerative disorder among polyglutamine (polyQ) diseases caused by cytosine-adenine-guanine repeat expansion in exon 1 of the huntingtin gene whose translation results in polyQ stretch in the N-terminus of the huntingtin protein (HD protein). polyglutamine 88-101 huntingtin Homo sapiens 272-282 25290828-1 2015 Huntington"s disease (HD) is the most common inherited neurodegenerative disorder among polyglutamine (polyQ) diseases caused by cytosine-adenine-guanine repeat expansion in exon 1 of the huntingtin gene whose translation results in polyQ stretch in the N-terminus of the huntingtin protein (HD protein). polyglutamine 103-108 huntingtin Homo sapiens 188-198 25290828-1 2015 Huntington"s disease (HD) is the most common inherited neurodegenerative disorder among polyglutamine (polyQ) diseases caused by cytosine-adenine-guanine repeat expansion in exon 1 of the huntingtin gene whose translation results in polyQ stretch in the N-terminus of the huntingtin protein (HD protein). polyglutamine 103-108 huntingtin Homo sapiens 272-282 25205111-6 2015 The critical domains for this response have been mapped to two regions of huntingtin flanking the polyglutamine tract, and we observe polyglutamine-expanded huntingtin-expressing cells to be defective in their ability to recover from this stress response. polyglutamine 98-111 huntingtin Homo sapiens 74-84 25205111-6 2015 The critical domains for this response have been mapped to two regions of huntingtin flanking the polyglutamine tract, and we observe polyglutamine-expanded huntingtin-expressing cells to be defective in their ability to recover from this stress response. polyglutamine 98-111 huntingtin Homo sapiens 157-167 25205111-6 2015 The critical domains for this response have been mapped to two regions of huntingtin flanking the polyglutamine tract, and we observe polyglutamine-expanded huntingtin-expressing cells to be defective in their ability to recover from this stress response. polyglutamine 134-147 huntingtin Homo sapiens 74-84 25205111-6 2015 The critical domains for this response have been mapped to two regions of huntingtin flanking the polyglutamine tract, and we observe polyglutamine-expanded huntingtin-expressing cells to be defective in their ability to recover from this stress response. polyglutamine 134-147 huntingtin Homo sapiens 157-167 25446099-2 2015 Many reports suggests roles of N-terminal 17 amino acid domain of HTT (HTT-N17) towards subcellular localization, aggregate formation and subsequent pathogenicity induced by N-terminal HTT harboring polyQ stretch in pathogenic range. polyglutamine 199-204 huntingtin Homo sapiens 66-69 25446099-2 2015 Many reports suggests roles of N-terminal 17 amino acid domain of HTT (HTT-N17) towards subcellular localization, aggregate formation and subsequent pathogenicity induced by N-terminal HTT harboring polyQ stretch in pathogenic range. polyglutamine 199-204 huntingtin Homo sapiens 71-78 25446099-2 2015 Many reports suggests roles of N-terminal 17 amino acid domain of HTT (HTT-N17) towards subcellular localization, aggregate formation and subsequent pathogenicity induced by N-terminal HTT harboring polyQ stretch in pathogenic range. polyglutamine 199-204 huntingtin Homo sapiens 71-74 25927346-1 2015 Abnormal protein interactions of mutant huntingtin (Htt) triggered by polyglutamine expansion are thought to mediate Huntington"s disease (HD) pathogenesis. polyglutamine 70-83 huntingtin Homo sapiens 52-55 25549323-6 2014 We validated this approach by detection of known yeast prions and mammalian proteins with established capacity for amyloid formation and also revealed yeast proteins forming detergent-insoluble aggregates in the presence of human huntingtin with expanded polyglutamine domain. polyglutamine 255-268 huntingtin Homo sapiens 230-240 25159076-2 2015 The genetic mutation is characterized by a CAG expansion, resulting in the formation of a mutant huntingtin protein with an expanded polyglutamine repeat region. polyglutamine 133-146 huntingtin Homo sapiens 97-107 24048953-1 2015 Huntington"s disease is caused by the expansion of a polyglutamine repeat (>37 glutamines) in the disease protein huntingtin, which results in preferential neuronal loss in distinct brain regions. polyglutamine 53-66 huntingtin Homo sapiens 114-124 25601683-1 2015 Huntington"s disease is a genetic neurodegenerative disorder caused by an expansion in a polyglutamine domain near the N-terminus of the huntingtin (htt) protein that results in the formation of protein aggregates. polyglutamine 89-102 huntingtin Homo sapiens 137-147 25601683-1 2015 Huntington"s disease is a genetic neurodegenerative disorder caused by an expansion in a polyglutamine domain near the N-terminus of the huntingtin (htt) protein that results in the formation of protein aggregates. polyglutamine 89-102 huntingtin Homo sapiens 149-152 25282404-3 2015 In Huntington disease (HD), an expansion of the polyglutamine (polyQ) tract in the N-terminus of the huntingtin (HTT) protein leads to protein aggregation. polyglutamine 48-61 huntingtin Homo sapiens 101-111 25282404-3 2015 In Huntington disease (HD), an expansion of the polyglutamine (polyQ) tract in the N-terminus of the huntingtin (HTT) protein leads to protein aggregation. polyglutamine 48-61 huntingtin Homo sapiens 113-116 25282404-3 2015 In Huntington disease (HD), an expansion of the polyglutamine (polyQ) tract in the N-terminus of the huntingtin (HTT) protein leads to protein aggregation. polyglutamine 63-68 huntingtin Homo sapiens 101-111 25282404-3 2015 In Huntington disease (HD), an expansion of the polyglutamine (polyQ) tract in the N-terminus of the huntingtin (HTT) protein leads to protein aggregation. polyglutamine 63-68 huntingtin Homo sapiens 113-116 25464275-0 2014 Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy. polyglutamine 0-13 huntingtin Homo sapiens 75-85 25330023-1 2014 Polyglutamine-expanded huntingtin, the protein encoded by HTT mutations associated with Huntington"s disease, forms aggregate species in vitro and in vivo. polyglutamine 0-13 huntingtin Homo sapiens 23-33 25330023-1 2014 Polyglutamine-expanded huntingtin, the protein encoded by HTT mutations associated with Huntington"s disease, forms aggregate species in vitro and in vivo. polyglutamine 0-13 huntingtin Homo sapiens 58-61 25464275-1 2014 BACKGROUND: In Huntington"s disease, expansion of a CAG triplet repeat occurs in exon 1 of the huntingtin gene (HTT), resulting in a protein bearing>35 polyglutamine residues whose N-terminal fragments display a high propensity to misfold and aggregate. polyglutamine 155-168 huntingtin Homo sapiens 95-105 25464275-1 2014 BACKGROUND: In Huntington"s disease, expansion of a CAG triplet repeat occurs in exon 1 of the huntingtin gene (HTT), resulting in a protein bearing>35 polyglutamine residues whose N-terminal fragments display a high propensity to misfold and aggregate. polyglutamine 155-168 huntingtin Homo sapiens 112-115 25464275-2 2014 Recent data demonstrate that polyglutamine expansion results in conformational changes in the huntingtin protein (HTT), which likely influence its biological and biophysical properties. polyglutamine 29-42 huntingtin Homo sapiens 94-104 25464275-2 2014 Recent data demonstrate that polyglutamine expansion results in conformational changes in the huntingtin protein (HTT), which likely influence its biological and biophysical properties. polyglutamine 29-42 huntingtin Homo sapiens 114-117 25464275-9 2014 Circular dichroism spectroscopy confirms the temperature and polyglutamine-dependent change in HTT structure, revealing an effect of polyglutamine length and of temperature on the alpha-helical content of the protein. polyglutamine 61-74 huntingtin Homo sapiens 95-98 25464275-9 2014 Circular dichroism spectroscopy confirms the temperature and polyglutamine-dependent change in HTT structure, revealing an effect of polyglutamine length and of temperature on the alpha-helical content of the protein. polyglutamine 133-146 huntingtin Homo sapiens 95-98 25464275-10 2014 CONCLUSIONS/SIGNIFICANCE: The temperature- and polyglutamine-dependent effects observed with TR-FRET on HTT proteins represent a simple, scalable, quantitative and sensitive assay to identify genetic and pharmacological modulators of mutant HTT conformation, and potentially to assess the relevance of conformational changes during onset and progression of Huntington"s disease. polyglutamine 47-60 huntingtin Homo sapiens 104-107 25464275-10 2014 CONCLUSIONS/SIGNIFICANCE: The temperature- and polyglutamine-dependent effects observed with TR-FRET on HTT proteins represent a simple, scalable, quantitative and sensitive assay to identify genetic and pharmacological modulators of mutant HTT conformation, and potentially to assess the relevance of conformational changes during onset and progression of Huntington"s disease. polyglutamine 47-60 huntingtin Homo sapiens 241-244 25461618-2 2014 Expansion of htt"s polyglutamine domain induces novel, toxic interactions and likely also disrupts normal htt function. polyglutamine 19-32 huntingtin Homo sapiens 13-16 25118797-1 2014 INTRODUCTION: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a polyglutamine expansion in the amino-terminal region of the huntingtin (htt) protein, which underlies the loss of striatal and cortical neurons. polyglutamine 104-117 huntingtin Homo sapiens 164-174 25118797-1 2014 INTRODUCTION: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a polyglutamine expansion in the amino-terminal region of the huntingtin (htt) protein, which underlies the loss of striatal and cortical neurons. polyglutamine 104-117 huntingtin Homo sapiens 176-179 25461618-2 2014 Expansion of htt"s polyglutamine domain induces novel, toxic interactions and likely also disrupts normal htt function. polyglutamine 19-32 huntingtin Homo sapiens 106-109 25280367-0 2014 Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance. polyglutamine 0-13 huntingtin Homo sapiens 70-80 25280367-1 2014 In Huntington"s disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation. polyglutamine 40-53 huntingtin Homo sapiens 76-86 25280367-1 2014 In Huntington"s disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation. polyglutamine 40-53 huntingtin Homo sapiens 88-91 25280367-1 2014 In Huntington"s disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation. polyglutamine 55-60 huntingtin Homo sapiens 76-86 25280367-1 2014 In Huntington"s disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation. polyglutamine 55-60 huntingtin Homo sapiens 88-91 25351248-1 2014 In patients with Huntington"s disease (HD), the protein huntingtin (Htt) has an expanded polyglutamine (poly-Q) tract. polyglutamine 89-102 huntingtin Homo sapiens 56-66 25351248-1 2014 In patients with Huntington"s disease (HD), the protein huntingtin (Htt) has an expanded polyglutamine (poly-Q) tract. polyglutamine 89-102 huntingtin Homo sapiens 68-71 25351248-1 2014 In patients with Huntington"s disease (HD), the protein huntingtin (Htt) has an expanded polyglutamine (poly-Q) tract. polyglutamine 104-110 huntingtin Homo sapiens 56-66 25351248-1 2014 In patients with Huntington"s disease (HD), the protein huntingtin (Htt) has an expanded polyglutamine (poly-Q) tract. polyglutamine 104-110 huntingtin Homo sapiens 68-71 25351248-4 2014 We found that Htt promotes signaling by mTORC1 [mechanistic target of rapamycin (mTOR) complex 1] and that this signaling is potentiated by poly-Q-expanded Htt. polyglutamine 140-146 huntingtin Homo sapiens 156-159 25351248-6 2014 Striatal cells expressing endogenous poly-Q-expanded Htt showed an increase in the number and size of mTOR puncta on the perinuclear regions compared to cells expressing wild-type Htt. polyglutamine 37-43 huntingtin Homo sapiens 53-56 25351248-6 2014 Striatal cells expressing endogenous poly-Q-expanded Htt showed an increase in the number and size of mTOR puncta on the perinuclear regions compared to cells expressing wild-type Htt. polyglutamine 37-43 huntingtin Homo sapiens 180-183 25351248-8 2014 Pharmacologically inhibiting PI3K (phosphatidylinositol 3-kinase) or knocking down Rheb abrogated mTORC1 activity induced by expression of a poly-Q-expanded amino-terminal Htt fragment. polyglutamine 141-147 huntingtin Homo sapiens 172-175 25339908-1 2014 Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by the expansion of a polyglutamine stretch within the huntingtin protein (HTT). polyglutamine 98-111 huntingtin Homo sapiens 131-141 25339908-1 2014 Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by the expansion of a polyglutamine stretch within the huntingtin protein (HTT). polyglutamine 98-111 huntingtin Homo sapiens 151-154 25309327-1 2014 HD is caused by a mutation in the huntingtin gene that consists in a CAG repeat expansion translated into an abnormal poly-glutamine (polyQ) tract in the huntingtin (Htt) protein. polyglutamine 118-132 huntingtin Homo sapiens 34-44 25324717-2 2014 This triplet expansion encodes a polyglutamine stretch (polyQ) in the N-terminus of the high molecular weight (348-kDa) and ubiquitously expressed protein htt. polyglutamine 33-46 huntingtin Homo sapiens 155-158 25324717-2 2014 This triplet expansion encodes a polyglutamine stretch (polyQ) in the N-terminus of the high molecular weight (348-kDa) and ubiquitously expressed protein htt. polyglutamine 56-61 huntingtin Homo sapiens 155-158 25309327-1 2014 HD is caused by a mutation in the huntingtin gene that consists in a CAG repeat expansion translated into an abnormal poly-glutamine (polyQ) tract in the huntingtin (Htt) protein. polyglutamine 118-132 huntingtin Homo sapiens 154-164 25309327-1 2014 HD is caused by a mutation in the huntingtin gene that consists in a CAG repeat expansion translated into an abnormal poly-glutamine (polyQ) tract in the huntingtin (Htt) protein. polyglutamine 118-132 huntingtin Homo sapiens 166-169 25309327-1 2014 HD is caused by a mutation in the huntingtin gene that consists in a CAG repeat expansion translated into an abnormal poly-glutamine (polyQ) tract in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 34-44 25309327-1 2014 HD is caused by a mutation in the huntingtin gene that consists in a CAG repeat expansion translated into an abnormal poly-glutamine (polyQ) tract in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 154-164 25309327-1 2014 HD is caused by a mutation in the huntingtin gene that consists in a CAG repeat expansion translated into an abnormal poly-glutamine (polyQ) tract in the huntingtin (Htt) protein. polyglutamine 134-139 huntingtin Homo sapiens 166-169 24534762-2 2014 We compared the distributions of polyQ repeat lengths in 8 common genes (ATXN1, ATXN2, ATXN3, CACNA1A, ATXN7, TBP, ATN1, and HTT) in 299 unrelated patients with autosomal dominant PD (ADPD) and 329 normal controls. polyglutamine 33-38 huntingtin Homo sapiens 125-128 24603212-1 2014 Huntington"s disease (HD) is an inherited neurodegenerative disorder of movement, mood and cognition, caused by a polyglutamine expansion in the huntingtin (Htt) protein. polyglutamine 114-127 huntingtin Homo sapiens 145-155 24603212-1 2014 Huntington"s disease (HD) is an inherited neurodegenerative disorder of movement, mood and cognition, caused by a polyglutamine expansion in the huntingtin (Htt) protein. polyglutamine 114-127 huntingtin Homo sapiens 157-160 25124273-1 2014 The polyglutamine expansion within huntingtin is the causative factor in the pathogenesis of Huntington"s disease (HD). polyglutamine 4-17 huntingtin Homo sapiens 35-45 24998512-4 2014 MW1 has much higher apparent affinity to mutant HTT with expanded polyQ stretch than to wild-type HTT with shorter polyQ, and thus the assays detect mutant HTT preferentially. polyglutamine 66-71 huntingtin Homo sapiens 48-51 24998512-4 2014 MW1 has much higher apparent affinity to mutant HTT with expanded polyQ stretch than to wild-type HTT with shorter polyQ, and thus the assays detect mutant HTT preferentially. polyglutamine 115-120 huntingtin Homo sapiens 98-101 24998512-4 2014 MW1 has much higher apparent affinity to mutant HTT with expanded polyQ stretch than to wild-type HTT with shorter polyQ, and thus the assays detect mutant HTT preferentially. polyglutamine 115-120 huntingtin Homo sapiens 98-101 24998512-6 2014 We further revealed that it is likely due to a temperature and polyQ length-dependent structural or spatial change of HTT, which is potentially useful for understanding polyQ structure and toxicity. polyglutamine 63-68 huntingtin Homo sapiens 118-121 24998512-6 2014 We further revealed that it is likely due to a temperature and polyQ length-dependent structural or spatial change of HTT, which is potentially useful for understanding polyQ structure and toxicity. polyglutamine 169-174 huntingtin Homo sapiens 118-121 24944802-1 2014 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by mutant huntingtin (Htt) with an expanded polyglutamine tract. polyglutamine 128-141 huntingtin Homo sapiens 94-104 24944802-1 2014 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by mutant huntingtin (Htt) with an expanded polyglutamine tract. polyglutamine 128-141 huntingtin Homo sapiens 106-109 24865853-6 2014 In a cell culture model, we demonstrate ITCH recruitment by cytoplasmic inclusions containing polyglutamine-expanded huntingtin or ataxin-3 proteins. polyglutamine 94-107 huntingtin Homo sapiens 117-127 24452335-2 2014 HD is caused by a trinucleotide CAG repeat expansion that encodes a polyglutamine stretch in the huntingtin (HTT) protein. polyglutamine 68-81 huntingtin Homo sapiens 97-107 24452335-2 2014 HD is caused by a trinucleotide CAG repeat expansion that encodes a polyglutamine stretch in the huntingtin (HTT) protein. polyglutamine 68-81 huntingtin Homo sapiens 109-112 24459296-2 2014 It is caused by the expansion of a polyglutamine tract in the huntingtin (HTT) protein, which leads to aggregation of the protein and eventually cellular death. polyglutamine 35-48 huntingtin Homo sapiens 62-72 24459296-2 2014 It is caused by the expansion of a polyglutamine tract in the huntingtin (HTT) protein, which leads to aggregation of the protein and eventually cellular death. polyglutamine 35-48 huntingtin Homo sapiens 74-77 24926995-1 2014 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder resulting from polyglutamine expansion in the huntingtin (HTT) protein and for which there is no cure. polyglutamine 93-106 huntingtin Homo sapiens 124-134 24926995-1 2014 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder resulting from polyglutamine expansion in the huntingtin (HTT) protein and for which there is no cure. polyglutamine 93-106 huntingtin Homo sapiens 136-139 25723022-1 2014 Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by a polyQ expansion (>36 glutamine repeats) in Huntingtin (Htt) protein. polyglutamine 100-105 huntingtin Homo sapiens 143-153 25723022-1 2014 Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by a polyQ expansion (>36 glutamine repeats) in Huntingtin (Htt) protein. polyglutamine 100-105 huntingtin Homo sapiens 155-158 24354677-1 2014 Huntington"s disease (HD) is caused by the presence of an extended polyglutamine (polyQ) region at the N-terminus of the huntingtin (htt) protein. polyglutamine 67-80 huntingtin Homo sapiens 121-131 24354677-1 2014 Huntington"s disease (HD) is caused by the presence of an extended polyglutamine (polyQ) region at the N-terminus of the huntingtin (htt) protein. polyglutamine 67-80 huntingtin Homo sapiens 133-136 24354677-1 2014 Huntington"s disease (HD) is caused by the presence of an extended polyglutamine (polyQ) region at the N-terminus of the huntingtin (htt) protein. polyglutamine 82-87 huntingtin Homo sapiens 121-131 24354677-1 2014 Huntington"s disease (HD) is caused by the presence of an extended polyglutamine (polyQ) region at the N-terminus of the huntingtin (htt) protein. polyglutamine 82-87 huntingtin Homo sapiens 133-136 24816435-1 2014 The expansion of a CAG trinucleotide repeat in the huntingtin gene, which produces huntingtin protein with an expanded polyglutamine tract, is the cause of Huntington"s disease (HD). polyglutamine 119-132 huntingtin Homo sapiens 51-61 24816435-1 2014 The expansion of a CAG trinucleotide repeat in the huntingtin gene, which produces huntingtin protein with an expanded polyglutamine tract, is the cause of Huntington"s disease (HD). polyglutamine 119-132 huntingtin Homo sapiens 83-93 24816435-2 2014 Recent studies have reported that RNAi suppression of polyglutamine-expanded huntingtin (mutant HTT) in HD animal models can ameliorate disease phenotypes. polyglutamine 54-67 huntingtin Homo sapiens 77-87 24816435-2 2014 Recent studies have reported that RNAi suppression of polyglutamine-expanded huntingtin (mutant HTT) in HD animal models can ameliorate disease phenotypes. polyglutamine 54-67 huntingtin Homo sapiens 96-99 24816435-4 2014 We have developed several sensitive and selective assays that measure either total human HTT or polyglutamine-expanded human HTT proteins on the electrochemiluminescence Meso Scale Discovery detection platform with an increased dynamic range over other methods. polyglutamine 96-109 huntingtin Homo sapiens 125-128 24670006-1 2014 Huntington disease (HD) is a genetic neurodegenerative disease caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin (Htt) protein, facilitating its aggregation. polyglutamine 85-98 huntingtin Homo sapiens 139-149 24795586-4 2014 HD is caused by an expanded polyglutamine stretch in the N-terminal part of a 350 kDa protein called huntingtin (HTT). polyglutamine 28-41 huntingtin Homo sapiens 101-111 24795586-4 2014 HD is caused by an expanded polyglutamine stretch in the N-terminal part of a 350 kDa protein called huntingtin (HTT). polyglutamine 28-41 huntingtin Homo sapiens 113-116 24795586-10 2014 Thus, the pathogenic polyQ expansion in HTT could lead to mood disorders not only by the gain of a new toxic function but also by the perturbation of its normal function. polyglutamine 21-26 huntingtin Homo sapiens 40-43 24670006-1 2014 Huntington disease (HD) is a genetic neurodegenerative disease caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin (Htt) protein, facilitating its aggregation. polyglutamine 85-98 huntingtin Homo sapiens 151-154 24412394-1 2014 Huntington"s disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. polyglutamine 103-116 huntingtin Homo sapiens 132-142 24584051-1 2014 Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an extended polyglutamine repeat in the N terminus of the Huntingtin protein (HTT). polyglutamine 86-99 huntingtin Homo sapiens 132-142 24584051-1 2014 Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an extended polyglutamine repeat in the N terminus of the Huntingtin protein (HTT). polyglutamine 86-99 huntingtin Homo sapiens 152-155 25054095-1 2014 Huntington disease is a rare neurodegenerative disease resulting from insertion and/or expansion of a polyglutamine repeats close to the N-terminal of the huntingtin protein. polyglutamine 102-115 huntingtin Homo sapiens 155-165 24377263-4 2014 We have used an inducible system to express human huntingtin fragments harboring normal (25Q) and pathogenic (103Q) polyglutamine lengths under the control of a galactose promoter in a yeast model of HD. polyglutamine 116-129 huntingtin Homo sapiens 50-60 24412394-1 2014 Huntington"s disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. polyglutamine 103-116 huntingtin Homo sapiens 144-147 24412394-1 2014 Huntington"s disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. polyglutamine 118-123 huntingtin Homo sapiens 132-142 24412394-1 2014 Huntington"s disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. polyglutamine 118-123 huntingtin Homo sapiens 144-147 23904097-2 2014 A highly efficient suppressor of polyQ aggregation was identified, the DNAJB6, when molecular chaperones from the HSPH, HSPA, and DNAJ families were screened for huntingtin exon 1 aggregation in cells (Hageman et al. polyglutamine 33-38 huntingtin Homo sapiens 162-172 24737938-1 2014 Huntington"s disease (HD) is a late-onset and progressive neurodegenerative disorder that is caused by aggregation of mutant huntingtin protein which contains expanded-polyglutamine. polyglutamine 168-181 huntingtin Homo sapiens 125-135 24323530-1 2014 Mutant N-terminal huntingtin (Htt) protein resulting from Huntington"s disease (HD) with expanded polyglutamine accumulates and forms aggregates in vulnerable neurons. polyglutamine 98-111 huntingtin Homo sapiens 18-28 24573776-2 2014 The genetic cause of the illness is a CAG repeat expansion in the huntingtin gene, which leads to a polyglutamine expansion in the huntingtin protein. polyglutamine 100-113 huntingtin Homo sapiens 66-76 24573776-2 2014 The genetic cause of the illness is a CAG repeat expansion in the huntingtin gene, which leads to a polyglutamine expansion in the huntingtin protein. polyglutamine 100-113 huntingtin Homo sapiens 131-141 24587280-1 2014 Huntington"s disease (HD) is a neurodegenerative disorder characterized by progressive motor, cognitive and psychiatric deficits, associated with predominant loss of striatal neurons and is caused by polyglutamine expansion in the huntingtin protein. polyglutamine 200-213 huntingtin Homo sapiens 231-241 24505464-4 2014 Using site-directed mutagenesis we introduced alterations of phosphorylation sites in a N586 Htt construct containing 82 polyglutamine repeats. polyglutamine 121-134 huntingtin Homo sapiens 93-96 24323530-1 2014 Mutant N-terminal huntingtin (Htt) protein resulting from Huntington"s disease (HD) with expanded polyglutamine accumulates and forms aggregates in vulnerable neurons. polyglutamine 98-111 huntingtin Homo sapiens 30-33 24362588-2 2014 This gene encodes a protein called Huntingtin (Htt), and mutation of the gene results in a polyglutamine (polyQ) near the N-terminus of Htt. polyglutamine 91-104 huntingtin Homo sapiens 35-45 24298020-6 2014 Interestingly, VRK2-mediated downregulation of TRiC increased aggregate formation of a polyQ-expanded huntingtin fragment. polyglutamine 87-92 huntingtin Homo sapiens 102-112 24362588-2 2014 This gene encodes a protein called Huntingtin (Htt), and mutation of the gene results in a polyglutamine (polyQ) near the N-terminus of Htt. polyglutamine 91-104 huntingtin Homo sapiens 47-50 24362588-2 2014 This gene encodes a protein called Huntingtin (Htt), and mutation of the gene results in a polyglutamine (polyQ) near the N-terminus of Htt. polyglutamine 91-104 huntingtin Homo sapiens 136-139 24362588-2 2014 This gene encodes a protein called Huntingtin (Htt), and mutation of the gene results in a polyglutamine (polyQ) near the N-terminus of Htt. polyglutamine 106-111 huntingtin Homo sapiens 35-45 24362588-2 2014 This gene encodes a protein called Huntingtin (Htt), and mutation of the gene results in a polyglutamine (polyQ) near the N-terminus of Htt. polyglutamine 106-111 huntingtin Homo sapiens 47-50 24362588-2 2014 This gene encodes a protein called Huntingtin (Htt), and mutation of the gene results in a polyglutamine (polyQ) near the N-terminus of Htt. polyglutamine 106-111 huntingtin Homo sapiens 136-139 24330821-3 2013 In this study, we used striatal cells expressing wild type (STHdhQ7/Q7) or mutant (STHdhQ111/Q111) huntingtin protein, and cortical neurons expressing the exon 1 of the huntingtin protein with physiological or pathological polyglutamine domains, to examine the interrelationship among specific mitochondrial functions. polyglutamine 223-236 huntingtin Homo sapiens 169-179 24388390-3 2014 HD is caused by mutant HTT protein (mHTT) containing an expanded polyglutamine (polyQ) stretch, but the function of mHTT and how mHTT causes HD are unknown, thus preventing efforts to screen for mHTT "inhibitors". polyglutamine 65-78 huntingtin Homo sapiens 23-26 24388390-3 2014 HD is caused by mutant HTT protein (mHTT) containing an expanded polyglutamine (polyQ) stretch, but the function of mHTT and how mHTT causes HD are unknown, thus preventing efforts to screen for mHTT "inhibitors". polyglutamine 80-85 huntingtin Homo sapiens 23-26 24359962-3 2014 PolyQ-expanded htt induced ubiquitinated aggregates cause cell death in neuronal cells. polyglutamine 0-5 huntingtin Homo sapiens 15-18 24359962-4 2014 Using a HD cellular model, we demonstrate that Tollip protects cells against the toxicity of polyQ-expanded htt and also protects cells from death (Oguro, Kubota, Shimizu, Ishiura, & Atomi, 2011). polyglutamine 93-98 huntingtin Homo sapiens 108-111 23908352-0 2013 Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes. polyglutamine 9-22 huntingtin Homo sapiens 45-55 24366087-5 2013 Strikingly, many proteins that were previously implicated in formation or clearance of intracellular aggregates, including several stress granule components, were found to co-aggregate with amyloid formed by a polyglutamine-expanded huntingtin fragment. polyglutamine 210-223 huntingtin Homo sapiens 233-243 23562876-1 2013 Huntington"s Disease is a rare neurodegenerative disease caused by an abnormal expansion of CAG repeats encoding polyglutamine in the first exon of the huntingtin gene. polyglutamine 113-126 huntingtin Homo sapiens 152-162 23908352-1 2013 Huntington disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) repeat within the protein huntingtin (Htt). polyglutamine 73-86 huntingtin Homo sapiens 121-131 23908352-1 2013 Huntington disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) repeat within the protein huntingtin (Htt). polyglutamine 73-86 huntingtin Homo sapiens 133-136 23908352-2 2013 N-terminal fragments of the mutant Htt (mHtt) proteins containing the polyQ repeat are aggregation-prone and form intracellular inclusion bodies. polyglutamine 70-75 huntingtin Homo sapiens 35-38 24012756-1 2013 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disease caused by the expansion of polyglutamine repeats in the gene for huntingtin (Htt). polyglutamine 104-117 huntingtin Homo sapiens 142-152 24012756-1 2013 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disease caused by the expansion of polyglutamine repeats in the gene for huntingtin (Htt). polyglutamine 104-117 huntingtin Homo sapiens 154-157 23898200-0 2013 Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin. polyglutamine 0-13 huntingtin Homo sapiens 86-96 23975930-0 2013 A flexible polyglutamine hinge opens new doors for understanding huntingtin function. polyglutamine 11-24 huntingtin Homo sapiens 65-75 23583659-5 2013 HD is an autosomal dominant neurodegenerative disease caused by a poly-glutamine expansion in the protein huntingtin. polyglutamine 66-80 huntingtin Homo sapiens 106-116 23898200-6 2013 This flexibility is impaired with expanded polyglutamine tracts, and we can detect changes in huntingtin conformation at the pathogenic threshold for HD. polyglutamine 43-56 huntingtin Homo sapiens 94-104 23898200-11 2013 Therefore, we hypothesize that wild-type length polyglutamine tracts within huntingtin can form a flexible domain that is essential for proper functional intramolecular proximity, conformations, and dynamics. polyglutamine 48-61 huntingtin Homo sapiens 76-86 23957861-1 2013 BACKGROUND: Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by an expansion in the polyglutamine (polyQ) region of the Huntingtin (HTT) gene. polyglutamine 112-125 huntingtin Homo sapiens 148-158 23873212-3 2013 Here, we used optical pulse labeling to measure effects of polyQ expansions on the mean lifetime of a fragment of huntingtin, the protein that causes Huntington"s disease, in living neurons. polyglutamine 59-64 huntingtin Homo sapiens 114-124 23873212-4 2013 We show that polyQ expansion reduced the mean lifetime of mutant huntingtin within a given neuron and that the mean lifetime varied among neurons, indicating differences in their capacity to clear the polypeptide. polyglutamine 13-18 huntingtin Homo sapiens 65-75 23839939-3 2013 Surprisingly, HSR activation by HSF1 overexpression or by administration of a small molecule activator lowers the concentration threshold at which HTT forms inclusion bodies in cells expressing aggregation-prone, polyglutamine-expanded fragments of HTT. polyglutamine 213-226 huntingtin Homo sapiens 147-150 23839939-3 2013 Surprisingly, HSR activation by HSF1 overexpression or by administration of a small molecule activator lowers the concentration threshold at which HTT forms inclusion bodies in cells expressing aggregation-prone, polyglutamine-expanded fragments of HTT. polyglutamine 213-226 huntingtin Homo sapiens 249-252 23957861-1 2013 BACKGROUND: Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by an expansion in the polyglutamine (polyQ) region of the Huntingtin (HTT) gene. polyglutamine 112-125 huntingtin Homo sapiens 160-163 23957861-1 2013 BACKGROUND: Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by an expansion in the polyglutamine (polyQ) region of the Huntingtin (HTT) gene. polyglutamine 127-132 huntingtin Homo sapiens 148-158 23957861-1 2013 BACKGROUND: Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by an expansion in the polyglutamine (polyQ) region of the Huntingtin (HTT) gene. polyglutamine 127-132 huntingtin Homo sapiens 160-163 23768628-3 2013 Recent findings have enhanced our understanding of the way cells regulate and respond to expanded polyglutamine proteins such as mutant huntingtin. polyglutamine 98-111 huntingtin Homo sapiens 136-146 23781027-1 2013 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by CAG expansion in the huntingtin gene, which adds a homopolymeric tract of polyglutamine (polyQ) to the encoded protein leading to the formation of toxic aggregates. polyglutamine 162-175 huntingtin Homo sapiens 109-119 23781027-1 2013 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by CAG expansion in the huntingtin gene, which adds a homopolymeric tract of polyglutamine (polyQ) to the encoded protein leading to the formation of toxic aggregates. polyglutamine 177-182 huntingtin Homo sapiens 109-119 23781027-3 2013 It has been recently reported that synthetic polyQ peptides and recombinant fragments of mutant Htt are readily internalized in cell cultures and able to seed polymerization of a reporter wild-type Htt. polyglutamine 45-50 huntingtin Homo sapiens 198-201 23931318-1 2013 The very amino-terminal domain of the huntingtin protein is directly located upstream of the protein"s polyglutamine tract, plays a decisive role in several important properties of this large protein and in the development of Huntington"s disease. polyglutamine 103-116 huntingtin Homo sapiens 38-48 23931318-9 2013 The pronounced structural transitions of huntingtin 1-17 upon membrane-association result in a alpha-helical conformation from K6 to F17, i.e., up to the very start of the polyglutamine tract. polyglutamine 172-185 huntingtin Homo sapiens 41-51 23931318-11 2013 This arrangement facilitates electrostatic interactions between huntingtin 1-17 domains and possibly with the proximal polyglutamine tract. polyglutamine 119-132 huntingtin Homo sapiens 64-74 23643759-2 2013 Aggregation is directly caused by an expanded polyglutamine (polyQ) domain in htt, leading to a diverse population of aggregate species, such as oligomers, fibrils, and annular aggregates. polyglutamine 46-59 huntingtin Homo sapiens 78-81 23643759-2 2013 Aggregation is directly caused by an expanded polyglutamine (polyQ) domain in htt, leading to a diverse population of aggregate species, such as oligomers, fibrils, and annular aggregates. polyglutamine 61-66 huntingtin Homo sapiens 78-81 23894380-1 2013 The cause of Huntington disease (HD) is a polyglutamine repeat expansion of more than 36 units in the huntingtin protein, which is inversely correlated with the age at onset of the disease. polyglutamine 42-55 huntingtin Homo sapiens 102-112 23572526-1 2013 Huntington disease (HD) is caused by an expanded polyglutamine (poly(Q)) repeat near the N terminus of the huntingtin (htt) protein. polyglutamine 49-62 huntingtin Homo sapiens 107-117 23720755-1 2013 Huntington disease is caused by cell death after the expansion of polyglutamine (polyQ) tracts longer than ~40 repeats encoded by exon 1 of the huntingtin (HTT) gene. polyglutamine 66-79 huntingtin Homo sapiens 144-154 23720755-1 2013 Huntington disease is caused by cell death after the expansion of polyglutamine (polyQ) tracts longer than ~40 repeats encoded by exon 1 of the huntingtin (HTT) gene. polyglutamine 66-79 huntingtin Homo sapiens 156-159 23720755-1 2013 Huntington disease is caused by cell death after the expansion of polyglutamine (polyQ) tracts longer than ~40 repeats encoded by exon 1 of the huntingtin (HTT) gene. polyglutamine 81-86 huntingtin Homo sapiens 144-154 23720755-1 2013 Huntington disease is caused by cell death after the expansion of polyglutamine (polyQ) tracts longer than ~40 repeats encoded by exon 1 of the huntingtin (HTT) gene. polyglutamine 81-86 huntingtin Homo sapiens 156-159 23766742-2 2013 The HD mutation causes a polyglutamine repeat expansion within the N-terminal of the huntingtin (Htt) protein. polyglutamine 25-38 huntingtin Homo sapiens 85-95 23766742-2 2013 The HD mutation causes a polyglutamine repeat expansion within the N-terminal of the huntingtin (Htt) protein. polyglutamine 25-38 huntingtin Homo sapiens 97-100 23853712-4 2013 Using cryo-electron microscopy (cryoEM) and single particle cryo-electron tomography (SPT) we characterize the growth of fibrillar aggregates of mutant huntingtin exon 1 containing an expanded polyglutamine tract with 51 residues (mhttQ51), and resolve 3-D structures of the chaperonin TRiC interacting with mhttQ51. polyglutamine 193-206 huntingtin Homo sapiens 152-162 23762270-1 2013 Intracellular accumulation of polyglutamine (polyQ)-expanded Huntingtin (Htt) protein is a hallmark of Huntington"s disease (HD). polyglutamine 30-43 huntingtin Homo sapiens 61-71 23762270-1 2013 Intracellular accumulation of polyglutamine (polyQ)-expanded Huntingtin (Htt) protein is a hallmark of Huntington"s disease (HD). polyglutamine 30-43 huntingtin Homo sapiens 73-76 23762270-1 2013 Intracellular accumulation of polyglutamine (polyQ)-expanded Huntingtin (Htt) protein is a hallmark of Huntington"s disease (HD). polyglutamine 45-50 huntingtin Homo sapiens 61-71 23762270-1 2013 Intracellular accumulation of polyglutamine (polyQ)-expanded Huntingtin (Htt) protein is a hallmark of Huntington"s disease (HD). polyglutamine 45-50 huntingtin Homo sapiens 73-76 23572526-1 2013 Huntington disease (HD) is caused by an expanded polyglutamine (poly(Q)) repeat near the N terminus of the huntingtin (htt) protein. polyglutamine 49-62 huntingtin Homo sapiens 119-122 22990145-1 2013 Huntington disease (HD) is caused by the expansion of an unstable polymorphic trinucleotide (CAG)n repeat in exon 1 of the HTT gene, which translates into an extended polyglutamine tract in the protein. polyglutamine 167-180 huntingtin Homo sapiens 123-126 23370273-0 2013 Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues. polyglutamine 21-34 huntingtin Homo sapiens 76-86 23325320-2 2013 Among them, Huntington"s disease (HD) is caused by an expanded polyglutamine repeat stretch in the N terminus of the mutant huntingtin protein (mHTT), which gets cleaved and aggregates in the brain. polyglutamine 63-76 huntingtin Homo sapiens 124-134 23370273-1 2013 Huntington disease is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine (polyQ) expansion (> 35Q) in the first exon (EX1) of huntingtin protein (Htt). polyglutamine 83-96 huntingtin Homo sapiens 153-163 23370273-1 2013 Huntington disease is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine (polyQ) expansion (> 35Q) in the first exon (EX1) of huntingtin protein (Htt). polyglutamine 83-96 huntingtin Homo sapiens 173-176 23370273-1 2013 Huntington disease is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine (polyQ) expansion (> 35Q) in the first exon (EX1) of huntingtin protein (Htt). polyglutamine 98-103 huntingtin Homo sapiens 153-163 23370273-1 2013 Huntington disease is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine (polyQ) expansion (> 35Q) in the first exon (EX1) of huntingtin protein (Htt). polyglutamine 98-103 huntingtin Homo sapiens 173-176 23319588-1 2013 Huntington disease is a dominantly inherited neurodegenerative condition caused by polyglutamine expansion in the N terminus of the huntingtin protein (Htt). polyglutamine 83-96 huntingtin Homo sapiens 132-142 23190281-1 2013 A transgenic primate model for Huntington"s Disease (HD) first reported by our group that (HD monkeys) carry the mutant Huntingtin (HTT) gene with expanded polyglutamine (CAG) repeats and, develop chorea, dystonia, and other involuntary motor deficiencies similar to HD [ 1 ]. polyglutamine 156-169 huntingtin Homo sapiens 120-130 23190281-1 2013 A transgenic primate model for Huntington"s Disease (HD) first reported by our group that (HD monkeys) carry the mutant Huntingtin (HTT) gene with expanded polyglutamine (CAG) repeats and, develop chorea, dystonia, and other involuntary motor deficiencies similar to HD [ 1 ]. polyglutamine 156-169 huntingtin Homo sapiens 132-135 23458159-1 2013 Huntington"s disease is caused by a polyglutamine expansion in huntingtin. polyglutamine 36-49 huntingtin Homo sapiens 63-73 23750301-1 2013 Nuclear accumulation of the polyglutamine-expanded mutant huntingtin protein remains one of the most predictive cell biological phenotypes of Huntington"s disease (HD) progression in patient brain samples and mouse models of the disease. polyglutamine 28-41 huntingtin Homo sapiens 58-68 23319588-1 2013 Huntington disease is a dominantly inherited neurodegenerative condition caused by polyglutamine expansion in the N terminus of the huntingtin protein (Htt). polyglutamine 83-96 huntingtin Homo sapiens 152-155 22974559-6 2013 PolyQ-htt-induced alteration of EGFR trafficking affected cell migration and proliferation, at least in part, through inhibition of ERK signaling. polyglutamine 0-5 huntingtin Homo sapiens 6-9 23148019-2 2013 Potential cross-talk between this domain and the polyQ region may play a central role in regulating the aggregation and toxicity of Htt-N-terminal fragments. polyglutamine 49-54 huntingtin Homo sapiens 132-135 23305455-1 2013 The amino-terminal domain of huntingtin (Htt17), located immediately upstream of the decisive polyglutamine tract, strongly influences important properties of this large protein and thereby the development of Huntington"s disease. polyglutamine 94-107 huntingtin Homo sapiens 29-39 23341638-1 2013 The earliest stages of Huntington disease are marked by changes in gene expression that are caused in an indirect and poorly understood manner by polyglutamine expansions in the huntingtin (HTT) protein. polyglutamine 146-159 huntingtin Homo sapiens 178-188 23341638-1 2013 The earliest stages of Huntington disease are marked by changes in gene expression that are caused in an indirect and poorly understood manner by polyglutamine expansions in the huntingtin (HTT) protein. polyglutamine 146-159 huntingtin Homo sapiens 190-193 23341638-6 2013 Our findings suggest new mechanisms for the effects of polyglutamine-expanded HTT. polyglutamine 55-68 huntingtin Homo sapiens 78-81 23089356-0 2013 Lack of huntingtin promotes neural stem cells differentiation into glial cells while neurons expressing huntingtin with expanded polyglutamine tracts undergo cell death. polyglutamine 129-142 huntingtin Homo sapiens 104-114 22974559-7 2013 To our knowledge the data here reported represent the first signaling and phenotypic characterization of polyQ-htt involvement in the modulation of growth factor stimulation in non-neuronal cells. polyglutamine 105-110 huntingtin Homo sapiens 111-114 25062676-1 2013 BACKGROUND: Huntington"s disease is a neurodegenerative disorder, typically with clinical manifestations in adult years, caused by an expanded polyglutamine-coding repeat in HTT. polyglutamine 143-156 huntingtin Homo sapiens 174-177 23723000-9 2013 A transition from full disorder to semi-disorder at about 30-40 Qs is observed in the poly-Q (poly-glutamine) tract of huntingtin. polyglutamine 86-92 huntingtin Homo sapiens 119-129 23723000-9 2013 A transition from full disorder to semi-disorder at about 30-40 Qs is observed in the poly-Q (poly-glutamine) tract of huntingtin. polyglutamine 94-108 huntingtin Homo sapiens 119-129 24217578-2 2013 However, growing evidence implicates soluble oligomeric polyglutamine-expanded huntingtin in cytotoxicity. polyglutamine 56-69 huntingtin Homo sapiens 79-89 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 94-107 huntingtin Homo sapiens 18-28 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 94-107 huntingtin Homo sapiens 30-33 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 94-107 huntingtin Homo sapiens 63-66 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 94-107 huntingtin Homo sapiens 63-66 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 109-114 huntingtin Homo sapiens 18-28 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 109-114 huntingtin Homo sapiens 30-33 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 109-114 huntingtin Homo sapiens 63-66 23754229-3 2013 In the context of huntingtin (Htt), antibodies can distinguish Htt with normal or an expanded polyglutamine (polyQ) repeats, and they can identify distinct conformations of Htt. polyglutamine 109-114 huntingtin Homo sapiens 63-66 23719918-1 2013 Aggregation of repeat-containing proteins is associated with neurodegenerative disorders; a specific example is the established link between expansion of the polyglutamine domain in huntingtin and the appearance of nuclear inclusions in Huntington"s disease. polyglutamine 158-171 huntingtin Homo sapiens 182-192 23719920-7 2013 In this assay, exon 1 variants of Htt (Htt(ex1)) containing non-pathological or HD-associated polyQ lengths were fused to two different nonfluorescent fragments of sfGFP. polyglutamine 94-99 huntingtin Homo sapiens 34-37 23324594-1 2013 The expansion of the N-terminal poly-glutamine tract of the huntingtin (Htt) protein is responsible for Huntington disease (HD). polyglutamine 32-46 huntingtin Homo sapiens 60-70 23324594-1 2013 The expansion of the N-terminal poly-glutamine tract of the huntingtin (Htt) protein is responsible for Huntington disease (HD). polyglutamine 32-46 huntingtin Homo sapiens 72-75 22891683-1 2012 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expansion of CAG trinucleotide repeats encoding for polyglutamine (polyQ) in the huntingtin (Htt) gene. polyglutamine 135-148 huntingtin Homo sapiens 164-174 23022625-9 2012 We investigated 3 polyQ-containing proteins known to interact with PQBP-1: BRN-2, Huntingtin, and ATAXIN-1, and showed a diverse nature of protein-protein interaction in Vertebrata. polyglutamine 18-23 huntingtin Homo sapiens 82-92 22814437-1 2012 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by polyglutamine expansion in the amino-terminus of huntingtin (HTT). polyglutamine 88-101 huntingtin Homo sapiens 137-147 22814437-1 2012 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by polyglutamine expansion in the amino-terminus of huntingtin (HTT). polyglutamine 88-101 huntingtin Homo sapiens 149-152 22835760-0 2012 Length of polyglutamine tract affects secondary and tertiary structures of huntingtin protein. polyglutamine 10-23 huntingtin Homo sapiens 75-85 22772050-2 2012 A polyglutamine expansion in the N-terminus of the huntingtin protein (HTT) leads to protein misfolding and downstream pathogenic processes culminating in widespread functional impairment and neurodegeneration in the striatum, cortex and other brain areas. polyglutamine 2-15 huntingtin Homo sapiens 51-61 22772050-2 2012 A polyglutamine expansion in the N-terminus of the huntingtin protein (HTT) leads to protein misfolding and downstream pathogenic processes culminating in widespread functional impairment and neurodegeneration in the striatum, cortex and other brain areas. polyglutamine 2-15 huntingtin Homo sapiens 71-74 22200539-3 2012 As a result, the translated protein huntingtin contains disease-causing expansions of glutamines (polyQ) that make it prone to misfold and aggregate. polyglutamine 98-103 huntingtin Homo sapiens 36-46 22627493-2 2012 When the number of CAG repeats exceeds 36, the translated polyglutamine-expanded Htt protein interferes with the normal functions of many types of cellular machinery and causes cytotoxicity. polyglutamine 58-71 huntingtin Homo sapiens 81-84 22891683-1 2012 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expansion of CAG trinucleotide repeats encoding for polyglutamine (polyQ) in the huntingtin (Htt) gene. polyglutamine 135-148 huntingtin Homo sapiens 176-179 22891683-1 2012 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expansion of CAG trinucleotide repeats encoding for polyglutamine (polyQ) in the huntingtin (Htt) gene. polyglutamine 150-155 huntingtin Homo sapiens 164-174 22891683-1 2012 Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expansion of CAG trinucleotide repeats encoding for polyglutamine (polyQ) in the huntingtin (Htt) gene. polyglutamine 150-155 huntingtin Homo sapiens 176-179 22875942-3 2012 Expression of an expanded polyglutamine repeat within the Huntingtin (Htt) protein impacts numerous cellular processes, including protein folding and clearance. polyglutamine 26-39 huntingtin Homo sapiens 58-68 22306738-6 2012 Using small-angle X-ray scattering, we confirmed that the polyQ epitope recognized by 3B5H10 is a compact two-stranded hairpin within monomeric htt and is abundant in htt fragments unbound to antibody. polyglutamine 58-63 huntingtin Homo sapiens 144-147 22306738-6 2012 Using small-angle X-ray scattering, we confirmed that the polyQ epitope recognized by 3B5H10 is a compact two-stranded hairpin within monomeric htt and is abundant in htt fragments unbound to antibody. polyglutamine 58-63 huntingtin Homo sapiens 167-170 22929228-1 2012 BACKGROUND: Huntington"s Disease (HD) is a fatal hereditary neurodegenerative disease caused by the accumulation of mutant huntingtin protein (Htt) containing an expanded polyglutamine (polyQ) tract. polyglutamine 171-184 huntingtin Homo sapiens 123-133 22929228-1 2012 BACKGROUND: Huntington"s Disease (HD) is a fatal hereditary neurodegenerative disease caused by the accumulation of mutant huntingtin protein (Htt) containing an expanded polyglutamine (polyQ) tract. polyglutamine 171-184 huntingtin Homo sapiens 143-146 22929228-1 2012 BACKGROUND: Huntington"s Disease (HD) is a fatal hereditary neurodegenerative disease caused by the accumulation of mutant huntingtin protein (Htt) containing an expanded polyglutamine (polyQ) tract. polyglutamine 186-191 huntingtin Homo sapiens 123-133 22929228-1 2012 BACKGROUND: Huntington"s Disease (HD) is a fatal hereditary neurodegenerative disease caused by the accumulation of mutant huntingtin protein (Htt) containing an expanded polyglutamine (polyQ) tract. polyglutamine 186-191 huntingtin Homo sapiens 143-146 22748967-2 2012 Expansion of the polyglutamine tract in the huntingtin protein results in massive cell death in the striatum of HD patients. polyglutamine 17-30 huntingtin Homo sapiens 44-54 22875942-3 2012 Expression of an expanded polyglutamine repeat within the Huntingtin (Htt) protein impacts numerous cellular processes, including protein folding and clearance. polyglutamine 26-39 huntingtin Homo sapiens 70-73 22617512-1 2012 Huntington disease (HD) is caused by an extended polyglutamine [poly(Q)] stretch in the Huntingtin (HTT) protein, and is associated with the accumulation of intracellular protein aggregates, onset of progressive chorea, psychiatric symptoms and dementia. polyglutamine 49-62 huntingtin Homo sapiens 88-98 22648412-1 2012 Huntington disease (HD) is an inherited neurodegenerative disorder caused by an abnormal polyglutamine expansion in the protein Huntingtin (Htt). polyglutamine 89-102 huntingtin Homo sapiens 128-138 22648412-1 2012 Huntington disease (HD) is an inherited neurodegenerative disorder caused by an abnormal polyglutamine expansion in the protein Huntingtin (Htt). polyglutamine 89-102 huntingtin Homo sapiens 140-143 26307259-1 2012 Huntington"s disease (HD) is a fatal neurodegenerative disorder that is caused by a CAG repeat expansion encoding a polyglutamine tract in the huntingtin (htt) gene. polyglutamine 116-129 huntingtin Homo sapiens 143-153 26307259-1 2012 Huntington"s disease (HD) is a fatal neurodegenerative disorder that is caused by a CAG repeat expansion encoding a polyglutamine tract in the huntingtin (htt) gene. polyglutamine 116-129 huntingtin Homo sapiens 155-158 22741533-1 2012 BACKGROUND: Huntington"s disease (HD) is a fatal progressive neurodegenerative disorder caused by the expansion of the polyglutamine repeat region in the huntingtin gene. polyglutamine 119-132 huntingtin Homo sapiens 154-164 22617512-1 2012 Huntington disease (HD) is caused by an extended polyglutamine [poly(Q)] stretch in the Huntingtin (HTT) protein, and is associated with the accumulation of intracellular protein aggregates, onset of progressive chorea, psychiatric symptoms and dementia. polyglutamine 49-62 huntingtin Homo sapiens 100-103 22617512-1 2012 Huntington disease (HD) is caused by an extended polyglutamine [poly(Q)] stretch in the Huntingtin (HTT) protein, and is associated with the accumulation of intracellular protein aggregates, onset of progressive chorea, psychiatric symptoms and dementia. polyglutamine 64-71 huntingtin Homo sapiens 88-98 22617512-1 2012 Huntington disease (HD) is caused by an extended polyglutamine [poly(Q)] stretch in the Huntingtin (HTT) protein, and is associated with the accumulation of intracellular protein aggregates, onset of progressive chorea, psychiatric symptoms and dementia. polyglutamine 64-71 huntingtin Homo sapiens 100-103 22580459-0 2012 Huntingtin protein interactions altered by polyglutamine expansion as determined by quantitative proteomic analysis. polyglutamine 43-56 huntingtin Homo sapiens 0-10 22399227-1 2012 Huntington"s disease (HD) is a hereditary neurodegenerative disorder resulting from the expansion of a polyglutamine tract in the huntingtin protein. polyglutamine 103-116 huntingtin Homo sapiens 130-140 22426400-0 2012 Huntingtin with an expanded polyglutamine repeat affects the Jab1-p27(Kip1) pathway. polyglutamine 28-41 huntingtin Homo sapiens 0-10 22623107-1 2012 Huntington"s disease (HD) is caused by a CAG triplet repeat expansion in exon 1 of the Huntingtin (Htt) gene, encoding an abnormal expanded polyglutamine (polyQ) tract that confers toxicity to the mutant Htt (mHtt) protein. polyglutamine 140-153 huntingtin Homo sapiens 87-97 22623107-1 2012 Huntington"s disease (HD) is caused by a CAG triplet repeat expansion in exon 1 of the Huntingtin (Htt) gene, encoding an abnormal expanded polyglutamine (polyQ) tract that confers toxicity to the mutant Htt (mHtt) protein. polyglutamine 140-153 huntingtin Homo sapiens 99-102 22623107-1 2012 Huntington"s disease (HD) is caused by a CAG triplet repeat expansion in exon 1 of the Huntingtin (Htt) gene, encoding an abnormal expanded polyglutamine (polyQ) tract that confers toxicity to the mutant Htt (mHtt) protein. polyglutamine 140-153 huntingtin Homo sapiens 204-207 22613578-3 2012 The causative mutation of this hereditary disease is a trinucleotide repeat expansion (CAG) in the Huntingtin gene that results in an expanded polyglutamine tract. polyglutamine 143-156 huntingtin Homo sapiens 99-109 22580459-1 2012 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of a polyglutamine repeat within the HD gene product, huntingtin. polyglutamine 84-97 huntingtin Homo sapiens 133-143 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 3-16 huntingtin Homo sapiens 82-92 22352297-1 2012 An unstable expansion of the polyglutamine repeat within exon 1 of the protein Htt (huntingtin) causes HD (Huntington"s disease). polyglutamine 29-42 huntingtin Homo sapiens 79-82 22352297-1 2012 An unstable expansion of the polyglutamine repeat within exon 1 of the protein Htt (huntingtin) causes HD (Huntington"s disease). polyglutamine 29-42 huntingtin Homo sapiens 84-94 22375012-1 2012 Huntington disease (HD) is caused by polyglutamine expansion in the N terminus of huntingtin (htt). polyglutamine 37-50 huntingtin Homo sapiens 82-92 22375012-1 2012 Huntington disease (HD) is caused by polyglutamine expansion in the N terminus of huntingtin (htt). polyglutamine 37-50 huntingtin Homo sapiens 94-97 22375012-5 2012 Anti-polyglutamine antisera detected full-length mutant htt in HD brain. polyglutamine 5-18 huntingtin Homo sapiens 56-59 22433867-7 2012 Importantly, these species are recognized by 3B5H10, an antibody that recognizes a two-stranded hairpin conformation of expanded polyglutamine believed to be associated with a toxic form of huntingtin. polyglutamine 129-142 huntingtin Homo sapiens 190-200 22138129-2 2012 The disease is caused by a cytosine-adenine-guanine (CAG) repeat expansion in the huntingtin gene, which causes an expanded polyglutamine repeat in the huntingtin protein, resulting in a protein with a novel gain of function. polyglutamine 124-137 huntingtin Homo sapiens 82-92 22138129-2 2012 The disease is caused by a cytosine-adenine-guanine (CAG) repeat expansion in the huntingtin gene, which causes an expanded polyglutamine repeat in the huntingtin protein, resulting in a protein with a novel gain of function. polyglutamine 124-137 huntingtin Homo sapiens 152-162 22446390-1 2012 Intense research on the pathogenesis of Huntington"s disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, revealed multiple potential mechanisms, among which mitochondrial alterations had emerged as key determinants of the natural history of the disease. polyglutamine 115-128 huntingtin Homo sapiens 146-156 22446390-1 2012 Intense research on the pathogenesis of Huntington"s disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, revealed multiple potential mechanisms, among which mitochondrial alterations had emerged as key determinants of the natural history of the disease. polyglutamine 115-128 huntingtin Homo sapiens 158-161 22251933-1 2012 INTRODUCTION: Huntington"s disease (HD) is a neurodegenerative genetic disorder caused by expansion of polyglutamine repeats in the huntingtin gene and characterised by the loss of striatal and cortical neurons. polyglutamine 103-116 huntingtin Homo sapiens 132-142 21964520-1 2012 Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. polyglutamine 120-134 huntingtin Homo sapiens 95-105 21964520-1 2012 Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. polyglutamine 136-142 huntingtin Homo sapiens 95-105 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 3-16 huntingtin Homo sapiens 94-97 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 3-16 huntingtin Homo sapiens 129-132 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 18-23 huntingtin Homo sapiens 82-92 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 18-23 huntingtin Homo sapiens 94-97 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 18-23 huntingtin Homo sapiens 129-132 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 242-247 huntingtin Homo sapiens 82-92 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 242-247 huntingtin Homo sapiens 94-97 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 242-247 huntingtin Homo sapiens 129-132 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 242-247 huntingtin Homo sapiens 82-92 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 242-247 huntingtin Homo sapiens 94-97 22432740-1 2012 In polyglutamine (polyQ) containing fragments of the Huntington"s disease protein huntingtin (htt), the N-terminal 17 amino acid htt(NT) segment serves as the core of alpha-helical oligomers whose reversible assembly locally concentrates the polyQ segments, thereby facilitating polyQ amyloid nucleation. polyglutamine 242-247 huntingtin Homo sapiens 129-132 22432740-5 2012 That is, under htt(NT) inhibition, nucleation of polyQ amyloid formation by a previously described alternative nucleation mechanism proceeds unabated and transiently dominates the aggregation process. polyglutamine 49-54 huntingtin Homo sapiens 15-18 22432740-8 2012 These data show that the htt(NT)-dependent and -independent pathways of amyloid nucleation in polyQ-containing htt fragments are in direct kinetic competition. polyglutamine 94-99 huntingtin Homo sapiens 25-28 22432740-8 2012 These data show that the htt(NT)-dependent and -independent pathways of amyloid nucleation in polyQ-containing htt fragments are in direct kinetic competition. polyglutamine 94-99 huntingtin Homo sapiens 111-114 22252996-1 2012 Huntington"s disease is caused by expression of a mutant form of Huntingtin protein containing an expanded polyglutamine repeat. polyglutamine 107-120 huntingtin Homo sapiens 65-75 22103299-1 2012 HD (Huntington"s disease) is caused by an expanded polyQ (polyglutamine) repeat in the htt (huntingtin protein). polyglutamine 51-56 huntingtin Homo sapiens 87-90 22198539-2 2012 This expansion creates a toxic polyglutamine tract in the huntingtin protein (HTT). polyglutamine 31-44 huntingtin Homo sapiens 58-68 22198539-2 2012 This expansion creates a toxic polyglutamine tract in the huntingtin protein (HTT). polyglutamine 31-44 huntingtin Homo sapiens 78-81 22234237-0 2012 Truncated N-terminal huntingtin fragment with expanded-polyglutamine (htt552-100Q) suppresses brain-derived neurotrophic factor transcription in astrocytes. polyglutamine 54-68 huntingtin Homo sapiens 21-31 22103299-1 2012 HD (Huntington"s disease) is caused by an expanded polyQ (polyglutamine) repeat in the htt (huntingtin protein). polyglutamine 51-56 huntingtin Homo sapiens 92-102 22103299-1 2012 HD (Huntington"s disease) is caused by an expanded polyQ (polyglutamine) repeat in the htt (huntingtin protein). polyglutamine 58-71 huntingtin Homo sapiens 87-90 22103299-1 2012 HD (Huntington"s disease) is caused by an expanded polyQ (polyglutamine) repeat in the htt (huntingtin protein). polyglutamine 58-71 huntingtin Homo sapiens 92-102 22178474-3 2012 We describe here the use of very short polyQ repeat lengths in htt N-terminal fragments to slow this disease-associated aggregation. polyglutamine 39-44 huntingtin Homo sapiens 63-66 22178474-0 2012 Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments. polyglutamine 79-92 huntingtin Homo sapiens 104-114 22178474-1 2012 The 17-amino-acid N-terminal segment (htt(NT)) that leads into the polyglutamine (polyQ) segment in the Huntington"s disease protein huntingtin (htt) dramatically increases aggregation rates and changes the aggregation mechanism, compared to a simple polyQ peptide of similar length. polyglutamine 67-80 huntingtin Homo sapiens 38-41 22178474-1 2012 The 17-amino-acid N-terminal segment (htt(NT)) that leads into the polyglutamine (polyQ) segment in the Huntington"s disease protein huntingtin (htt) dramatically increases aggregation rates and changes the aggregation mechanism, compared to a simple polyQ peptide of similar length. polyglutamine 67-80 huntingtin Homo sapiens 133-143 22178474-1 2012 The 17-amino-acid N-terminal segment (htt(NT)) that leads into the polyglutamine (polyQ) segment in the Huntington"s disease protein huntingtin (htt) dramatically increases aggregation rates and changes the aggregation mechanism, compared to a simple polyQ peptide of similar length. polyglutamine 67-80 huntingtin Homo sapiens 145-148 22178474-2 2012 With polyQ segments near or above the pathological repeat length threshold of about 37, aggregation of htt N-terminal fragments is so rapid that it is difficult to tease out mechanistic details. polyglutamine 5-10 huntingtin Homo sapiens 103-106 22178478-3 2012 In this mechanism, the htt(NT) segment forms the alpha-helix-rich core of the oligomers, leaving much of the polyglutamine (polyQ) segment disordered and solvent-exposed. polyglutamine 109-122 huntingtin Homo sapiens 23-26 22178478-3 2012 In this mechanism, the htt(NT) segment forms the alpha-helix-rich core of the oligomers, leaving much of the polyglutamine (polyQ) segment disordered and solvent-exposed. polyglutamine 124-129 huntingtin Homo sapiens 23-26 22178478-8 2012 In the other class, nucleation is actively suppressed by a proline-rich polyQ segment covalently attached to htt(NT). polyglutamine 72-77 huntingtin Homo sapiens 109-112 23339311-1 2012 Huntington"s disease arises from CAG codon-repeat expansions in the Htt gene, which leads to a Htt gene product with an expanded polyglutamine (polyQ) sequence. polyglutamine 129-142 huntingtin Homo sapiens 68-71 22334892-4 2012 HD is caused by an expanded polyglutamine repeat in the huntingtin (Htt) protein that actuates a diverse set of pathogenic mechanisms. polyglutamine 28-41 huntingtin Homo sapiens 56-66 22334892-4 2012 HD is caused by an expanded polyglutamine repeat in the huntingtin (Htt) protein that actuates a diverse set of pathogenic mechanisms. polyglutamine 28-41 huntingtin Homo sapiens 68-71 22110140-1 2012 Huntington disease (HD), a fatal neurodegenerative disorder, is caused by a lengthening of the polyglutamine tract in the huntingtin (Htt) protein. polyglutamine 95-108 huntingtin Homo sapiens 122-132 22110140-1 2012 Huntington disease (HD), a fatal neurodegenerative disorder, is caused by a lengthening of the polyglutamine tract in the huntingtin (Htt) protein. polyglutamine 95-108 huntingtin Homo sapiens 134-137 23560309-2 2012 Despite the disease being caused by dysfunction ofa single gene, expressed as an expanded polyglutamine in the huntingtin protein, there is a major variability in the symptom profile of patients with Huntington"s disease as well as great variability in the neuropathology. polyglutamine 90-103 huntingtin Homo sapiens 111-121 23050151-1 2012 Huntington"s disease is a progressive neurodegenerative disease, caused by a polyglutamine expansion in the huntingtin protein. polyglutamine 77-90 huntingtin Homo sapiens 108-118 23050151-2 2012 A prominent hallmark of the disease is the presence of intracellular aggregates initiated by N-terminal huntingtin fragments containing the polyglutamine repeat, which recruit components of the ubiquitin-proteasome system. polyglutamine 140-153 huntingtin Homo sapiens 104-114 23339311-1 2012 Huntington"s disease arises from CAG codon-repeat expansions in the Htt gene, which leads to a Htt gene product with an expanded polyglutamine (polyQ) sequence. polyglutamine 129-142 huntingtin Homo sapiens 95-98 23339311-1 2012 Huntington"s disease arises from CAG codon-repeat expansions in the Htt gene, which leads to a Htt gene product with an expanded polyglutamine (polyQ) sequence. polyglutamine 144-149 huntingtin Homo sapiens 68-71 23339311-1 2012 Huntington"s disease arises from CAG codon-repeat expansions in the Htt gene, which leads to a Htt gene product with an expanded polyglutamine (polyQ) sequence. polyglutamine 144-149 huntingtin Homo sapiens 95-98 23339311-3 2012 Yet after nearly 20 years since the genetic basis for HD was identified, our knowledge of how polyQ-expanded Htt fragment aggregation relates to disease mechanisms remains fragmentary and controversial. polyglutamine 94-99 huntingtin Homo sapiens 109-112 23339311-6 2012 This review discusses these issues in light of a historic summary of Htt aggregation in the cellular milieu and the intrinsic attributes of polyQ-expanded Htt that lead to aggregation. polyglutamine 140-145 huntingtin Homo sapiens 155-158 23293686-0 2012 Poly-glutamine expanded huntingtin dramatically alters the genome wide binding of HSF1. polyglutamine 0-14 huntingtin Homo sapiens 24-34 22292820-1 2012 Huntington"s disease (HD) is caused by expansion of a polyglutamine repeat in the N-terminal region of huntingtin (htt), a large protein that has been found to interact with a variety of proteins. polyglutamine 54-67 huntingtin Homo sapiens 103-113 22292820-1 2012 Huntington"s disease (HD) is caused by expansion of a polyglutamine repeat in the N-terminal region of huntingtin (htt), a large protein that has been found to interact with a variety of proteins. polyglutamine 54-67 huntingtin Homo sapiens 115-118 23293686-1 2012 In Huntington"s disease (HD), polyglutamine expansions in the huntingtin (Htt) protein cause subtle changes in cellular functions that, over-time, lead to neurodegeneration and death. polyglutamine 30-43 huntingtin Homo sapiens 62-72 23293686-1 2012 In Huntington"s disease (HD), polyglutamine expansions in the huntingtin (Htt) protein cause subtle changes in cellular functions that, over-time, lead to neurodegeneration and death. polyglutamine 30-43 huntingtin Homo sapiens 74-77 23293686-5 2012 However, polyQ-expanded Htt severely blunts the HSF1-mediated stress response. polyglutamine 9-14 huntingtin Homo sapiens 24-27 22536159-3 2012 Fragments of human huntingtin protein having an expanded polyglutamine stretch form aggregates and cause cytotoxicity in yeast cells bearing endogenous QN-rich proteins in the aggregated (prion) form. polyglutamine 57-70 huntingtin Homo sapiens 19-29 22383888-2 2012 The abnormally extended polyglutamine in the HTT protein encoded by the CAG repeats has toxic effects. polyglutamine 24-37 huntingtin Homo sapiens 45-48 21199443-2 2011 HD is caused by a trinucleotide repeat expansion in the HTT gene and a corresponding neurotoxic polyglutamine expansion in the huntingtin protein. polyglutamine 96-109 huntingtin Homo sapiens 56-59 22815947-2 2012 Mutant huntingtin protein (mHtt) contains an expanded polyglutamine repeat region near the N-terminus. polyglutamine 54-67 huntingtin Homo sapiens 7-17 22354228-1 2012 In Huntington"s disease, CAG repeat expansion of the Huntingtin gene produces mutant RNA and mutant protein containing elongated polyglutamine tract, which causes dysfunction and cell death of neurons. polyglutamine 129-142 huntingtin Homo sapiens 53-63 22179319-1 2011 Huntington"s disease is a fatal neurodegenerative disorder caused by an expanded polyglutamine repeat in huntingtin (HTT) protein. polyglutamine 81-94 huntingtin Homo sapiens 105-115 22179319-1 2011 Huntington"s disease is a fatal neurodegenerative disorder caused by an expanded polyglutamine repeat in huntingtin (HTT) protein. polyglutamine 81-94 huntingtin Homo sapiens 117-120 22056561-1 2011 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 123-128 huntingtin Homo sapiens 153-156 23071649-10 2012 Expansion of the polyQ tract in Htt-552 impaired its uptake and degradation by lysosomes. polyglutamine 17-22 huntingtin Homo sapiens 32-35 22276192-1 2012 Impairments in mitochondria and transcription are important factors in the pathogenesis of Huntington disease (HD), a neurodegenerative disease caused by a polyglutamine expansion in the huntingtin protein. polyglutamine 156-169 huntingtin Homo sapiens 187-197 21984825-5 2011 Live imaging of cells expressing a fragment of huntingtin (httExon1) with a poly(Q) expansion shows increased ROS production preceding cell death. polyglutamine 76-83 huntingtin Homo sapiens 47-57 22056561-1 2011 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 108-121 huntingtin Homo sapiens 141-151 22056561-1 2011 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 108-121 huntingtin Homo sapiens 153-156 22056561-1 2011 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 123-128 huntingtin Homo sapiens 141-151 21199443-2 2011 HD is caused by a trinucleotide repeat expansion in the HTT gene and a corresponding neurotoxic polyglutamine expansion in the huntingtin protein. polyglutamine 96-109 huntingtin Homo sapiens 127-137 22158031-1 2011 Huntington"s disease (HD) is caused by an expansion of CAG triplets at the 5" end of the HD gene, which encodes a pathologically elongated polyglutamine stretch near the N-terminus of huntingtin. polyglutamine 139-152 huntingtin Homo sapiens 184-194 21985782-1 2011 Huntington disease (HD) is a dominantly inherited neurodegenerative disorder that is caused by a mutant huntingtin (HTT) gene encoding a version of the Htt protein with an expanded polyglutamine stretch. polyglutamine 181-194 huntingtin Homo sapiens 104-114 21360185-2 2011 Expansion of polyglutamine tracts in htt results in neurodegenerative Huntington disease. polyglutamine 13-26 huntingtin Homo sapiens 37-40 21985782-1 2011 Huntington disease (HD) is a dominantly inherited neurodegenerative disorder that is caused by a mutant huntingtin (HTT) gene encoding a version of the Htt protein with an expanded polyglutamine stretch. polyglutamine 181-194 huntingtin Homo sapiens 116-119 21985782-1 2011 Huntington disease (HD) is a dominantly inherited neurodegenerative disorder that is caused by a mutant huntingtin (HTT) gene encoding a version of the Htt protein with an expanded polyglutamine stretch. polyglutamine 181-194 huntingtin Homo sapiens 152-155 21519949-2 2011 The elongated polyglutamine (polyQ) stretch in the N-terminal region of htt leads to dysfunctional and degenerative events in neurons and peripheral tissues. polyglutamine 14-27 huntingtin Homo sapiens 72-75 21519949-2 2011 The elongated polyglutamine (polyQ) stretch in the N-terminal region of htt leads to dysfunctional and degenerative events in neurons and peripheral tissues. polyglutamine 29-34 huntingtin Homo sapiens 72-75 21775503-2 2011 It was suggested that expanded polyglutamine chains (polyQ) of mutant huntingtin are cross-linked to other proteins such as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). polyglutamine 31-44 huntingtin Homo sapiens 70-80 22017874-6 2011 Furthermore, CK2 overexpression or phosphatase inhibition reduces the formation of inclusion bodies of the polyglutamine-expanded huntingtin exon1 fragment in a p62-dependent manner. polyglutamine 107-120 huntingtin Homo sapiens 130-140 21910495-1 2011 Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the N-terminal fragment of the Huntingtin (Htt) protein. polyglutamine 65-78 huntingtin Homo sapiens 131-141 21910495-1 2011 Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the N-terminal fragment of the Huntingtin (Htt) protein. polyglutamine 65-78 huntingtin Homo sapiens 143-146 21910495-1 2011 Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the N-terminal fragment of the Huntingtin (Htt) protein. polyglutamine 80-85 huntingtin Homo sapiens 131-141 21910495-1 2011 Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in the N-terminal fragment of the Huntingtin (Htt) protein. polyglutamine 80-85 huntingtin Homo sapiens 143-146 21910495-3 2011 We performed all-atom replica exchange molecular dynamics to investigate the structures of Htt N-terminal parts with polyQ tracts of nonpathogenic and pathogenic lengths. polyglutamine 117-122 huntingtin Homo sapiens 91-94 21910495-8 2011 The predicted structure of the native N-terminal fragment agrees with the X-ray structure of the Htt first exon containing polyQ(17). polyglutamine 123-128 huntingtin Homo sapiens 97-100 21685499-1 2011 Huntingtin (Htt) is a protein with a polyglutamine stretch in the N-terminus and expansion of the polyglutamine stretch causes Huntington"s disease (HD). polyglutamine 37-50 huntingtin Homo sapiens 0-10 21465263-1 2011 Huntington"s disease (HD) occurs through an expansion of the trinucleotide repeat in the HD gene resulting in the lengthening of the polyglutamine stretch within the N terminus of the protein, huntingtin (Htt). polyglutamine 133-146 huntingtin Homo sapiens 193-203 21465263-1 2011 Huntington"s disease (HD) occurs through an expansion of the trinucleotide repeat in the HD gene resulting in the lengthening of the polyglutamine stretch within the N terminus of the protein, huntingtin (Htt). polyglutamine 133-146 huntingtin Homo sapiens 205-208 21854390-2 2011 This expansion produces a mutant form of the huntingtin protein, which contains an elongated polyglutamine stretch at its amino-terminus. polyglutamine 93-106 huntingtin Homo sapiens 45-55 21685499-1 2011 Huntingtin (Htt) is a protein with a polyglutamine stretch in the N-terminus and expansion of the polyglutamine stretch causes Huntington"s disease (HD). polyglutamine 37-50 huntingtin Homo sapiens 12-15 21685499-1 2011 Huntingtin (Htt) is a protein with a polyglutamine stretch in the N-terminus and expansion of the polyglutamine stretch causes Huntington"s disease (HD). polyglutamine 98-111 huntingtin Homo sapiens 0-10 21685499-1 2011 Huntingtin (Htt) is a protein with a polyglutamine stretch in the N-terminus and expansion of the polyglutamine stretch causes Huntington"s disease (HD). polyglutamine 98-111 huntingtin Homo sapiens 12-15 21971961-3 2011 The disorder is caused by an expanded cystosine adenine guanine (CAG) tri-nucleotide repeat encoding polyglutamine (polyQ) in the first exon of the Huntingtin gene. polyglutamine 101-114 huntingtin Homo sapiens 148-158 21971961-3 2011 The disorder is caused by an expanded cystosine adenine guanine (CAG) tri-nucleotide repeat encoding polyglutamine (polyQ) in the first exon of the Huntingtin gene. polyglutamine 116-121 huntingtin Homo sapiens 148-158 21791172-1 2011 The huntingtin (htt) mutation causes a polyglutamine expansion in the N-terminal region of protein. polyglutamine 39-52 huntingtin Homo sapiens 4-14 21894212-3 2011 Studies have demonstrated that Huntington disease (HD), a progressive and fatal neurodegenerative disorder resulting from polyglutamine expansion in the huntingtin protein, is associated with changes in cellular cholesterol metabolism. polyglutamine 122-135 huntingtin Homo sapiens 153-163 21116768-1 2011 Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine expansion near the N-terminus of huntingtin. polyglutamine 70-83 huntingtin Homo sapiens 117-127 21791172-1 2011 The huntingtin (htt) mutation causes a polyglutamine expansion in the N-terminal region of protein. polyglutamine 39-52 huntingtin Homo sapiens 16-19 21518730-1 2011 Huntington"s disease (HD) is caused by the expansion mutation above a length threshold of a polyglutamine (polyQ) stretch in the huntingtin (Htt) protein. polyglutamine 92-105 huntingtin Homo sapiens 129-139 21454471-1 2011 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of polyglutamines in the first exon of huntingtin (HTT), which confers aggregation-promoting properties to amino-terminal fragments of the protein (N-HTT). polyglutamine 82-96 huntingtin Homo sapiens 118-128 21454471-1 2011 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of polyglutamines in the first exon of huntingtin (HTT), which confers aggregation-promoting properties to amino-terminal fragments of the protein (N-HTT). polyglutamine 82-96 huntingtin Homo sapiens 130-133 21454471-1 2011 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of polyglutamines in the first exon of huntingtin (HTT), which confers aggregation-promoting properties to amino-terminal fragments of the protein (N-HTT). polyglutamine 82-96 huntingtin Homo sapiens 229-232 21566141-0 2011 Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA). polyglutamine 17-30 huntingtin Homo sapiens 40-50 21566141-2 2011 The polyglutamine (polyQ) expansion of huntingtin (Htt) is implicated in the pathogenesis of HD via interaction with an RNA splicing factor, Htt yeast two-hybrid protein A/forming-binding protein 11 (HYPA/FBP11). polyglutamine 4-17 huntingtin Homo sapiens 39-49 21566141-2 2011 The polyglutamine (polyQ) expansion of huntingtin (Htt) is implicated in the pathogenesis of HD via interaction with an RNA splicing factor, Htt yeast two-hybrid protein A/forming-binding protein 11 (HYPA/FBP11). polyglutamine 4-17 huntingtin Homo sapiens 51-54 21566141-2 2011 The polyglutamine (polyQ) expansion of huntingtin (Htt) is implicated in the pathogenesis of HD via interaction with an RNA splicing factor, Htt yeast two-hybrid protein A/forming-binding protein 11 (HYPA/FBP11). polyglutamine 4-17 huntingtin Homo sapiens 141-144 21566141-2 2011 The polyglutamine (polyQ) expansion of huntingtin (Htt) is implicated in the pathogenesis of HD via interaction with an RNA splicing factor, Htt yeast two-hybrid protein A/forming-binding protein 11 (HYPA/FBP11). polyglutamine 19-24 huntingtin Homo sapiens 39-49 21566141-2 2011 The polyglutamine (polyQ) expansion of huntingtin (Htt) is implicated in the pathogenesis of HD via interaction with an RNA splicing factor, Htt yeast two-hybrid protein A/forming-binding protein 11 (HYPA/FBP11). polyglutamine 19-24 huntingtin Homo sapiens 51-54 21566141-2 2011 The polyglutamine (polyQ) expansion of huntingtin (Htt) is implicated in the pathogenesis of HD via interaction with an RNA splicing factor, Htt yeast two-hybrid protein A/forming-binding protein 11 (HYPA/FBP11). polyglutamine 19-24 huntingtin Homo sapiens 141-144 21566141-6 2011 The polyQ-expanded Htt sequesters HYPA to the cytosolic location and then significantly reduces the efficiency of pre-mRNA splicing. polyglutamine 4-9 huntingtin Homo sapiens 19-22 21518730-1 2011 Huntington"s disease (HD) is caused by the expansion mutation above a length threshold of a polyglutamine (polyQ) stretch in the huntingtin (Htt) protein. polyglutamine 92-105 huntingtin Homo sapiens 141-144 21518730-1 2011 Huntington"s disease (HD) is caused by the expansion mutation above a length threshold of a polyglutamine (polyQ) stretch in the huntingtin (Htt) protein. polyglutamine 107-112 huntingtin Homo sapiens 129-139 21518730-1 2011 Huntington"s disease (HD) is caused by the expansion mutation above a length threshold of a polyglutamine (polyQ) stretch in the huntingtin (Htt) protein. polyglutamine 107-112 huntingtin Homo sapiens 141-144 21441583-2 2011 The mutation responsible for HD leads to an abnormally long polyglutamine (polyQ) expansion in the huntingtin (Htt) protein, which confers one or more toxic functions to mutant Htt leading to neurodegeneration. polyglutamine 60-73 huntingtin Homo sapiens 99-109 21210219-2 2011 HD is caused by polyglutamine (polyQ) expansion in the amino-terminal region of a protein huntingtin (Htt) and primarily affects medium spiny striatal neurons (MSN). polyglutamine 16-29 huntingtin Homo sapiens 90-100 21210219-2 2011 HD is caused by polyglutamine (polyQ) expansion in the amino-terminal region of a protein huntingtin (Htt) and primarily affects medium spiny striatal neurons (MSN). polyglutamine 16-29 huntingtin Homo sapiens 102-105 21210219-2 2011 HD is caused by polyglutamine (polyQ) expansion in the amino-terminal region of a protein huntingtin (Htt) and primarily affects medium spiny striatal neurons (MSN). polyglutamine 31-36 huntingtin Homo sapiens 90-100 21210219-2 2011 HD is caused by polyglutamine (polyQ) expansion in the amino-terminal region of a protein huntingtin (Htt) and primarily affects medium spiny striatal neurons (MSN). polyglutamine 31-36 huntingtin Homo sapiens 102-105 21441583-2 2011 The mutation responsible for HD leads to an abnormally long polyglutamine (polyQ) expansion in the huntingtin (Htt) protein, which confers one or more toxic functions to mutant Htt leading to neurodegeneration. polyglutamine 60-73 huntingtin Homo sapiens 111-114 21441583-2 2011 The mutation responsible for HD leads to an abnormally long polyglutamine (polyQ) expansion in the huntingtin (Htt) protein, which confers one or more toxic functions to mutant Htt leading to neurodegeneration. polyglutamine 60-73 huntingtin Homo sapiens 177-180 21441583-2 2011 The mutation responsible for HD leads to an abnormally long polyglutamine (polyQ) expansion in the huntingtin (Htt) protein, which confers one or more toxic functions to mutant Htt leading to neurodegeneration. polyglutamine 75-80 huntingtin Homo sapiens 99-109 21441583-2 2011 The mutation responsible for HD leads to an abnormally long polyglutamine (polyQ) expansion in the huntingtin (Htt) protein, which confers one or more toxic functions to mutant Htt leading to neurodegeneration. polyglutamine 75-80 huntingtin Homo sapiens 111-114 21441583-2 2011 The mutation responsible for HD leads to an abnormally long polyglutamine (polyQ) expansion in the huntingtin (Htt) protein, which confers one or more toxic functions to mutant Htt leading to neurodegeneration. polyglutamine 75-80 huntingtin Homo sapiens 177-180 21441583-3 2011 The polyQ expansion makes Htt prone to aggregate and accumulate, and manipulations that mitigate protein misfolding or facilitate the clearance of misfolded proteins tend to slow disease progression in HD models. polyglutamine 4-9 huntingtin Homo sapiens 26-29 21294586-1 2011 Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion near the N-terminus of huntingtin. polyglutamine 65-78 huntingtin Homo sapiens 120-130 21674644-2 2011 The mutation results in the pathological expansion of the polyQ stretch that is normally present within the N-terminal region of Htt. polyglutamine 58-63 huntingtin Homo sapiens 129-132 21294586-1 2011 Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion near the N-terminus of huntingtin. polyglutamine 80-85 huntingtin Homo sapiens 120-130 21552328-1 2011 Huntingtin is a large HEAT repeat protein first identified in humans, where a polyglutamine tract expansion near the amino terminus causes a gain-of-function mechanism that leads to selective neuronal loss in Huntington"s disease (HD). polyglutamine 78-91 huntingtin Homo sapiens 0-10 21539755-2 2011 The underlying molecular genetic defect is an expanded trinucleotide (CAG)n repeat encoding a polyglutamine stretch in the N-terminus of the huntingtin protein. polyglutamine 94-107 huntingtin Homo sapiens 141-151 21209075-1 2011 Huntington disease results from an expanded polyglutamine region in the N terminus of the huntingtin protein. polyglutamine 44-57 huntingtin Homo sapiens 90-100 21209075-3 2011 Structural information is minimal, though it is believed that mutant huntingtin polyglutamine adopts beta structure upon conversion to a toxic form. polyglutamine 80-93 huntingtin Homo sapiens 69-79 21304940-10 2011 Similar large PML-NBs, termed clastosomes, sequester aberrant polyglutamine (polyQ) proteins, such as Huntingtin (Htt), in several neurodegenerative disorders. polyglutamine 62-75 huntingtin Homo sapiens 102-112 21187152-1 2011 Huntington disease (HD), a neurodegenerative disorder, is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats located near the N-terminus of the huntingtin (htt) protein. polyglutamine 100-113 huntingtin Homo sapiens 165-175 21187152-1 2011 Huntington disease (HD), a neurodegenerative disorder, is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats located near the N-terminus of the huntingtin (htt) protein. polyglutamine 100-113 huntingtin Homo sapiens 177-180 21187152-2 2011 The expansion of the polyQ domain results in the ordered assembly of htt fragments into fibrillar aggregates that are the main constituents of inclusion bodies, which are a hallmark of the disease. polyglutamine 21-26 huntingtin Homo sapiens 69-72 21195182-2 2011 For example, expansion of the polyQ tract (>40 repeats) in huntingtin (htt) proteins leads to Huntington disease, while polyQ-expanded ataxins cause several types of ataxias. polyglutamine 30-35 huntingtin Homo sapiens 59-69 21195182-2 2011 For example, expansion of the polyQ tract (>40 repeats) in huntingtin (htt) proteins leads to Huntington disease, while polyQ-expanded ataxins cause several types of ataxias. polyglutamine 30-35 huntingtin Homo sapiens 71-74 21304940-10 2011 Similar large PML-NBs, termed clastosomes, sequester aberrant polyglutamine (polyQ) proteins, such as Huntingtin (Htt), in several neurodegenerative disorders. polyglutamine 62-75 huntingtin Homo sapiens 114-117 21189122-2 2011 Mutations leading to expansion of a poly-glutamine track in Huntingtin cause HD, and trigger its misfolding and aggregation. polyglutamine 36-50 huntingtin Homo sapiens 60-70 21211002-1 2011 BACKGROUND: Huntington disease (HD) is caused by a polyglutamine expansion of more than 35 units in the huntingtin protein. polyglutamine 51-64 huntingtin Homo sapiens 104-114 21285520-1 2011 Huntington disease (HD) is a dominantly inherited neurodegenerative disorder that results from expansion of the polyglutamine repeat in the huntingtin (HTT) gene. polyglutamine 112-125 huntingtin Homo sapiens 140-150 21285520-1 2011 Huntington disease (HD) is a dominantly inherited neurodegenerative disorder that results from expansion of the polyglutamine repeat in the huntingtin (HTT) gene. polyglutamine 112-125 huntingtin Homo sapiens 152-155 21153060-2 2011 A polyglutamine expansion in the amino-terminal region of the huntingtin (htt) protein is the genetic cause of HD. polyglutamine 2-15 huntingtin Homo sapiens 62-72 21153060-2 2011 A polyglutamine expansion in the amino-terminal region of the huntingtin (htt) protein is the genetic cause of HD. polyglutamine 2-15 huntingtin Homo sapiens 74-77 21882411-13 2011 HD is a dominantly inherited disease caused by expanded polyglutamines (polyQs) in the huntingtin (htt) protein (Figure 6.1) and is clinically characterized by cortical and striatal degeneration accompanied by motor, cognitive, and neuropsychiatric symptoms (Walker, 2007). polyglutamine 56-70 huntingtin Homo sapiens 87-97 21882411-13 2011 HD is a dominantly inherited disease caused by expanded polyglutamines (polyQs) in the huntingtin (htt) protein (Figure 6.1) and is clinically characterized by cortical and striatal degeneration accompanied by motor, cognitive, and neuropsychiatric symptoms (Walker, 2007). polyglutamine 56-70 huntingtin Homo sapiens 99-102 21882411-14 2011 The toxic effects of polyQ-expanded htt forms and genetic modifiers of cytotoxicity are being studied in several cell systems and in model organisms, including yeast, nematodes, flies, and rodents (Levine et al., 2004; Rubinsztein, 2002; Sipione and Cattaneo, 2001). polyglutamine 21-26 huntingtin Homo sapiens 36-39 21882411-15 2011 Thus, a large amount of knowledge is being accumulated on the roles of normal htt and the effects of polyQ-expanded htt at the neuronal cell level. polyglutamine 101-106 huntingtin Homo sapiens 116-119 21496571-2 2011 The abnormal elongation of the CAG increases the polyglutamine stretch of huntingtin, which becomes proportionally toxic. polyglutamine 49-62 huntingtin Homo sapiens 74-84 21056115-2 2011 The disease is caused by pathological CAG-triplet repeat extension(s), encoding polyglutamines, within the gene product, huntingtin. polyglutamine 80-94 huntingtin Homo sapiens 121-131 21056115-4 2011 Mutant huntingtin, containing pathologically extended polyglutamines causes the earliest and most dramatic neuropathologic changes in the neostriatum and cerebral cortex. polyglutamine 54-68 huntingtin Homo sapiens 7-17 21056115-5 2011 Extended polyglutamines confer structural conformational changes to huntingtin, which gains novel properties, resulting in aberrant interactions with multiple cellular components. polyglutamine 9-23 huntingtin Homo sapiens 68-78 21907094-2 2011 The basis of HD is a CAG repeat expansion to >35 CAG in a gene that codes for a ubiquitous protein known as huntingtin, resulting in an expanded N-terminal polyglutamine tract. polyglutamine 156-169 huntingtin Homo sapiens 108-118 21909428-7 2011 This antisense oligonucleotide is not only a promising therapeutic tool to reduce mutant huntingtin levels in Huntington"s disease but our results in spinocerebellar ataxia and dentatorubral-pallidoluysian atrophy cells suggest that this could also be applicable to other polyglutamine expansion disorders as well. polyglutamine 272-285 huntingtin Homo sapiens 89-99 20644995-1 2010 Glutamate excitotoxicity is thought to play an important role in Huntington"s disease (HD), which is caused by a polyglutamine expansion in the HD protein huntingtin (htt). polyglutamine 113-126 huntingtin Homo sapiens 155-165 21209946-6 2010 Here, we describe two complementary biophysical fluorescence microscopy techniques to directly detect soluble polyglutamine oligomers (using Htt exon 1 or Htt(ex1)) and monitor their fates in live cells. polyglutamine 110-123 huntingtin Homo sapiens 141-144 21209946-6 2010 Here, we describe two complementary biophysical fluorescence microscopy techniques to directly detect soluble polyglutamine oligomers (using Htt exon 1 or Htt(ex1)) and monitor their fates in live cells. polyglutamine 110-123 huntingtin Homo sapiens 155-158 20942784-1 2010 Huntington"s disease (HD) is an adult onset neurodegenerative disease caused by a polyglutamine expansion in the huntingtin protein. polyglutamine 82-95 huntingtin Homo sapiens 113-123 20708032-2 2010 An expanded CAG repeat sequence in the huntingtin gene leads to a polyglutamine expansion in the expressed protein, resulting in complex dysfunctions including cellular excitotoxicity and transcriptional dysregulation. polyglutamine 66-79 huntingtin Homo sapiens 39-49 21069748-1 2010 Huntington"s disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. polyglutamine 75-88 huntingtin Homo sapiens 106-116 21069748-1 2010 Huntington"s disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. polyglutamine 75-88 huntingtin Homo sapiens 118-121 21117121-1 2010 Polyglutamine expansions in huntingtin (Htt) are known to cause the profound neurodegenerative disorder, Huntington"s disease (HD). polyglutamine 0-13 huntingtin Homo sapiens 28-38 21117121-1 2010 Polyglutamine expansions in huntingtin (Htt) are known to cause the profound neurodegenerative disorder, Huntington"s disease (HD). polyglutamine 0-13 huntingtin Homo sapiens 40-43 20739295-1 2010 Expansion of a polyglutamine (polyQ) tract in the Huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited neurodegenerative disorder. polyglutamine 15-28 huntingtin Homo sapiens 50-60 20739295-1 2010 Expansion of a polyglutamine (polyQ) tract in the Huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited neurodegenerative disorder. polyglutamine 15-28 huntingtin Homo sapiens 62-65 20739295-1 2010 Expansion of a polyglutamine (polyQ) tract in the Huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited neurodegenerative disorder. polyglutamine 30-35 huntingtin Homo sapiens 50-60 20739295-1 2010 Expansion of a polyglutamine (polyQ) tract in the Huntingtin (Htt) protein causes Huntington"s disease (HD), a fatal inherited neurodegenerative disorder. polyglutamine 30-35 huntingtin Homo sapiens 62-65 20739295-6 2010 We show that this novel function of Htt is impaired by the polyQ expansion and thus may contribute to the etiology of HD. polyglutamine 59-64 huntingtin Homo sapiens 36-39 20710011-9 2010 CONCLUSION: These findings suggest sympathetic hyperactivity as an underlying mechanism of increased energy expenditure in HD, as well as peripheral polyglutamine length dependent interference of mutant huntingtin with insulin signalling that may become clinically relevant in carriers of mutations with large CAG repeat sizes. polyglutamine 149-162 huntingtin Homo sapiens 203-213 20644995-1 2010 Glutamate excitotoxicity is thought to play an important role in Huntington"s disease (HD), which is caused by a polyglutamine expansion in the HD protein huntingtin (htt). polyglutamine 113-126 huntingtin Homo sapiens 167-170 20697744-1 2010 Huntington"s disease (HD) is caused by an expansion of a polyglutamine repeat of more than 35 units in the huntingtin protein. polyglutamine 57-70 huntingtin Homo sapiens 107-117 20685997-1 2010 An expanded polyglutamine (polyQ) stretch in the protein huntingtin (htt) induces self-aggregation into inclusion bodies (IBs) and causes Huntington"s disease (HD). polyglutamine 12-25 huntingtin Homo sapiens 57-67 20665636-1 2010 Caused by a polyglutamine expansion in the huntingtin protein, Huntington"s disease leads to striatal degeneration via the transcriptional dysregulation of a number of genes, including those involved in mitochondrial biogenesis. polyglutamine 12-25 huntingtin Homo sapiens 43-53 21977007-1 2010 Huntington"s disease (HD) is a noncurable and progressive autosomal-dominant neurodegenerative disorder that results from a polyglutamine expansion in the amino-terminal region of the huntingtin protein. polyglutamine 124-137 huntingtin Homo sapiens 184-194 20583779-1 2010 Polyglutamine expansion in the exon 1 domain of huntingtin leads to aggregation into beta-sheet-rich insoluble aggregates associated with Huntington"s disease. polyglutamine 0-13 huntingtin Homo sapiens 48-58 20685997-1 2010 An expanded polyglutamine (polyQ) stretch in the protein huntingtin (htt) induces self-aggregation into inclusion bodies (IBs) and causes Huntington"s disease (HD). polyglutamine 12-25 huntingtin Homo sapiens 69-72 20685997-1 2010 An expanded polyglutamine (polyQ) stretch in the protein huntingtin (htt) induces self-aggregation into inclusion bodies (IBs) and causes Huntington"s disease (HD). polyglutamine 27-32 huntingtin Homo sapiens 57-67 20685997-1 2010 An expanded polyglutamine (polyQ) stretch in the protein huntingtin (htt) induces self-aggregation into inclusion bodies (IBs) and causes Huntington"s disease (HD). polyglutamine 27-32 huntingtin Homo sapiens 69-72 20581077-1 2010 Huntington"s disease (HD) is a fatal neurodegenerative disease characterized by progressive cognitive, behavioral, and motor deficits and caused by expansion of a polyglutamine repeat in the Huntingtin protein (Htt). polyglutamine 163-176 huntingtin Homo sapiens 191-201 20581077-1 2010 Huntington"s disease (HD) is a fatal neurodegenerative disease characterized by progressive cognitive, behavioral, and motor deficits and caused by expansion of a polyglutamine repeat in the Huntingtin protein (Htt). polyglutamine 163-176 huntingtin Homo sapiens 211-214 20670829-4 2010 To accomplish this, we designed a high-throughput western blot-based screen to examine the generation of the smallest N-terminal polyglutamine-containing Htt fragment. polyglutamine 129-142 huntingtin Homo sapiens 154-157 20552561-4 2010 It has been demonstrated in various animal models that only the expression of exon 1 huntingtin, a 67-amino acid-long polypeptide plus a variable poly-Q stretch, is sufficient to cause full HD-like pathology. polyglutamine 146-152 huntingtin Homo sapiens 85-95 20444706-1 2010 Huntington disease is caused by expanded polyglutamine sequences in huntingtin, which procures its aggregation into intracellular inclusion bodies (IBs). polyglutamine 41-54 huntingtin Homo sapiens 68-78 20444706-5 2010 Purified polyglutamine-expanded pathogenic huntingtin formed elongated monomers (2.4 S) that evolved into a heterogeneous aggregate population of increasing size over time (100-6,000 S). polyglutamine 9-22 huntingtin Homo sapiens 43-53 20403078-1 2010 Polyglutamine expansion mutation in huntingtin causes Huntington"s disease (HD). polyglutamine 0-13 huntingtin Homo sapiens 36-46 20552561-6 2010 Here, we describe the synthesis of a 109-amino acid-long exon 1 huntingtin peptide including a poly-Q stretch of 42 glutamines. polyglutamine 95-101 huntingtin Homo sapiens 64-74 20552561-8 2010 We also synthesized a nonpathogenic version of exon 1 huntingtin (90-amino acid long including a poly-Q stretch of 23 glutamine residues) using the same strategy. polyglutamine 97-103 huntingtin Homo sapiens 54-64 20220138-0 2010 Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. polyglutamine 48-61 huntingtin Homo sapiens 7-17 20232225-2 2010 We show that the expression of mutant huntingtin proteins with extended polyglutamine repeats differentially affected endoplasmic reticulum signaling cascades linked to the inositol-requiring enzyme-1 (IRE1) pathway. polyglutamine 72-85 huntingtin Homo sapiens 38-48 20461451-6 2010 In affected individuals, the mutant HD protein (Huntingtin, mHtt) thus contains an extended polyglutamine repeat. polyglutamine 92-105 huntingtin Homo sapiens 48-58 20236390-1 2010 Abnormal expansion of a polyglutamine tract in huntingtin (Htt) protein results in Huntington"s disease (HD), an autosomal dominant neurodegenerative disorder involving progressive loss of motor and cognitive function. polyglutamine 24-37 huntingtin Homo sapiens 47-57 20236390-1 2010 Abnormal expansion of a polyglutamine tract in huntingtin (Htt) protein results in Huntington"s disease (HD), an autosomal dominant neurodegenerative disorder involving progressive loss of motor and cognitive function. polyglutamine 24-37 huntingtin Homo sapiens 59-62 20236390-2 2010 Contrasting with the ubiquitous tissue expression of polyglutamine-expanded Htt, HD pathology is characterized by the increased vulnerability of specific neuronal populations within the striatum and the cerebral cortex. polyglutamine 53-66 huntingtin Homo sapiens 76-79 20236390-3 2010 Morphological, biochemical, and functional characteristics of neurons affected in HD that might render these cells more vulnerable to the toxic effects of polyglutamine-Htt are covered in this review. polyglutamine 155-168 huntingtin Homo sapiens 169-172 20154343-7 2010 Microinjection of a full-length human HTT cDNA containing 73 polyglutamine repeats under the control of the human promotor resulted in six transgenic founders varying in copy number of the transgene. polyglutamine 61-74 huntingtin Homo sapiens 38-41 20220138-1 2010 Huntington disease (HD) is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats in the huntingtin (htt) protein, resulting in accumulation of inclusion bodies containing fibrillar deposits of mutant htt fragments. polyglutamine 69-82 huntingtin Homo sapiens 106-116 20220138-1 2010 Huntington disease (HD) is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats in the huntingtin (htt) protein, resulting in accumulation of inclusion bodies containing fibrillar deposits of mutant htt fragments. polyglutamine 69-82 huntingtin Homo sapiens 118-121 20220138-1 2010 Huntington disease (HD) is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats in the huntingtin (htt) protein, resulting in accumulation of inclusion bodies containing fibrillar deposits of mutant htt fragments. polyglutamine 84-89 huntingtin Homo sapiens 106-116 20220138-1 2010 Huntington disease (HD) is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats in the huntingtin (htt) protein, resulting in accumulation of inclusion bodies containing fibrillar deposits of mutant htt fragments. polyglutamine 84-89 huntingtin Homo sapiens 118-121 20220138-1 2010 Huntington disease (HD) is caused by an expansion of more than 35-40 polyglutamine (polyQ) repeats in the huntingtin (htt) protein, resulting in accumulation of inclusion bodies containing fibrillar deposits of mutant htt fragments. polyglutamine 84-89 huntingtin Homo sapiens 218-221 20154145-8 2010 Knockdown of HYPK or hNAA10 resulted in increased aggregation of an Htt-enhanced green fluorescent protein (Htt-EGFP) fusion with expanded polyglutamine stretches, suggesting that both HYPK and NatA prevent Htt aggregation. polyglutamine 139-152 huntingtin Homo sapiens 68-71 20442863-0 2010 Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences. polyglutamine 0-13 huntingtin Homo sapiens 36-46 20442863-1 2010 Polyglutamine (polyQ) expansion in exon1 (XN1) of the huntingtin protein is linked to Huntington"s disease. polyglutamine 0-13 huntingtin Homo sapiens 54-64 20442863-1 2010 Polyglutamine (polyQ) expansion in exon1 (XN1) of the huntingtin protein is linked to Huntington"s disease. polyglutamine 15-20 huntingtin Homo sapiens 54-64 20298208-1 2010 HD (Huntington"s disease) is produced by the expression of mutant forms of the protein htt (huntingtin) containing a pathologically expanded poly-glutamine repeat. polyglutamine 141-155 huntingtin Homo sapiens 87-90 20298208-1 2010 HD (Huntington"s disease) is produced by the expression of mutant forms of the protein htt (huntingtin) containing a pathologically expanded poly-glutamine repeat. polyglutamine 141-155 huntingtin Homo sapiens 92-102 20298220-1 2010 HD (Huntington"s disease) is caused by a polyQ (polyglutamine) expansion in the huntingtin protein, which leads to protein misfolding and aggregation of this protein. polyglutamine 41-46 huntingtin Homo sapiens 80-90 20298220-1 2010 HD (Huntington"s disease) is caused by a polyQ (polyglutamine) expansion in the huntingtin protein, which leads to protein misfolding and aggregation of this protein. polyglutamine 48-61 huntingtin Homo sapiens 80-90 20298220-4 2010 We have demonstrated that in vitro copper accelerates the fibrillization of an N-terminal fragment of huntingtin with an expanded polyQ stretch (httExon1). polyglutamine 130-135 huntingtin Homo sapiens 102-112 20154145-8 2010 Knockdown of HYPK or hNAA10 resulted in increased aggregation of an Htt-enhanced green fluorescent protein (Htt-EGFP) fusion with expanded polyglutamine stretches, suggesting that both HYPK and NatA prevent Htt aggregation. polyglutamine 139-152 huntingtin Homo sapiens 108-111 20154145-8 2010 Knockdown of HYPK or hNAA10 resulted in increased aggregation of an Htt-enhanced green fluorescent protein (Htt-EGFP) fusion with expanded polyglutamine stretches, suggesting that both HYPK and NatA prevent Htt aggregation. polyglutamine 139-152 huntingtin Homo sapiens 108-111 20237277-1 2010 Huntington"s disease (HD) is a neurodegenerative disorder caused by the expansion of a polyglutamine stretch in the protein huntingtin (Htt). polyglutamine 87-100 huntingtin Homo sapiens 124-134 20237277-1 2010 Huntington"s disease (HD) is a neurodegenerative disorder caused by the expansion of a polyglutamine stretch in the protein huntingtin (Htt). polyglutamine 87-100 huntingtin Homo sapiens 136-139 19394403-1 2010 The neurodegenerative disease Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the protein huntingtin (htt). polyglutamine 81-94 huntingtin Homo sapiens 124-134 19969308-1 2010 Huntington"s disease is caused by polyglutamine-expanded mutant huntingtin (muhtt), an aggregation-prone protein. polyglutamine 34-47 huntingtin Homo sapiens 64-74 20026071-0 2010 Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. polyglutamine 14-27 huntingtin Homo sapiens 83-93 20026071-3 2010 We report results from atomistic simulations and circular dichroism experiments that quantify the effect of the N-terminal 17-residue (Nt17) segment of the huntingtin protein on polyglutamine conformations and intermolecular interactions. polyglutamine 178-191 huntingtin Homo sapiens 156-166 19933700-1 2010 Huntington"s disease (HD) is caused by expansion of the polymorphic polyglutamine segment in the huntingtin protein. polyglutamine 68-81 huntingtin Homo sapiens 97-107 19933700-6 2010 Supporting a direct stimulatory role, full-length recombinant huntingtin significantly increased the histone H3K27 tri-methylase activity of reconstituted PRC2 in vitro, and structure-function analysis demonstrated that the polyglutamine region augmented full-length huntingtin PRC2 stimulation, both in Hdh(Q111) EBs and in vitro, with reconstituted PRC2. polyglutamine 224-237 huntingtin Homo sapiens 62-72 19933700-6 2010 Supporting a direct stimulatory role, full-length recombinant huntingtin significantly increased the histone H3K27 tri-methylase activity of reconstituted PRC2 in vitro, and structure-function analysis demonstrated that the polyglutamine region augmented full-length huntingtin PRC2 stimulation, both in Hdh(Q111) EBs and in vitro, with reconstituted PRC2. polyglutamine 224-237 huntingtin Homo sapiens 267-277 19933700-7 2010 Knowledge of full-length huntingtin"s alpha-helical organization and role as a facilitator of the multi-subunit PRC2 complex provides a novel starting point for studying PRC2 regulation, implicates this chromatin repressive complex in a neurodegenerative disorder and sets the stage for further study of huntingtin"s molecular function and the impact of its modulatory polyglutamine region. polyglutamine 369-382 huntingtin Homo sapiens 25-35 19394403-1 2010 The neurodegenerative disease Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the protein huntingtin (htt). polyglutamine 81-94 huntingtin Homo sapiens 136-139 19394403-1 2010 The neurodegenerative disease Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the protein huntingtin (htt). polyglutamine 96-101 huntingtin Homo sapiens 124-134 19394403-1 2010 The neurodegenerative disease Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the protein huntingtin (htt). polyglutamine 96-101 huntingtin Homo sapiens 136-139 20140226-4 2010 Sequences that flank the polyglutamine tract of AR and Htt might influence protein aggregation and toxicity through protein-protein interactions, but this has not been studied in detail. polyglutamine 25-38 huntingtin Homo sapiens 55-58 20140226-7 2010 Deletion of these actin-binding regions renders the polyglutamine-expanded forms of ARN127 and Htt exon 1 less aggregation-prone, and increases the SDS-solubility of aggregates that do form. polyglutamine 52-65 huntingtin Homo sapiens 95-98 19705452-0 2010 A stable G-quartet binds to a huntingtin protein fragment containing expanded polyglutamine tracks. polyglutamine 78-91 huntingtin Homo sapiens 30-40 19705452-2 2010 The disease is the result of an expanded CAG repeat in exon 1 of the HD gene, which encodes an elongated polyglutamine tract in the mutant form of the protein, huntingtin. polyglutamine 105-118 huntingtin Homo sapiens 160-170 19705452-6 2010 We have previously reported that guanosine-rich oligonucleotides with the ability to fold into a G-quartet are effective inhibitors of the aggregation process of a huntingtin protein fragment with an elongated polyglutamine tract, Htn 1-171(Q58). polyglutamine 210-223 huntingtin Homo sapiens 164-174 20126661-1 2010 Huntington"s disease (HD) is caused by polyglutamine expansion in huntingtin (htt) protein, but the exact mechanism of HD pathogenesis remains uncertain. polyglutamine 39-52 huntingtin Homo sapiens 66-76 20126661-1 2010 Huntington"s disease (HD) is caused by polyglutamine expansion in huntingtin (htt) protein, but the exact mechanism of HD pathogenesis remains uncertain. polyglutamine 39-52 huntingtin Homo sapiens 78-81 20126661-2 2010 Recent evidence suggests that htt proteins with expanded polyglutamine tracts induce endoplasmic reticulum (ER) stress, probably by interfering with ER-associated degradation (ERAD). polyglutamine 57-70 huntingtin Homo sapiens 30-33 20126661-6 2010 These effects of htt negatively regulate the function of gp78 in ERAD and are aggravated by polyglutamine expansion. polyglutamine 92-105 huntingtin Homo sapiens 17-20 20126661-7 2010 Paradoxically, gp78 is still able to ubiquitinate and facilitate degradation of htt proteins with expanded polyglutamine. polyglutamine 107-120 huntingtin Homo sapiens 80-83 19878659-7 2009 Overexpression of ATP synthase alpha is able to protect cell death caused by polyglutamine-expanded htt. polyglutamine 77-90 huntingtin Homo sapiens 100-103 19338577-1 2010 Huntington"s disease (HD) is a neurodegenerative disease caused by mutant huntingtin protein containing an expanded polyglutamine tract, which may cause abnormal protein-protein interactions such as increased association with calmodulin (CaM). polyglutamine 116-129 huntingtin Homo sapiens 74-84 20026656-1 2009 Expansion of the polyglutamine repeat within the protein Huntingtin (Htt) causes Huntington"s disease, a neurodegenerative disease associated with aging and the accumulation of mutant Htt in diseased neurons. polyglutamine 17-30 huntingtin Homo sapiens 57-67 20026656-1 2009 Expansion of the polyglutamine repeat within the protein Huntingtin (Htt) causes Huntington"s disease, a neurodegenerative disease associated with aging and the accumulation of mutant Htt in diseased neurons. polyglutamine 17-30 huntingtin Homo sapiens 69-72 20026656-1 2009 Expansion of the polyglutamine repeat within the protein Huntingtin (Htt) causes Huntington"s disease, a neurodegenerative disease associated with aging and the accumulation of mutant Htt in diseased neurons. polyglutamine 17-30 huntingtin Homo sapiens 184-187 19664996-1 2009 The genetic mutation causing Huntington"s disease is a polyglutamine expansion in the huntingtin protein where more than 37 glutamines cause disease by formation of toxic intracellular fragments, aggregates, and cell death. polyglutamine 55-68 huntingtin Homo sapiens 86-96 20001957-4 2009 The authors have also identified HspB6 as a new binding partner for Bag3 and characterized further the binding of both HspB8 and HspB6 in Bag3-mediated clearance of aggregated polyglutamine-containing protein Htt43Q (huntingtin exon 1 fragment with 43 CAG repeats). polyglutamine 176-189 huntingtin Homo sapiens 217-227 19909260-3 2009 HD is caused by an expanded CAG repeat in the first exon of the HD gene that results in an abnormally elongated polyQ (polyglutamine) tract in its protein product, Htt (Huntingtin). polyglutamine 112-117 huntingtin Homo sapiens 164-167 19909260-3 2009 HD is caused by an expanded CAG repeat in the first exon of the HD gene that results in an abnormally elongated polyQ (polyglutamine) tract in its protein product, Htt (Huntingtin). polyglutamine 112-117 huntingtin Homo sapiens 169-179 19909260-3 2009 HD is caused by an expanded CAG repeat in the first exon of the HD gene that results in an abnormally elongated polyQ (polyglutamine) tract in its protein product, Htt (Huntingtin). polyglutamine 119-132 huntingtin Homo sapiens 164-167 19909260-3 2009 HD is caused by an expanded CAG repeat in the first exon of the HD gene that results in an abnormally elongated polyQ (polyglutamine) tract in its protein product, Htt (Huntingtin). polyglutamine 119-132 huntingtin Homo sapiens 169-179 19915590-4 2009 Unexpectedly, TRiC does not physically block the polyQ tract itself, but rather sequesters a short Htt sequence element, N-terminal to the polyQ tract, that promotes the amyloidogenic conformation. polyglutamine 139-144 huntingtin Homo sapiens 99-102 19710014-1 2009 Huntingtin (Htt) is a widely expressed protein that causes tissue-specific degeneration when mutated to contain an expanded polyglutamine (poly(Q)) domain. polyglutamine 139-146 huntingtin Homo sapiens 12-15 19710014-1 2009 Huntingtin (Htt) is a widely expressed protein that causes tissue-specific degeneration when mutated to contain an expanded polyglutamine (poly(Q)) domain. polyglutamine 124-137 huntingtin Homo sapiens 0-10 19710014-1 2009 Huntingtin (Htt) is a widely expressed protein that causes tissue-specific degeneration when mutated to contain an expanded polyglutamine (poly(Q)) domain. polyglutamine 124-137 huntingtin Homo sapiens 12-15 19710014-1 2009 Huntingtin (Htt) is a widely expressed protein that causes tissue-specific degeneration when mutated to contain an expanded polyglutamine (poly(Q)) domain. polyglutamine 139-146 huntingtin Homo sapiens 0-10 19752198-3 2009 Here we studied fibroblasts of healthy individuals and patients with Huntington"s disease (HD), which is a movement disorder caused by polyglutamine expansion in Htt. polyglutamine 135-148 huntingtin Homo sapiens 162-165 19843462-10 2009 The conformational adaptability of the polyQ segment permits the cis-inhibitory effect of polyP segments on fibrillation by the polyQ segments in proteins such as huntingtin. polyglutamine 39-44 huntingtin Homo sapiens 163-173 19843462-10 2009 The conformational adaptability of the polyQ segment permits the cis-inhibitory effect of polyP segments on fibrillation by the polyQ segments in proteins such as huntingtin. polyglutamine 128-133 huntingtin Homo sapiens 163-173 19776381-7 2009 The underlying mechanism may involve interaction of the polyglutamine domains of normal and mutant huntingtin (fragments) and needs further elucidation. polyglutamine 56-69 huntingtin Homo sapiens 99-109 19602103-8 2009 These data indicate that insulin release from beta-cells expressing mutant huntingtin appears to be polyglutamine length-dependent, and that polyglutamine lengths within the range normally found in adult onset HD do not influence insulin release. polyglutamine 100-113 huntingtin Homo sapiens 75-85 19607813-0 2009 Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers. polyglutamine 0-13 huntingtin Homo sapiens 27-37 19607813-1 2009 An expanded polyglutamine (Q) tract (>37Q) in huntingtin (htt) causes Huntington disease. polyglutamine 12-25 huntingtin Homo sapiens 46-56 19607813-1 2009 An expanded polyglutamine (Q) tract (>37Q) in huntingtin (htt) causes Huntington disease. polyglutamine 12-25 huntingtin Homo sapiens 58-61 19607813-2 2009 Htt associates with membranes and polyglutamine expansion in htt may alter membrane function in Huntington disease through a mechanism that is not known. polyglutamine 34-47 huntingtin Homo sapiens 61-64 19607813-3 2009 Here we used differential scanning calorimetry to examine the effects of polyQ expansion in htt on its insertion into lipid bilayers. polyglutamine 73-78 huntingtin Homo sapiens 92-95 19726651-2 2009 Previously, we demonstrated that NMDA receptor (NMDAR)-mediated current and/or toxicity is increased in MSNs from the yeast artificial chromosome (YAC) transgenic mouse model expressing polyglutamine (polyQ)-expanded (mutant) full-length human huntingtin (htt). polyglutamine 186-199 huntingtin Homo sapiens 244-254 19726651-2 2009 Previously, we demonstrated that NMDA receptor (NMDAR)-mediated current and/or toxicity is increased in MSNs from the yeast artificial chromosome (YAC) transgenic mouse model expressing polyglutamine (polyQ)-expanded (mutant) full-length human huntingtin (htt). polyglutamine 186-199 huntingtin Homo sapiens 256-259 19726651-2 2009 Previously, we demonstrated that NMDA receptor (NMDAR)-mediated current and/or toxicity is increased in MSNs from the yeast artificial chromosome (YAC) transgenic mouse model expressing polyglutamine (polyQ)-expanded (mutant) full-length human huntingtin (htt). polyglutamine 201-206 huntingtin Homo sapiens 244-254 19726651-2 2009 Previously, we demonstrated that NMDA receptor (NMDAR)-mediated current and/or toxicity is increased in MSNs from the yeast artificial chromosome (YAC) transgenic mouse model expressing polyglutamine (polyQ)-expanded (mutant) full-length human huntingtin (htt). polyglutamine 201-206 huntingtin Homo sapiens 256-259 19759302-1 2009 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, caused by a polyglutamine expansion in the huntingtin protein (htt). polyglutamine 91-104 huntingtin Homo sapiens 122-140 19759302-1 2009 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, caused by a polyglutamine expansion in the huntingtin protein (htt). polyglutamine 91-104 huntingtin Homo sapiens 142-145 19748335-3 2009 now describe multiple crystal structures and demonstrate that polyglutamine in huntingtin dances through multiple conformations. polyglutamine 62-75 huntingtin Homo sapiens 79-89 19748341-1 2009 Huntington"s disease is a genetic neurodegenerative disorder resulting from polyglutamine (polyQ) expansion (>36Q) within the first exon of Huntingtin (Htt) protein. polyglutamine 76-89 huntingtin Homo sapiens 143-153 19748341-1 2009 Huntington"s disease is a genetic neurodegenerative disorder resulting from polyglutamine (polyQ) expansion (>36Q) within the first exon of Huntingtin (Htt) protein. polyglutamine 76-89 huntingtin Homo sapiens 155-158 19748341-1 2009 Huntington"s disease is a genetic neurodegenerative disorder resulting from polyglutamine (polyQ) expansion (>36Q) within the first exon of Huntingtin (Htt) protein. polyglutamine 91-96 huntingtin Homo sapiens 143-153 19748341-1 2009 Huntington"s disease is a genetic neurodegenerative disorder resulting from polyglutamine (polyQ) expansion (>36Q) within the first exon of Huntingtin (Htt) protein. polyglutamine 91-96 huntingtin Homo sapiens 155-158 21048629-1 2009 Huntington"s disease is caused by a trinucleotide repeat expansion (CAG)n in the gene coding for Huntingtin (Htt) and is one of the several polyglutamine diseases. polyglutamine 140-153 huntingtin Homo sapiens 97-107 19549822-1 2009 Huntington"s disease is linked to the insertion of glutamine (Q) in the protein huntingtin, resulting in polyglutamine (polyQ) expansions that self-associate to form aggregates. polyglutamine 105-118 huntingtin Homo sapiens 80-90 19549822-1 2009 Huntington"s disease is linked to the insertion of glutamine (Q) in the protein huntingtin, resulting in polyglutamine (polyQ) expansions that self-associate to form aggregates. polyglutamine 120-125 huntingtin Homo sapiens 80-90 19667213-1 2009 Huntington disease is an incurable, dominant neurodegenerative disorder caused by polyglutamine repeat expansion in the huntingtin protein. polyglutamine 82-95 huntingtin Homo sapiens 120-130 19491400-0 2009 Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment. polyglutamine 75-88 huntingtin Homo sapiens 101-111 19491400-1 2009 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt). polyglutamine 84-97 huntingtin Homo sapiens 141-151 19491400-1 2009 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt). polyglutamine 84-97 huntingtin Homo sapiens 153-156 19491400-1 2009 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt). polyglutamine 99-104 huntingtin Homo sapiens 141-151 19491400-1 2009 Huntington disease (HD) is a neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt). polyglutamine 99-104 huntingtin Homo sapiens 153-156 19491400-2 2009 PolyQ expansion above 35-40 results in disease associated with htt aggregation into inclusion bodies. polyglutamine 0-5 huntingtin Homo sapiens 63-66 21048629-1 2009 Huntington"s disease is caused by a trinucleotide repeat expansion (CAG)n in the gene coding for Huntingtin (Htt) and is one of the several polyglutamine diseases. polyglutamine 140-153 huntingtin Homo sapiens 109-112 19487684-3 2009 Here we show that huntingtin-exon1 (thtt) with expanded polyglutamines remarkably misfolds into distinct amyloid conformations under different temperatures, such as 4 degrees C and 37 degrees C. The 4 degrees C amyloid has loop/turn structures together with mostly beta-sheets, including exposed polyglutamines, whereas the 37 degrees C amyloid has more extended and buried beta-sheets. polyglutamine 296-310 huntingtin Homo sapiens 18-28 19487684-3 2009 Here we show that huntingtin-exon1 (thtt) with expanded polyglutamines remarkably misfolds into distinct amyloid conformations under different temperatures, such as 4 degrees C and 37 degrees C. The 4 degrees C amyloid has loop/turn structures together with mostly beta-sheets, including exposed polyglutamines, whereas the 37 degrees C amyloid has more extended and buried beta-sheets. polyglutamine 56-70 huntingtin Homo sapiens 18-28 19270310-3 2009 How the huntingtin protein with expanded polyglutamines (mutant huntingtin) causes the disease is still unclear, but phosphorylation of huntingtin appears to be protective. polyglutamine 41-55 huntingtin Homo sapiens 8-18 19278999-1 2009 Huntington disease (HD) is a fatal hereditary neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 102-115 huntingtin Homo sapiens 135-145 19278999-1 2009 Huntington disease (HD) is a fatal hereditary neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 102-115 huntingtin Homo sapiens 147-150 19278999-1 2009 Huntington disease (HD) is a fatal hereditary neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 117-122 huntingtin Homo sapiens 135-145 19278999-1 2009 Huntington disease (HD) is a fatal hereditary neurodegenerative disease caused by an expansion of the polyglutamine (polyQ) stretch in huntingtin (htt). polyglutamine 117-122 huntingtin Homo sapiens 147-150 19361448-10 2009 We propose the most fundamental role played by N17(Htt) would be initializing the dimerization and pulling the polyQ chains into adequate spatial proximity for the nucleation event to proceed. polyglutamine 111-116 huntingtin Homo sapiens 51-54 19270310-3 2009 How the huntingtin protein with expanded polyglutamines (mutant huntingtin) causes the disease is still unclear, but phosphorylation of huntingtin appears to be protective. polyglutamine 41-55 huntingtin Homo sapiens 64-74 19270310-3 2009 How the huntingtin protein with expanded polyglutamines (mutant huntingtin) causes the disease is still unclear, but phosphorylation of huntingtin appears to be protective. polyglutamine 41-55 huntingtin Homo sapiens 64-74 19039036-5 2009 Immunofluorescence staining of cells using antibodies against Tom20, a mitochondrion localized protein, revealed that cells expressing Htt proteins with 74 or 138 polyglutamine repeats were more sensitized to oxidative stress-induced mitochondria fragmentation and had reduced ATP levels compared with cells expressing Htt proteins with 17 or 28 polyglutamine repeats. polyglutamine 346-359 huntingtin Homo sapiens 135-138 19039036-1 2009 Huntington"s disease (HD) is caused by an expansion of a CAG trinucleotide sequence that encodes a polyglutamine tract in the huntingtin (Htt) protein. polyglutamine 99-112 huntingtin Homo sapiens 126-136 19039036-1 2009 Huntington"s disease (HD) is caused by an expansion of a CAG trinucleotide sequence that encodes a polyglutamine tract in the huntingtin (Htt) protein. polyglutamine 99-112 huntingtin Homo sapiens 138-141 19039036-4 2009 We examined mitochondrial properties of HeLa cells that expressed green fluorescent protein (GFP)- or FLAG-tagged N-terminal portions of the Htt protein containing either, 17, 28, 74 or 138 polyglutamine repeats. polyglutamine 190-203 huntingtin Homo sapiens 141-144 19039036-5 2009 Immunofluorescence staining of cells using antibodies against Tom20, a mitochondrion localized protein, revealed that cells expressing Htt proteins with 74 or 138 polyglutamine repeats were more sensitized to oxidative stress-induced mitochondria fragmentation and had reduced ATP levels compared with cells expressing Htt proteins with 17 or 28 polyglutamine repeats. polyglutamine 163-176 huntingtin Homo sapiens 135-138 19386911-6 2009 We thus propose that Htt aggregates act as an intracellular hub for the cross-seeded fibrillation of Q/N-rich AIPs and that a cross-seeding reaction is a molecular origin to cause diverse pathologies in a polyglutamine disease. polyglutamine 205-218 huntingtin Homo sapiens 21-24 19270701-0 2009 Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. polyglutamine 0-13 huntingtin Homo sapiens 32-42 19270701-2 2009 We show here that the 17-amino-acid flanking sequence (HTT(NT)) N-terminal to the polyQ in the toxic huntingtin exon 1 fragment imparts onto this peptide a complex alternative aggregation mechanism. polyglutamine 82-87 huntingtin Homo sapiens 101-111 19269181-1 2009 The neurodegenerative disorder Huntington"s disease is caused by an expansion in the polyglutamine repeat region of the protein huntingtin. polyglutamine 85-98 huntingtin Homo sapiens 128-138 19240112-1 2009 Huntington"s disease is caused by a polyglutamine expansion in the huntingtin protein. polyglutamine 36-49 huntingtin Homo sapiens 67-77 19334076-1 2009 OBJECTIVE: Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin (htt) protein. polyglutamine 106-119 huntingtin Homo sapiens 137-147 19334076-1 2009 OBJECTIVE: Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin (htt) protein. polyglutamine 106-119 huntingtin Homo sapiens 149-152 19039036-6 2009 By measuring changes in fluorescence of a photoactivated GFP protein targeted to mitochondria, we found that cells expressing red fluorescent protein (RFP)-tagged Htt protein containing 74 polyglutamine repeats had mitochondria that displayed reduced movement and fusion than cells expressing RFP-Htt protein with 28 polyglutamine repeats. polyglutamine 189-202 huntingtin Homo sapiens 163-166 19039036-6 2009 By measuring changes in fluorescence of a photoactivated GFP protein targeted to mitochondria, we found that cells expressing red fluorescent protein (RFP)-tagged Htt protein containing 74 polyglutamine repeats had mitochondria that displayed reduced movement and fusion than cells expressing RFP-Htt protein with 28 polyglutamine repeats. polyglutamine 317-330 huntingtin Homo sapiens 163-166 19039036-8 2009 In a Caenorhabditis elegans model of HD, we found that reduction of Drp-1 expression by RNA interference rescued the motility defect associated with the expression of Htt proteins with polyglutamine repeats. polyglutamine 185-198 huntingtin Homo sapiens 167-170 19039036-9 2009 These results suggest that the increase in cytotoxicity induced by Htt proteins containing expanded polyglutamine tracts is likely mediated, at least in part, by an alteration in normal mitochondrial dynamics, which results in increased mitochondrial fragmentation. polyglutamine 100-113 huntingtin Homo sapiens 67-70 19203385-1 2009 BACKGROUND: Expansion of a polyglutamine repeat at the amino-terminus of huntingtin is the probable cause for Huntington"s disease, a lethal progressive autosomal-dominant neurodegenerative disorders characterized by impaired motor performance and severe brain atrophy. polyglutamine 27-40 huntingtin Homo sapiens 73-83 19203385-2 2009 The expanded polyglutamine repeat changes the conformation of huntingtin and initiates a range of pathogenic mechanisms in neurons including intracellular huntingtin aggregates, transcriptional dysregulation, energy metabolism deficits, synaptic dystrophy and ultimately neurodegeneration. polyglutamine 13-26 huntingtin Homo sapiens 155-165 19203385-2 2009 The expanded polyglutamine repeat changes the conformation of huntingtin and initiates a range of pathogenic mechanisms in neurons including intracellular huntingtin aggregates, transcriptional dysregulation, energy metabolism deficits, synaptic dystrophy and ultimately neurodegeneration. polyglutamine 13-26 huntingtin Homo sapiens 62-72 19262167-1 2009 Huntington disease (HD) is caused by a polyglutamine expansion in the protein huntingtin (Htt). polyglutamine 39-52 huntingtin Homo sapiens 78-88 18636076-0 2009 Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. polyglutamine 73-86 huntingtin Homo sapiens 96-106 19262167-1 2009 Huntington disease (HD) is caused by a polyglutamine expansion in the protein huntingtin (Htt). polyglutamine 39-52 huntingtin Homo sapiens 90-93 19094060-1 2009 Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by a poly-glutamine expansion in huntingtin, the protein encoded by the HD gene. polyglutamine 90-104 huntingtin Homo sapiens 118-128 19094060-2 2009 PolyQ-expanded huntingtin is toxic to neurons, especially the medium spiny neurons of the striatum. polyglutamine 0-5 huntingtin Homo sapiens 15-25 19036965-9 2008 Thus, the cumulative effect of increasing huntingtin polyglutamine length is to enhance MSN sensitivity to excitotoxicity at least in part by calpain-mediated cell death signaling. polyglutamine 53-66 huntingtin Homo sapiens 42-52 19458943-1 2009 Huntington"s disease (HD) is an incurable, fatal neurodegenerative disorder that is caused by a polyglutamine expansion in the huntingtin (Htt) protein. polyglutamine 96-109 huntingtin Homo sapiens 127-137 19458943-1 2009 Huntington"s disease (HD) is an incurable, fatal neurodegenerative disorder that is caused by a polyglutamine expansion in the huntingtin (Htt) protein. polyglutamine 96-109 huntingtin Homo sapiens 139-142 18772195-3 2008 Using a strategy involving RNA (ribonucleic acid) interference and re-expression of various constructs, we show that polyQ (polyglutamine)-htt is unable to promote transport of brain-derived neurotrophic factor (BDNF)-containing vesicles, but polyQ-htt constitutively phosphorylated at S421 is as effective as the wild-type (wt) as concerns transport of these vesicles. polyglutamine 117-122 huntingtin Homo sapiens 139-142 18772195-4 2008 The S421 phosphorylated polyQ-htt displays the wt function of inducing BDNF release. polyglutamine 24-29 huntingtin Homo sapiens 30-33 19118166-3 2008 Polyglutamine expansions in huntingtin, which causes Huntington"s disease (HD), abrogates REST-huntingtin binding. polyglutamine 0-13 huntingtin Homo sapiens 28-38 19118166-3 2008 Polyglutamine expansions in huntingtin, which causes Huntington"s disease (HD), abrogates REST-huntingtin binding. polyglutamine 0-13 huntingtin Homo sapiens 95-105 18840504-1 2008 Huntington"s disease is an autosomal dominant neurodegenerative disorder caused by the expansion of a polyglutamine repeat tract in the huntingtin protein. polyglutamine 102-115 huntingtin Homo sapiens 136-146 18840504-2 2008 Polyglutamine-expanded huntingtin forms intranuclear as well as perinuclear inclusion bodies. polyglutamine 0-13 huntingtin Homo sapiens 23-33 18840504-5 2008 Laser confocal microscopy analysis revealed that huntingtin aggregates in a juxtanuclear position were associated with a clear focal distortion in the nuclear envelope in cells transfected with polyglutamine-expanded huntingtin. polyglutamine 194-207 huntingtin Homo sapiens 49-59 18840504-5 2008 Laser confocal microscopy analysis revealed that huntingtin aggregates in a juxtanuclear position were associated with a clear focal distortion in the nuclear envelope in cells transfected with polyglutamine-expanded huntingtin. polyglutamine 194-207 huntingtin Homo sapiens 217-227 18808762-2 2008 This mutation leads to the expression of an abnormal repeat of polyglutamines in the N-terminal region of Htt. polyglutamine 63-77 huntingtin Homo sapiens 106-109 18756529-2 2008 An expanded polyQ sequence in the huntingtin gene is known to cause the huntingtin protein to aggregate and form intracellular inclusions as disease progresses. polyglutamine 12-17 huntingtin Homo sapiens 34-44 18718937-1 2008 Huntington"s disease (HD) is caused by the expansion of the polyglutamine (polyQ) tract in the human Huntingtin (hHtt) protein (polyQ-hHtt). polyglutamine 60-73 huntingtin Homo sapiens 101-111 18718937-1 2008 Huntington"s disease (HD) is caused by the expansion of the polyglutamine (polyQ) tract in the human Huntingtin (hHtt) protein (polyQ-hHtt). polyglutamine 60-73 huntingtin Homo sapiens 113-117 18718937-1 2008 Huntington"s disease (HD) is caused by the expansion of the polyglutamine (polyQ) tract in the human Huntingtin (hHtt) protein (polyQ-hHtt). polyglutamine 60-73 huntingtin Homo sapiens 134-138 18718937-1 2008 Huntington"s disease (HD) is caused by the expansion of the polyglutamine (polyQ) tract in the human Huntingtin (hHtt) protein (polyQ-hHtt). polyglutamine 75-80 huntingtin Homo sapiens 101-111 18718937-1 2008 Huntington"s disease (HD) is caused by the expansion of the polyglutamine (polyQ) tract in the human Huntingtin (hHtt) protein (polyQ-hHtt). polyglutamine 75-80 huntingtin Homo sapiens 113-117 18718937-1 2008 Huntington"s disease (HD) is caused by the expansion of the polyglutamine (polyQ) tract in the human Huntingtin (hHtt) protein (polyQ-hHtt). polyglutamine 75-80 huntingtin Homo sapiens 134-138 18756529-2 2008 An expanded polyQ sequence in the huntingtin gene is known to cause the huntingtin protein to aggregate and form intracellular inclusions as disease progresses. polyglutamine 12-17 huntingtin Homo sapiens 72-82 18756529-4 2008 This review focuses on key questions remaining for how the expanded polyQ sequences affect the aggregation properties of the huntingtin protein and the corresponding effects on cellular machinery. polyglutamine 68-73 huntingtin Homo sapiens 125-135 18658163-5 2008 Ben markedly reduced the huntingtin-polyglutamine (htt-polyQ) aggregation in an inducible cellular system, and the therapeutic value of Ben was successfully recapitulated in the R6/2 animal model of HD. polyglutamine 55-60 huntingtin Homo sapiens 25-35 18658163-5 2008 Ben markedly reduced the huntingtin-polyglutamine (htt-polyQ) aggregation in an inducible cellular system, and the therapeutic value of Ben was successfully recapitulated in the R6/2 animal model of HD. polyglutamine 55-60 huntingtin Homo sapiens 51-54 18658163-6 2008 To reveal the mechanism of action, Ben was found to be able to alleviate the inhibition of the ubiquitin-proteasome system (UPS) activity, resulting in enhanced degradation of soluble htt-polyQ specifically in its pathological range. polyglutamine 188-193 huntingtin Homo sapiens 184-187 18923047-0 2008 Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. polyglutamine 100-113 huntingtin Homo sapiens 0-10 18923047-1 2008 Transcriptional dysregulation is a central pathogenic mechanism in Huntington"s disease, a fatal neurodegenerative disorder associated with polyglutamine (polyQ) expansion in the huntingtin (Htt) protein. polyglutamine 140-153 huntingtin Homo sapiens 179-189 18923047-1 2008 Transcriptional dysregulation is a central pathogenic mechanism in Huntington"s disease, a fatal neurodegenerative disorder associated with polyglutamine (polyQ) expansion in the huntingtin (Htt) protein. polyglutamine 140-153 huntingtin Homo sapiens 191-194 18923047-1 2008 Transcriptional dysregulation is a central pathogenic mechanism in Huntington"s disease, a fatal neurodegenerative disorder associated with polyglutamine (polyQ) expansion in the huntingtin (Htt) protein. polyglutamine 155-160 huntingtin Homo sapiens 179-189 18923047-1 2008 Transcriptional dysregulation is a central pathogenic mechanism in Huntington"s disease, a fatal neurodegenerative disorder associated with polyglutamine (polyQ) expansion in the huntingtin (Htt) protein. polyglutamine 155-160 huntingtin Homo sapiens 191-194 18923047-3 2008 Chromatin immunoprecipitation (ChIP) demonstrates Htt occupation of gene promoters in vivo in a polyQ-dependent manner, and furthermore, ChIP-on-chip and ChIP subcloning reveal that wild-type and mutant Htt exhibit differential genomic distributions. polyglutamine 96-101 huntingtin Homo sapiens 50-53 18923047-5 2008 PolyQ expansion increases Htt-DNA interactions, with binding to recognition elements of transcription factors whose function is altered in HD. polyglutamine 0-5 huntingtin Homo sapiens 26-29 18586675-1 2008 Huntington disease derives from a critically expanded polyglutamine tract in the huntingtin (Htt) protein; a similar polyglutamine expansion in the androgen receptor (AR) causes spinobulbar muscular atrophy. polyglutamine 54-67 huntingtin Homo sapiens 81-91 18573880-4 2008 The overexpression of profilin reduces the aggregation of polyglutamine-expanded Htt and androgen receptor (AR) peptides. polyglutamine 58-71 huntingtin Homo sapiens 81-84 18768695-2 2008 The polyQ expansion that causes Huntington"s disease (HD) is in the first exon (HDx-1) of huntingtin (Htt). polyglutamine 4-9 huntingtin Homo sapiens 90-100 18768695-2 2008 The polyQ expansion that causes Huntington"s disease (HD) is in the first exon (HDx-1) of huntingtin (Htt). polyglutamine 4-9 huntingtin Homo sapiens 102-105 18586675-1 2008 Huntington disease derives from a critically expanded polyglutamine tract in the huntingtin (Htt) protein; a similar polyglutamine expansion in the androgen receptor (AR) causes spinobulbar muscular atrophy. polyglutamine 54-67 huntingtin Homo sapiens 93-96 18488016-4 2008 Mutant HTT with expanded polyglutamine (polyQ) is widely expressed in the brain and peripheral tissues, but causes selective neurodegeneration that is most prominent in the striatum and cortex of the brain. polyglutamine 25-38 huntingtin Homo sapiens 7-10 18550760-0 2008 Full-length human mutant huntingtin with a stable polyglutamine repeat can elicit progressive and selective neuropathogenesis in BACHD mice. polyglutamine 50-63 huntingtin Homo sapiens 25-35 18488016-4 2008 Mutant HTT with expanded polyglutamine (polyQ) is widely expressed in the brain and peripheral tissues, but causes selective neurodegeneration that is most prominent in the striatum and cortex of the brain. polyglutamine 40-45 huntingtin Homo sapiens 7-10 18504298-3 2008 We generated an intracellular antibody (intrabody) whose binding to a unique epitope of human huntingtin is enhanced by polyglutamine expansion. polyglutamine 120-133 huntingtin Homo sapiens 94-104 18714598-1 2008 Huntington"s disease (HD) is a neurological degenerative disorder, inherited by an autosomal dominant mode, and caused by a CAG triplet expansion coding for a poly-glutamine sequence in the huntingtin protein. polyglutamine 159-173 huntingtin Homo sapiens 190-200 18466116-1 2008 Huntington"s disease (HD) is a devastating autosomal dominant neurodegenerative disease caused by a CAG trinucleotide repeat expansion encoding an abnormally long polyglutamine tract in the huntingtin protein. polyglutamine 163-176 huntingtin Homo sapiens 190-200 18466116-6 2008 It is likely that the toxicity of mutant huntingtin is revealed after a series of cleavage events leading to the production of N-terminal huntingtin fragment(s) containing the expanded polyglutamine tract. polyglutamine 185-198 huntingtin Homo sapiens 41-51 18466116-6 2008 It is likely that the toxicity of mutant huntingtin is revealed after a series of cleavage events leading to the production of N-terminal huntingtin fragment(s) containing the expanded polyglutamine tract. polyglutamine 185-198 huntingtin Homo sapiens 138-148 18243803-2 2008 As the polyglutamine (polyQ) region becomes longer than the critical length, the disease occurs and Huntingtin protein aggregates, both in vitro and in vivo, as suggested by experimental and clinical data. polyglutamine 7-20 huntingtin Homo sapiens 100-110 18454252-2 2008 In Huntington"s disease, a polyglutamine expansion in the huntingtin protein triggers neuronal toxicity. polyglutamine 27-40 huntingtin Homo sapiens 58-68 18192679-1 2008 A polyglutamine repeat expansion of more than 36 units in a protein called huntingtin (htt) is the only known cause of Huntington"s disease (HD). polyglutamine 2-15 huntingtin Homo sapiens 75-85 18192679-1 2008 A polyglutamine repeat expansion of more than 36 units in a protein called huntingtin (htt) is the only known cause of Huntington"s disease (HD). polyglutamine 2-15 huntingtin Homo sapiens 87-90 18243803-2 2008 As the polyglutamine (polyQ) region becomes longer than the critical length, the disease occurs and Huntingtin protein aggregates, both in vitro and in vivo, as suggested by experimental and clinical data. polyglutamine 22-27 huntingtin Homo sapiens 100-110 18065495-1 2008 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) expansion in the huntingtin (htt) protein. polyglutamine 41-54 huntingtin Homo sapiens 80-90 18199701-7 2008 Hence, a modest reduction in huntingtin synthesis by rapamycin may lead to a substantial decrease in the probability of reaching the critical concentration required for a nucleation event and subsequent toxic polyQ aggregation. polyglutamine 209-214 huntingtin Homo sapiens 29-39 18065495-1 2008 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) expansion in the huntingtin (htt) protein. polyglutamine 41-54 huntingtin Homo sapiens 92-95 18065495-1 2008 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) expansion in the huntingtin (htt) protein. polyglutamine 56-61 huntingtin Homo sapiens 80-90 18065495-1 2008 Huntington"s disease (HD) is caused by a polyglutamine (polyQ) expansion in the huntingtin (htt) protein. polyglutamine 56-61 huntingtin Homo sapiens 92-95 17999380-2 2008 The primary locus of the disorder is a polyglutamine expansion of the protein product of the huntingtin (htt) gene. polyglutamine 39-52 huntingtin Homo sapiens 93-103 18167354-0 2008 RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. polyglutamine 108-121 huntingtin Homo sapiens 76-86 18241680-8 2008 Phophorlyated Hsp27 also decreased the inclusion body formation by the huntingtin polyglutamines. polyglutamine 82-96 huntingtin Homo sapiens 71-81 17999380-2 2008 The primary locus of the disorder is a polyglutamine expansion of the protein product of the huntingtin (htt) gene. polyglutamine 39-52 huntingtin Homo sapiens 105-108 18048403-9 2008 Finally, we report an evident relaxing constraint of the N-terminal block in Ciona and drosophilids that correlates with the absence of polyQ and which may indicate that the N-terminal portion of htt has evolved different functions in Ciona and protostomes. polyglutamine 136-141 huntingtin Homo sapiens 196-199 17921520-1 2008 Huntington"s disease (HD) is caused by a polyglutamine expansion mutation in the huntingtin protein that confers a toxic gain-of-function and causes the protein to become aggregate-prone. polyglutamine 41-54 huntingtin Homo sapiens 81-91 17986868-4 2008 This release is inhibited when huntingtin contains the polyglutamine expansion seen in Huntington"s disease. polyglutamine 55-68 huntingtin Homo sapiens 31-41 19118672-7 2008 Our approach has been developed using as a case study the predominantly beta-sheet intracellular lipid-binding protein, cellular retinoic acid-binding protein, alone or as a chimera fused to the exon 1-encoded fragment of huntingtin, which harbors a polyglutamine repeat tract. polyglutamine 250-263 huntingtin Homo sapiens 222-232 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 140-153 huntingtin Homo sapiens 173-183 17989880-2 2007 The present study was undertaken to evaluate the potential contributions of the polyQ and polyproline (polyP) domains to the co-localization of mutant huntingtin (htt) and GAPDH. polyglutamine 80-85 huntingtin Homo sapiens 151-161 17989880-2 2007 The present study was undertaken to evaluate the potential contributions of the polyQ and polyproline (polyP) domains to the co-localization of mutant huntingtin (htt) and GAPDH. polyglutamine 80-85 huntingtin Homo sapiens 163-166 17240517-4 2007 Therefore, it is becoming increasingly paramount to understand the normal functions of these polyglutamine disease proteins, which include huntingtin, the polyglutamine-expanded protein in Huntington"s disease (HD). polyglutamine 93-106 huntingtin Homo sapiens 139-149 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 140-153 huntingtin Homo sapiens 193-196 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 155-160 huntingtin Homo sapiens 173-183 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 155-160 huntingtin Homo sapiens 193-196 17726098-2 2007 HD is caused by polyglutamine expansions in the huntingtin (htt) protein that result in neuronal loss and contribute to HD pathology. polyglutamine 16-29 huntingtin Homo sapiens 48-58 17726098-2 2007 HD is caused by polyglutamine expansions in the huntingtin (htt) protein that result in neuronal loss and contribute to HD pathology. polyglutamine 16-29 huntingtin Homo sapiens 60-63 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 huntingtin Homo sapiens 90-100 17687326-1 2007 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expansion of CAG triplet repeats in the huntingtin (HTT) gene (also called HD) and characterized by accumulation of aggregated fragments of polyglutamine-expanded HTT protein in affected neurons. polyglutamine 229-242 huntingtin Homo sapiens 129-139 17687326-1 2007 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expansion of CAG triplet repeats in the huntingtin (HTT) gene (also called HD) and characterized by accumulation of aggregated fragments of polyglutamine-expanded HTT protein in affected neurons. polyglutamine 229-242 huntingtin Homo sapiens 141-144 17687326-1 2007 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expansion of CAG triplet repeats in the huntingtin (HTT) gene (also called HD) and characterized by accumulation of aggregated fragments of polyglutamine-expanded HTT protein in affected neurons. polyglutamine 229-242 huntingtin Homo sapiens 252-255 17373643-1 2007 Huntington"s disease is a neurodegenerative disease caused by a polyglutamine (polyQ) expansion in Huntingtin, which provokes aggregation of a proteolytic amino-terminal fragment of the affected protein encompassing the polyQ expansion. polyglutamine 64-77 huntingtin Homo sapiens 99-109 17516099-6 2007 Most strikingly, we identified a Huntingtin allele with 21 uninterrupted CAG repeats encoding a stretch of 24 polyglutamines. polyglutamine 110-124 huntingtin Homo sapiens 33-43 17652581-2 2007 PolyQ expansion in Htt(exp) causes selective degeneration of striatal medium spiny neurons (MSNs) in HD patients. polyglutamine 0-5 huntingtin Homo sapiens 19-22 17653262-8 2007 Surprisingly, the correlation between the aggregation lag times of polyQ tracts and the intensity of anti-1C2 signal on soluble monomers of huntingtin precisely reflected the repeat-length dependent age-of-onset of HD patients. polyglutamine 67-72 huntingtin Homo sapiens 140-150 17611284-1 2007 Huntingtin is an antiapoptotic protein that becomes toxic when its polyglutamine stretch is expanded, resulting in Huntington"s disease (HD). polyglutamine 67-80 huntingtin Homo sapiens 0-10 17373643-1 2007 Huntington"s disease is a neurodegenerative disease caused by a polyglutamine (polyQ) expansion in Huntingtin, which provokes aggregation of a proteolytic amino-terminal fragment of the affected protein encompassing the polyQ expansion. polyglutamine 79-84 huntingtin Homo sapiens 99-109 17373643-1 2007 Huntington"s disease is a neurodegenerative disease caused by a polyglutamine (polyQ) expansion in Huntingtin, which provokes aggregation of a proteolytic amino-terminal fragment of the affected protein encompassing the polyQ expansion. polyglutamine 220-225 huntingtin Homo sapiens 99-109 17379859-5 2007 In a high-throughput chemical screen, they identified compounds that facilitate the clearance of a small huntingtin fragment with extended polyglutamines fused to green fluorescent protein reporter. polyglutamine 139-153 huntingtin Homo sapiens 105-115 17356014-0 2007 Extended polyglutamine repeats trigger a feedback loop involving the mitochondrial complex III, the proteasome and huntingtin aggregates. polyglutamine 9-22 huntingtin Homo sapiens 115-125 17318184-9 2007 Thus, PSA, which is induced in neurons expressing mutant huntingtin, appears critical in preventing the accumulation of polyQ peptides in normal cells, and its activity may influence susceptibility to polyQ diseases. polyglutamine 120-125 huntingtin Homo sapiens 57-67 17173700-1 2006 Huntington disease (HD) is caused by expansion of a polyglutamine (polyQ) domain in the protein known as huntingtin (htt), and the disease is characterized by selective neurodegeneration. polyglutamine 52-65 huntingtin Homo sapiens 105-115 17208201-2 2007 Aberrant expansion of the polyglutamine tract located in the N-terminal region of huntingtin results in Huntington"s disease. polyglutamine 26-39 huntingtin Homo sapiens 82-92 17208201-4 2007 Experimentally, both full-length huntingtin and N-terminal fragments of huntingtin with expanded polyglutamine tracts trigger aggregate formation. polyglutamine 97-110 huntingtin Homo sapiens 72-82 17189290-1 2007 Huntington disease (HD) is an autosomal dominant neurodegenerative disease caused by an expanded CAG trinucleotide repeat in the first exon of the HD gene, which results in a toxic polyglutamine stretch within huntingtin, the protein it encodes. polyglutamine 181-194 huntingtin Homo sapiens 210-220 17141218-0 2007 Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. polyglutamine 78-91 huntingtin Homo sapiens 101-111 17141218-4 2007 We tested this idea by using polyglutamine (polyQ)-containing huntingtin (htt) protein as a model substrate. polyglutamine 29-42 huntingtin Homo sapiens 62-72 17141218-4 2007 We tested this idea by using polyglutamine (polyQ)-containing huntingtin (htt) protein as a model substrate. polyglutamine 29-42 huntingtin Homo sapiens 74-77 17240289-3 2007 The mutant protein in Huntington"s disease--huntingtin--results from an expanded CAG repeat leading to a polyglutamine strand of variable length at the N-terminus. polyglutamine 105-118 huntingtin Homo sapiens 44-54 17266642-1 2007 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) tract in the huntingtin protein, resulting in intracellular aggregate formation and neurodegeneration. polyglutamine 104-117 huntingtin Homo sapiens 139-149 17266642-1 2007 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) tract in the huntingtin protein, resulting in intracellular aggregate formation and neurodegeneration. polyglutamine 119-124 huntingtin Homo sapiens 139-149 17596719-0 2007 Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation. polyglutamine 54-59 huntingtin Homo sapiens 69-79 19172113-1 2007 Huntingtin containing an expanded polyglutamine causes neuronal death and Huntington disease. polyglutamine 34-47 huntingtin Homo sapiens 0-10 17173700-1 2006 Huntington disease (HD) is caused by expansion of a polyglutamine (polyQ) domain in the protein known as huntingtin (htt), and the disease is characterized by selective neurodegeneration. polyglutamine 52-65 huntingtin Homo sapiens 117-120 17173700-1 2006 Huntington disease (HD) is caused by expansion of a polyglutamine (polyQ) domain in the protein known as huntingtin (htt), and the disease is characterized by selective neurodegeneration. polyglutamine 67-72 huntingtin Homo sapiens 105-115 17173700-1 2006 Huntington disease (HD) is caused by expansion of a polyglutamine (polyQ) domain in the protein known as huntingtin (htt), and the disease is characterized by selective neurodegeneration. polyglutamine 67-72 huntingtin Homo sapiens 117-120 17012230-1 2006 Huntington disease (HD) is an adult-onset neurodegenerative disease caused by expansion of a polyglutamine (poly(Q) tract in the N-terminal region of huntingtin (htt). polyglutamine 93-106 huntingtin Homo sapiens 150-160 17012230-1 2006 Huntington disease (HD) is an adult-onset neurodegenerative disease caused by expansion of a polyglutamine (poly(Q) tract in the N-terminal region of huntingtin (htt). polyglutamine 93-106 huntingtin Homo sapiens 162-165 17012230-1 2006 Huntington disease (HD) is an adult-onset neurodegenerative disease caused by expansion of a polyglutamine (poly(Q) tract in the N-terminal region of huntingtin (htt). polyglutamine 108-115 huntingtin Homo sapiens 150-160 17012230-1 2006 Huntington disease (HD) is an adult-onset neurodegenerative disease caused by expansion of a polyglutamine (poly(Q) tract in the N-terminal region of huntingtin (htt). polyglutamine 108-115 huntingtin Homo sapiens 162-165 16782707-3 2006 Polyglutamine (polyQ) expansion in the N terminus of Htt causes the neurodegenerative disorder Huntington disease (HD). polyglutamine 0-13 huntingtin Homo sapiens 53-56 17041811-2 2006 The defective gene in HD contains a trinucleotide CAG repeat expansion within its coding region that expresses a polyglutamine repeat in the protein huntingtin. polyglutamine 113-126 huntingtin Homo sapiens 149-159 16980958-5 2006 Analysis of the aggregation states of the Htt-polyQ proteins by fluorescence correlation spectroscopy revealed that CCT depletion results in the appearance of soluble Htt-polyQ aggregates. polyglutamine 46-51 huntingtin Homo sapiens 42-45 16980958-5 2006 Analysis of the aggregation states of the Htt-polyQ proteins by fluorescence correlation spectroscopy revealed that CCT depletion results in the appearance of soluble Htt-polyQ aggregates. polyglutamine 46-51 huntingtin Homo sapiens 167-170 16980959-2 2006 Here, we show that the hetero-oligomeric chaperonin TRiC (also known as CCT) physically interacts with polyglutamine-expanded variants of huntingtin (Htt) and effectively inhibits their aggregation. polyglutamine 103-116 huntingtin Homo sapiens 138-148 16980959-2 2006 Here, we show that the hetero-oligomeric chaperonin TRiC (also known as CCT) physically interacts with polyglutamine-expanded variants of huntingtin (Htt) and effectively inhibits their aggregation. polyglutamine 103-116 huntingtin Homo sapiens 150-153 16893904-2 2006 Preventing early misfolding steps and thereby aggregation of the polyglutamine (polyQ)-containing protein huntingtin (htt) in neurons of patients may represent an attractive therapeutic strategy to postpone the onset and progression of HD. polyglutamine 65-78 huntingtin Homo sapiens 106-116 16893904-2 2006 Preventing early misfolding steps and thereby aggregation of the polyglutamine (polyQ)-containing protein huntingtin (htt) in neurons of patients may represent an attractive therapeutic strategy to postpone the onset and progression of HD. polyglutamine 65-78 huntingtin Homo sapiens 118-121 16893904-2 2006 Preventing early misfolding steps and thereby aggregation of the polyglutamine (polyQ)-containing protein huntingtin (htt) in neurons of patients may represent an attractive therapeutic strategy to postpone the onset and progression of HD. polyglutamine 80-85 huntingtin Homo sapiens 106-116 16893904-2 2006 Preventing early misfolding steps and thereby aggregation of the polyglutamine (polyQ)-containing protein huntingtin (htt) in neurons of patients may represent an attractive therapeutic strategy to postpone the onset and progression of HD. polyglutamine 80-85 huntingtin Homo sapiens 118-121 16893904-5 2006 Also, EGCG significantly reduced polyQ-mediated htt protein aggregation and cytotoxicity in an yeast model of HD. polyglutamine 33-38 huntingtin Homo sapiens 48-51 16893904-7 2006 These results indicate that modulators of htt exon 1 misfolding and oligomerization like EGCG are likely to reduce polyQ-mediated toxicity in vivo. polyglutamine 115-120 huntingtin Homo sapiens 42-45 16829072-3 2006 However, continued application of genetic strategies has suggested that the disease process is, in fact, triggered by the presence of expanded polyglutamine in intact huntingtin. polyglutamine 143-156 huntingtin Homo sapiens 167-177 16782707-3 2006 Polyglutamine (polyQ) expansion in the N terminus of Htt causes the neurodegenerative disorder Huntington disease (HD). polyglutamine 15-20 huntingtin Homo sapiens 53-56 16782707-4 2006 The cytotoxicity of mutant Htt is modulated by proteolytic cleavage with caspases and calpains generating N-terminal polyQ-containing fragments. polyglutamine 117-122 huntingtin Homo sapiens 27-30 16817855-1 2006 We recently reported that the transient expression of polyglutamine tracts of various size in exon 1 of the huntingtin polypeptide (httEx1) generated abnormally high levels of intracellular reactive oxygen species that directly contributed to cell death. polyglutamine 54-67 huntingtin Homo sapiens 108-118 16840706-1 2006 Huntington"s disease is a neurological disorder caused by the expansion of a polyglutamine tract in the protein huntingtin. polyglutamine 77-90 huntingtin Homo sapiens 112-122 16822347-2 2006 Since the causative mutation of an expanded polyglutamine repeat in the huntingtin gene was identified, significant progress has been achieved in elucidating pathogenic mechanisms. polyglutamine 44-57 huntingtin Homo sapiens 72-82 16595690-1 2006 Huntington disease is an inherited neurodegenerative disorder that is caused by expanded CAG trinucleotide repeats, resulting in a polyglutamine stretch of >37 on the N terminus of the protein huntingtin (htt). polyglutamine 131-144 huntingtin Homo sapiens 196-206 16574233-7 2006 The G protein-uncoupling activity of optineurin appears to be facilitated by the presence of polyglutamine-expanded mutant huntingtin but not wild-type huntingtin. polyglutamine 93-106 huntingtin Homo sapiens 123-133 16595690-1 2006 Huntington disease is an inherited neurodegenerative disorder that is caused by expanded CAG trinucleotide repeats, resulting in a polyglutamine stretch of >37 on the N terminus of the protein huntingtin (htt). polyglutamine 131-144 huntingtin Homo sapiens 208-211 16380118-1 2006 N-terminal fragments of huntingtin containing an expanded polyglutamine stretch play an important role in the molecular pathogenesis of Huntington"s disease. polyglutamine 58-71 huntingtin Homo sapiens 24-34 16678490-6 2006 Our results are interesting not only because of the recent discovery of tubular protofibrils in experiments on aggregation of mutant huntingtin fragments containing expanded polyglutamine tracts but also because Perutz predicted that polyglutamine forms water filled nanotubes. polyglutamine 174-187 huntingtin Homo sapiens 133-143 16380118-6 2006 These findings suggest that especially an increased amount of monomeric form of small N-terminal mutant huntingtin fragments may facilitate aberrant interactions both with itself via the polyglutamine stretch and with other proteins and thereby contribute to molecular pathogenesis. polyglutamine 187-200 huntingtin Homo sapiens 104-114 16699519-3 2006 One hypothesis is that nucleation of protein aggregates containing exon I fragments of the mutant huntingtin protein (mhttex1), which contains an expanded polyglutamine region in patients with the disease, is the explanation for the infrequent but steady occurrence of neuronal death, resulting in adult onset of the disease. polyglutamine 155-168 huntingtin Homo sapiens 98-108 16932577-1 2006 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a polyglutamine repeat expansion within the huntingtin protein. polyglutamine 90-103 huntingtin Homo sapiens 132-142 16522639-1 2006 Intracellular accumulation of mutant Huntingtin with expanded polyglutamine provides a context-dependent cytotoxicity critical for the pathogenesis of Huntington disease (Everett, C. M., and Wood, N. W. (2004) Brain 127, 2385-2405). polyglutamine 62-75 huntingtin Homo sapiens 37-47 16524881-8 2006 We find that expansion of the polyglutamine segment beyond the pathological threshold (>35 glutamines) results in structural perturbation of the neighboring protein whether the huntingtin exon is N- or C-terminal. polyglutamine 30-43 huntingtin Homo sapiens 180-190 16473015-1 2006 Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine repeat in the huntingtin gene (Htt). polyglutamine 70-83 huntingtin Homo sapiens 98-108 16473015-1 2006 Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine repeat in the huntingtin gene (Htt). polyglutamine 70-83 huntingtin Homo sapiens 115-118 16472774-2 2006 A major hallmark of HD is the proteolytic production of N-terminal fragments of huntingtin containing polyglutamine repeats that form ubiquitinated aggregates in the nucleus and cytoplasm of the affected neurons. polyglutamine 102-115 huntingtin Homo sapiens 80-90 16452635-4 2006 We also examined several mitochondrial proteins in striatal neurons that were infected with lentiviral vectors coding for the N-terminus part of huntingtin (Htt) with either a pathological (Htt171-82Q) or physiological (Htt171-19Q) polyglutamine tract. polyglutamine 232-245 huntingtin Homo sapiens 145-155 16472774-4 2006 Here, we found that oxidative stimuli enhance the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-induced cell death. polyglutamine 50-63 huntingtin Homo sapiens 94-104 16472774-4 2006 Here, we found that oxidative stimuli enhance the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-induced cell death. polyglutamine 50-63 huntingtin Homo sapiens 113-123 16472774-4 2006 Here, we found that oxidative stimuli enhance the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-induced cell death. polyglutamine 50-63 huntingtin Homo sapiens 113-123 16492755-1 2006 The pathophysiology of Huntington"s disease reflects actions of mutant Huntingtin (Htt) (mHtt) protein with polyglutamine repeats, whose N-terminal fragment translocates to the nucleus to elicit neurotoxicity. polyglutamine 108-121 huntingtin Homo sapiens 71-81 16427603-1 2006 Huntington"s disease results from expansion of the polyglutamine (PolyQ) domain in the huntingtin protein. polyglutamine 51-64 huntingtin Homo sapiens 87-97 16427603-1 2006 Huntington"s disease results from expansion of the polyglutamine (PolyQ) domain in the huntingtin protein. polyglutamine 66-71 huntingtin Homo sapiens 87-97 16525063-0 2006 Differential contributions of Caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity. polyglutamine 88-101 huntingtin Homo sapiens 77-87 16525063-1 2006 Expansion of a polyglutamine tract in the huntingtin protein causes neuronal degeneration and death in Huntington"s disease patients, but the molecular mechanisms underlying polyglutamine-mediated cell death remain unclear. polyglutamine 15-28 huntingtin Homo sapiens 42-52 16525063-1 2006 Expansion of a polyglutamine tract in the huntingtin protein causes neuronal degeneration and death in Huntington"s disease patients, but the molecular mechanisms underlying polyglutamine-mediated cell death remain unclear. polyglutamine 174-187 huntingtin Homo sapiens 42-52 16525063-3 2006 We tested this hypothesis in Caenorhabditis elegans neurons expressing a human huntingtin fragment with an expanded polyglutamine tract (Htn-Q150). polyglutamine 116-129 huntingtin Homo sapiens 79-89 16369839-1 2006 An expanded polyglutamine stretch in the huntingtin protein has been identified as the pathogenetic cause of Huntington"s disease (HD). polyglutamine 12-25 huntingtin Homo sapiens 41-51 16416264-1 2006 Huntington"s disease (HD) is a fatal neurodegenerative disease caused by an expanded polyglutamine (polyQ) repeat in the protein huntingtin. polyglutamine 85-98 huntingtin Homo sapiens 129-139 16416264-1 2006 Huntington"s disease (HD) is a fatal neurodegenerative disease caused by an expanded polyglutamine (polyQ) repeat in the protein huntingtin. polyglutamine 100-105 huntingtin Homo sapiens 129-139 16492755-1 2006 The pathophysiology of Huntington"s disease reflects actions of mutant Huntingtin (Htt) (mHtt) protein with polyglutamine repeats, whose N-terminal fragment translocates to the nucleus to elicit neurotoxicity. polyglutamine 108-121 huntingtin Homo sapiens 83-86 16321399-4 2006 In HD, the N-terminal, exon-1 segment of the protein huntingtin contains the polyGln sequence immediately followed by an oligoproline region. polyglutamine 77-84 huntingtin Homo sapiens 53-63 16371362-4 2006 In this study, we use dynamic imaging analysis of living cells to compare the aggregation and growth properties of mutant huntingtin with polyglutamine expansions or mutant SOD1 (G85R/G93A) to examine the formation of aggregate structures and interactions with other cellular proteins. polyglutamine 138-151 huntingtin Homo sapiens 122-132 16274727-1 2006 Huntington"s disease (HD) is caused by a CAG repeat mutation translating as a polyglutamine (poly(Q)) expansion in the huntingtin protein, whose main pathogenic mechanism is a gain of toxic function. polyglutamine 78-91 huntingtin Homo sapiens 119-129 16274727-1 2006 Huntington"s disease (HD) is caused by a CAG repeat mutation translating as a polyglutamine (poly(Q)) expansion in the huntingtin protein, whose main pathogenic mechanism is a gain of toxic function. polyglutamine 93-100 huntingtin Homo sapiens 119-129 16336206-1 2006 HD (Huntington"s disease) is a devastating neurodegenerative disorder caused by a polyglutamine expansion in the gene encoding the huntingtin protein. polyglutamine 82-95 huntingtin Homo sapiens 131-141 16984809-3 2006 HD is an autosomal dominant genetic disorder caused by a CAG expansion in exon 1 of the HD gene, encoding an expanded polyglutamine (polyQ) tract near the N-terminus of the protein huntingtin. polyglutamine 118-131 huntingtin Homo sapiens 181-191 16984809-3 2006 HD is an autosomal dominant genetic disorder caused by a CAG expansion in exon 1 of the HD gene, encoding an expanded polyglutamine (polyQ) tract near the N-terminus of the protein huntingtin. polyglutamine 133-138 huntingtin Homo sapiens 181-191 16984809-7 2006 Consistent with this, evidence from vertebrate and invertebrate models of HD indicates that expression of the polyQ-expanded form of huntingtin results in early impairment of axonal transport and mitochondrial function. polyglutamine 110-115 huntingtin Homo sapiens 133-143 16377565-1 2005 Transcriptional dysregulation has emerged as a potentially important pathogenic mechanism in Huntington"s disease, a neurodegenerative disorder associated with polyglutamine expansion in the huntingtin (htt) protein. polyglutamine 160-173 huntingtin Homo sapiens 191-201 16377565-1 2005 Transcriptional dysregulation has emerged as a potentially important pathogenic mechanism in Huntington"s disease, a neurodegenerative disorder associated with polyglutamine expansion in the huntingtin (htt) protein. polyglutamine 160-173 huntingtin Homo sapiens 203-206 16377565-3 2005 We demonstrate that both gene-specific activator protein Sp1 and selective components of the core transcription apparatus, including TFIID and TFIIF, are direct targets inhibited by mutant htt in a polyglutamine-dependent manner. polyglutamine 198-211 huntingtin Homo sapiens 189-192 16085648-5 2005 N-terminal huntingtin fragments with an expanded polyglutamine tract aberrantly localized to intracellular regions instead of plasma membrane. polyglutamine 49-62 huntingtin Homo sapiens 11-21 16162412-2 2005 Htt is a widely expressed 350-kDa cytosolic protein bearing an N-terminal polyglutamine tract. polyglutamine 74-87 huntingtin Homo sapiens 0-3 16225422-1 2005 Huntington"s disease is a dominantly inherited, devastating neurodegenerative disorder, caused by a polyglutamine expansion (>37) in the N-terminal region of huntingtin, a protein of unknown function. polyglutamine 100-113 huntingtin Homo sapiens 161-171 16115810-5 2005 Intriguingly, expression of huntingtin, another polyglutamine protein interacting with endophilin-A3, was also toxic in Deltasac6 yeast. polyglutamine 48-61 huntingtin Homo sapiens 28-38 16040812-1 2005 Huntington"s disease is a progressive neurodegenerative disorder caused by a polyglutamine repeat expansion in the first exon of the huntingtin (Htt) protein. polyglutamine 77-90 huntingtin Homo sapiens 133-143 16181417-1 2005 Huntington"s disease resulting from huntingtin containing an expanded polyglutamine is associated with aggregates largely confined to neuronal inclusions, and with neuronal death. polyglutamine 70-83 huntingtin Homo sapiens 36-46 15968465-1 2005 Huntington"s disease (HD) is caused by a polyglutamine expansion in the protein huntingtin and is characterized by intraneuronal inclusions and widespread neuronal death at the late stage of the disease. polyglutamine 41-54 huntingtin Homo sapiens 80-90 16076956-1 2005 We have serendipitously established a mouse that expresses an N-terminal human huntingtin (htt) fragment with an expanded polyglutamine repeat (approximately 120) under the control of the endogenous human promoter (shortstop). polyglutamine 122-135 huntingtin Homo sapiens 79-89 16076956-1 2005 We have serendipitously established a mouse that expresses an N-terminal human huntingtin (htt) fragment with an expanded polyglutamine repeat (approximately 120) under the control of the endogenous human promoter (shortstop). polyglutamine 122-135 huntingtin Homo sapiens 91-94 16040812-1 2005 Huntington"s disease is a progressive neurodegenerative disorder caused by a polyglutamine repeat expansion in the first exon of the huntingtin (Htt) protein. polyglutamine 77-90 huntingtin Homo sapiens 145-148 16040812-2 2005 N-terminal Htt peptides with polyglutamine tracts in the pathological range (51-122 glutamines) form high-molecular-weight protein aggregates with fibrillar morphology in vitro, and they form discrete inclusion bodies in a cell-culture model. polyglutamine 29-42 huntingtin Homo sapiens 11-14 15809304-0 2005 Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. polyglutamine 56-61 huntingtin Homo sapiens 62-72 15967379-1 2005 Huntington"s Disease (HD) is a neurodegenerative disorder caused by an abnormally expanded polyglutamine trait in the amino-terminal region of huntingtin. polyglutamine 91-104 huntingtin Homo sapiens 143-153 15824100-1 2005 In yeast, aggregation and toxicity of the expanded polyglutamine fragment of human huntingtin strictly depend on the presence of the endogenous self-perpetuating aggregated proteins (prions), which contain glutamine/asparagine-rich domains. polyglutamine 51-64 huntingtin Homo sapiens 83-93 15809304-1 2005 Huntington disease (HD) is caused by an abnormal expanded polyglutamine repeat in the huntingtin protein. polyglutamine 58-71 huntingtin Homo sapiens 86-96 15837560-1 2005 Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington"s disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. polyglutamine 199-212 huntingtin Homo sapiens 28-38 15737634-1 2005 Huntington disease (HD) is a devastating neurologic disorder that is characterized by abnormal expansion of a CAG nt repeat in the first exon of the huntingtin (htt) gene, producing a mutant protein with an elongated polyglutamine stretch. polyglutamine 217-230 huntingtin Homo sapiens 161-164 16076022-2 2005 In patients with Huntington"s disease, there is a mutation in the gene encoding the protein huntingtin, which results in an expanded polyglutamine sequence leading to degeneration of the basal ganglia. polyglutamine 133-146 huntingtin Homo sapiens 92-102 15664989-3 2005 Here, we demonstrate that CHIP (C terminus of Hsp70-interacting protein) co-immunoprecipitates with the polyglutamine-expanded huntingtin or ataxin-3 and associates with their aggregates. polyglutamine 104-117 huntingtin Homo sapiens 127-137 15664989-4 2005 Transient overexpression of CHIP increases the ubiquitination and the rate of degradation of polyglutamine-expanded huntingtin or ataxin-3. polyglutamine 93-106 huntingtin Homo sapiens 116-126 15644269-2 2005 Given the ability of expanded polyglutamine (poly-Q) tract present in Htt protein to interact with other proteins and increased neuronal cell death by apoptosis, variations in the genes coding for htt-interacting proteins and those involved in apoptosis are likely to alter the AO in HD. polyglutamine 30-43 huntingtin Homo sapiens 70-73 15689354-1 2005 Huntington"s disease (HD) arises from an expanded polyglutamine (polyQ) in the N-terminus of the huntingtin (htt) protein. polyglutamine 50-63 huntingtin Homo sapiens 97-107 15689354-1 2005 Huntington"s disease (HD) arises from an expanded polyglutamine (polyQ) in the N-terminus of the huntingtin (htt) protein. polyglutamine 50-63 huntingtin Homo sapiens 109-112 15689354-1 2005 Huntington"s disease (HD) arises from an expanded polyglutamine (polyQ) in the N-terminus of the huntingtin (htt) protein. polyglutamine 65-70 huntingtin Homo sapiens 97-107 15689354-1 2005 Huntington"s disease (HD) arises from an expanded polyglutamine (polyQ) in the N-terminus of the huntingtin (htt) protein. polyglutamine 65-70 huntingtin Homo sapiens 109-112 17292058-1 2005 BACKGROUND: Huntington"s disease is an autosomal dominant progressive neurodegenerative disease associated with dramatic expansion of a polyglutamine sequence in exon 1 of the huntingtin protein htt that leads to cytoplasmic, and even nuclear aggregation of fibrils. polyglutamine 136-149 huntingtin Homo sapiens 176-186 17292058-1 2005 BACKGROUND: Huntington"s disease is an autosomal dominant progressive neurodegenerative disease associated with dramatic expansion of a polyglutamine sequence in exon 1 of the huntingtin protein htt that leads to cytoplasmic, and even nuclear aggregation of fibrils. polyglutamine 136-149 huntingtin Homo sapiens 195-198 15644269-2 2005 Given the ability of expanded polyglutamine (poly-Q) tract present in Htt protein to interact with other proteins and increased neuronal cell death by apoptosis, variations in the genes coding for htt-interacting proteins and those involved in apoptosis are likely to alter the AO in HD. polyglutamine 45-51 huntingtin Homo sapiens 70-73 15483602-1 2004 Huntington"s disease is caused by an abnormal polyglutamine expansion within the protein huntingtin and is characterized by microscopic inclusion bodies of aggregated huntingtin and by the death of selected types of neuron. polyglutamine 46-59 huntingtin Homo sapiens 89-99 16471265-3 2005 The defective gene in HD contains a trinucleotide CAG repeat expansion within its coding region that is expressed as a polyglutamine (polyQ) repeat in the protein huntingtin. polyglutamine 119-132 huntingtin Homo sapiens 163-173 16471265-3 2005 The defective gene in HD contains a trinucleotide CAG repeat expansion within its coding region that is expressed as a polyglutamine (polyQ) repeat in the protein huntingtin. polyglutamine 134-139 huntingtin Homo sapiens 163-173 15571981-1 2004 Huntington"s disease (HD), an inherited neurodegenerative disorder, is caused by an abnormal polyglutamine expansion in the huntingtin protein. polyglutamine 93-106 huntingtin Homo sapiens 124-134 15720212-5 2005 Certainly htt is required for cell survival and impairment of wild-type htt function can be involved in neurodegeneration, but considerable evidence also shows that trinucleotide repeat expansion into glutamine (polyQ domain) endows the protein with a newly acquired toxic activity. polyglutamine 212-217 huntingtin Homo sapiens 10-13 16362929-2 2005 HD is caused by a polyglutamine (polyQ) expansion in the protein huntingtin (Htt). polyglutamine 18-31 huntingtin Homo sapiens 65-75 16362929-2 2005 HD is caused by a polyglutamine (polyQ) expansion in the protein huntingtin (Htt). polyglutamine 18-31 huntingtin Homo sapiens 77-80 16362929-2 2005 HD is caused by a polyglutamine (polyQ) expansion in the protein huntingtin (Htt). polyglutamine 33-38 huntingtin Homo sapiens 65-75 16362929-2 2005 HD is caused by a polyglutamine (polyQ) expansion in the protein huntingtin (Htt). polyglutamine 33-38 huntingtin Homo sapiens 77-80 15629196-1 2005 Huntington"s disease is caused by a polyglutamine expansion in the protein huntingtin. polyglutamine 36-49 huntingtin Homo sapiens 75-85 15543156-3 2004 Here, we show by atomic force microscopy that a mutant huntingtin fragment with an expanded polyglutamine repeat forms spherical and annular oligomeric structures reminiscent of those formed by Abeta and alpha-synuclein. polyglutamine 92-105 huntingtin Homo sapiens 55-65 15459747-2 2004 Huntington"s disease (HD) is a late-onset neurodegenerative disorder that is caused by a CAG repeat expansion in the IT15 gene, which results in a long stretch of polyglutamine close to the amino-terminus of the HD protein huntingtin (htt). polyglutamine 163-176 huntingtin Homo sapiens 117-121 15456523-1 2004 Huntingtons disease (HD) is caused by an expansion of the polyglutamine tract in the protein named huntingtin. polyglutamine 58-71 huntingtin Homo sapiens 99-109 15459747-2 2004 Huntington"s disease (HD) is a late-onset neurodegenerative disorder that is caused by a CAG repeat expansion in the IT15 gene, which results in a long stretch of polyglutamine close to the amino-terminus of the HD protein huntingtin (htt). polyglutamine 163-176 huntingtin Homo sapiens 223-233 15459747-2 2004 Huntington"s disease (HD) is a late-onset neurodegenerative disorder that is caused by a CAG repeat expansion in the IT15 gene, which results in a long stretch of polyglutamine close to the amino-terminus of the HD protein huntingtin (htt). polyglutamine 163-176 huntingtin Homo sapiens 235-238 15367583-5 2004 Moreover, the Hsp70 mutant shows reduced mobility in the presence of diffusive huntingtin fragments with expanded polyglutamine repeats. polyglutamine 114-127 huntingtin Homo sapiens 79-89 15474886-1 2004 Huntington"s disease is an inherited neurodegenerative disorder due to a mutation in exon 1 of the Huntingtin gene that encodes a stretch of polyglutamine (polyQ) residues close to the N-terminus of the huntingtin protein. polyglutamine 141-154 huntingtin Homo sapiens 99-109 15474886-1 2004 Huntington"s disease is an inherited neurodegenerative disorder due to a mutation in exon 1 of the Huntingtin gene that encodes a stretch of polyglutamine (polyQ) residues close to the N-terminus of the huntingtin protein. polyglutamine 141-154 huntingtin Homo sapiens 203-213 15474886-1 2004 Huntington"s disease is an inherited neurodegenerative disorder due to a mutation in exon 1 of the Huntingtin gene that encodes a stretch of polyglutamine (polyQ) residues close to the N-terminus of the huntingtin protein. polyglutamine 156-161 huntingtin Homo sapiens 99-109 15474886-1 2004 Huntington"s disease is an inherited neurodegenerative disorder due to a mutation in exon 1 of the Huntingtin gene that encodes a stretch of polyglutamine (polyQ) residues close to the N-terminus of the huntingtin protein. polyglutamine 156-161 huntingtin Homo sapiens 203-213 15474886-3 2004 The mechanisms by which aggregated polyQ induces neurodegeneration include the binding of abnormal huntingtin to cyclic adenosine monophosphate response element binding protein, which hampers its ability to turn on transcription of other genes; mutant huntingtin binding to the active site on the cyclic adenosine monophosphate response element binding protein, which is essential for its acetyltransferase activity and, hence, the drugs that inhibit histone deacetylase arrest polyQ-dependent neurodegeneration; and/or disrupting the ubiquitin-proteasome system. polyglutamine 35-40 huntingtin Homo sapiens 99-109 15474886-3 2004 The mechanisms by which aggregated polyQ induces neurodegeneration include the binding of abnormal huntingtin to cyclic adenosine monophosphate response element binding protein, which hampers its ability to turn on transcription of other genes; mutant huntingtin binding to the active site on the cyclic adenosine monophosphate response element binding protein, which is essential for its acetyltransferase activity and, hence, the drugs that inhibit histone deacetylase arrest polyQ-dependent neurodegeneration; and/or disrupting the ubiquitin-proteasome system. polyglutamine 35-40 huntingtin Homo sapiens 252-262 15140195-0 2004 Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity. polyglutamine 39-52 huntingtin Homo sapiens 11-21 15906159-1 2004 Huntington"s disease (HD) is caused by a polyglutamine repeat expansion in the N-terminus of the huntingtin protein. polyglutamine 41-54 huntingtin Homo sapiens 97-107 15242639-1 2004 Huntington"s disease is a progressive autosomal dominant neurodegenerative disorder caused by expansion of a CAG repeat coding for polyglutamine in the huntingtin protein. polyglutamine 131-144 huntingtin Homo sapiens 152-162 15242649-1 2004 Polyglutamine expansion (polyQ) in the protein huntingtin is pathogenic and responsible for the neuronal toxicity associated with Huntington"s disease (HD). polyglutamine 0-13 huntingtin Homo sapiens 47-57 15242649-1 2004 Polyglutamine expansion (polyQ) in the protein huntingtin is pathogenic and responsible for the neuronal toxicity associated with Huntington"s disease (HD). polyglutamine 25-30 huntingtin Homo sapiens 47-57 15225551-3 2004 We show, in vitro and in cells, that monomers or small soluble oligomers of huntingtin exon1 accumulate in the nucleus and inhibit the function of TBP in a polyQ-dependent manner. polyglutamine 156-161 huntingtin Homo sapiens 76-86 15225551-5 2004 Interaction of toxic huntingtin with the benign polyQ repeat of TBP structurally destabilizes the transcription factor, independent of the formation of insoluble coaggregates. polyglutamine 48-53 huntingtin Homo sapiens 21-31 15210964-2 2004 The huntingtin amino-terminal fragment with extended polyglutamine repeat forms aggregates closely associated with chaperones both in the cytoplasm and the nucleus. polyglutamine 53-66 huntingtin Homo sapiens 4-14 15140195-4 2004 We fused the first 171 amino acids of huntingtin, containing either a pathogenic or normal polyglutamine tract, to the enhanced green fluorescent protein (EGFP). polyglutamine 91-104 huntingtin Homo sapiens 38-48 14978262-5 2004 Huntingtin aggregates sequester other expanded polyglutamine proteins in the cytoplasm and lead to disruption of axonal transport and accumulation of aggregates at synapses. polyglutamine 47-60 huntingtin Homo sapiens 0-10 14557053-1 2003 Huntington"s disease (HD) is caused by a polyglutamine expansion in the protein huntingtin. polyglutamine 41-54 huntingtin Homo sapiens 80-90 15201452-8 2004 We have developed monoclonal antibodies that specifically recognize expanded polyglutamine stretches in mutant huntingtin. polyglutamine 77-90 huntingtin Homo sapiens 111-121 14570907-10 2003 These results indicate that CSP"s modulation of G protein inhibition of calcium channel activity is blocked in the presence of a huntingtin fragment with expanded polyglutamine tracts. polyglutamine 163-176 huntingtin Homo sapiens 129-139 14674843-1 2003 The Huntington"s disease R6/2 transgenic mouse model, containing exon 1 of the human huntingtin gene with a greatly increased CAG repeat length, shows multiple effects of the altered polyglutamine in the resultant protein. polyglutamine 183-196 huntingtin Homo sapiens 85-95 15036808-3 2004 A gain of toxic function as a result of an expanded polyglutamine tract can cause the protein huntingtin to interact abnormally with a variety of proteins, resulting in the complex of neuropathological changes seen in Huntington"s disease. polyglutamine 52-65 huntingtin Homo sapiens 94-104 14715959-1 2004 Polyglutamine expansion in the N terminus of huntingtin (htt) causes selective neuronal dysfunction and cell death by unknown mechanisms. polyglutamine 0-13 huntingtin Homo sapiens 45-55 14715959-1 2004 Polyglutamine expansion in the N terminus of huntingtin (htt) causes selective neuronal dysfunction and cell death by unknown mechanisms. polyglutamine 0-13 huntingtin Homo sapiens 57-60 14715959-6 2004 Removal of a series of prolines adjacent to the polyglutamine region in htt blocked formation of the shell of the htt body and redistribution of dynamin, HIP1, SH3GL3, and proteasome to it. polyglutamine 48-61 huntingtin Homo sapiens 72-75 14715959-6 2004 Removal of a series of prolines adjacent to the polyglutamine region in htt blocked formation of the shell of the htt body and redistribution of dynamin, HIP1, SH3GL3, and proteasome to it. polyglutamine 48-61 huntingtin Homo sapiens 114-117 14725621-1 2004 Huntington"s disease (HD) is caused by abnormal polyglutamine (polyQ) expansion in the protein huntingtin. polyglutamine 48-61 huntingtin Homo sapiens 95-105 14725621-1 2004 Huntington"s disease (HD) is caused by abnormal polyglutamine (polyQ) expansion in the protein huntingtin. polyglutamine 63-68 huntingtin Homo sapiens 95-105 14725621-6 2004 We show that SGK phosphorylates huntingtin at serine 421 and that phosphorylation can protect striatal neurons against polyQ-huntingtin-induced toxicity. polyglutamine 119-124 huntingtin Homo sapiens 125-135 14570716-1 2003 The N-terminus of mutant huntingtin (htt) has a polyglutamine expansion and forms neuronal aggregates in the brain of Huntington"s disease (HD) patients. polyglutamine 48-61 huntingtin Homo sapiens 25-35 14570716-1 2003 The N-terminus of mutant huntingtin (htt) has a polyglutamine expansion and forms neuronal aggregates in the brain of Huntington"s disease (HD) patients. polyglutamine 48-61 huntingtin Homo sapiens 37-40 12888569-2 2003 Previously, we have shown that mutant htt fragments with polyglutamine (polyQ) tracts in the pathological range (>37 glutamines) form SDS-resistant aggregates with a fibrillar morphology, whereas wild-type htt fragments with normal polyQ domains do not aggregate. polyglutamine 57-70 huntingtin Homo sapiens 38-41 12888569-2 2003 Previously, we have shown that mutant htt fragments with polyglutamine (polyQ) tracts in the pathological range (>37 glutamines) form SDS-resistant aggregates with a fibrillar morphology, whereas wild-type htt fragments with normal polyQ domains do not aggregate. polyglutamine 72-77 huntingtin Homo sapiens 38-41 12888569-2 2003 Previously, we have shown that mutant htt fragments with polyglutamine (polyQ) tracts in the pathological range (>37 glutamines) form SDS-resistant aggregates with a fibrillar morphology, whereas wild-type htt fragments with normal polyQ domains do not aggregate. polyglutamine 232-237 huntingtin Homo sapiens 38-41 14521962-2 2003 Once expressed, the expanded poly Q region of the huntingtin protein (Htt), which is normally soluble, becomes insoluble, leading to the formation of intracellular inclusions and ultimately to neuronal degeneration. polyglutamine 29-35 huntingtin Homo sapiens 50-60 14521962-2 2003 Once expressed, the expanded poly Q region of the huntingtin protein (Htt), which is normally soluble, becomes insoluble, leading to the formation of intracellular inclusions and ultimately to neuronal degeneration. polyglutamine 29-35 huntingtin Homo sapiens 70-73 14521962-3 2003 Interruption of the pure poly Q tract at the genetic level should undermine the transition from Htt solubility to Htt insolubility. polyglutamine 25-31 huntingtin Homo sapiens 96-99 14521962-3 2003 Interruption of the pure poly Q tract at the genetic level should undermine the transition from Htt solubility to Htt insolubility. polyglutamine 25-31 huntingtin Homo sapiens 114-117 14529364-2 2003 HD is one of several progressive neurodegenerative disorders, in which the underlying mutation is a CAG expansion encoding a polyglutamine tract in a specific protein, which in the case of HD, is called huntingtin. polyglutamine 125-138 huntingtin Homo sapiens 203-213 12810713-9 2003 Taken together, our studies show that polyglutamine-expanded huntingtin increases tyrosine phosphorylation of NMDA receptors via PSD-95 and Src, and increased tyrosine phosphorylation may contribute to the sensitization of the receptors mediated by polyglutamine-expanded huntingtin. polyglutamine 38-51 huntingtin Homo sapiens 61-71 12810713-0 2003 Expression of polyglutamine-expanded huntingtin induces tyrosine phosphorylation of N-methyl-D-aspartate receptors. polyglutamine 14-27 huntingtin Homo sapiens 37-47 12810713-1 2003 In our previous studies, we found that expression of polyglutamine-expanded huntingtin in HN33 cells induced sensitization of N-methyl-D-aspartate (NMDA) receptors (Sun, Y., Savinainen, A., and Liu, Y. F. (2001) J. Biol. polyglutamine 53-66 huntingtin Homo sapiens 76-86 12810713-5 2003 Expression of polyglutamine-expanded huntingtin induced elevation of phosphorylated or activated Src and increased targeting of PSD-95 (post-synaptic density 95) and activated Src to cell surface membrane. polyglutamine 14-27 huntingtin Homo sapiens 37-47 12810713-9 2003 Taken together, our studies show that polyglutamine-expanded huntingtin increases tyrosine phosphorylation of NMDA receptors via PSD-95 and Src, and increased tyrosine phosphorylation may contribute to the sensitization of the receptors mediated by polyglutamine-expanded huntingtin. polyglutamine 38-51 huntingtin Homo sapiens 272-282 12810713-9 2003 Taken together, our studies show that polyglutamine-expanded huntingtin increases tyrosine phosphorylation of NMDA receptors via PSD-95 and Src, and increased tyrosine phosphorylation may contribute to the sensitization of the receptors mediated by polyglutamine-expanded huntingtin. polyglutamine 249-262 huntingtin Homo sapiens 61-71 12486229-0 2002 Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans neurons from huntingtin polyglutamine neurotoxicity. polyglutamine 93-106 huntingtin Homo sapiens 82-92 12932731-1 2003 Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormally elongated polyglutamine (polyQ) tract in the large protein huntingtin (htt). polyglutamine 107-112 huntingtin Homo sapiens 153-156 12873376-1 2003 Huntingtin, a protein altered by polyglutamine expansion in Huntington"s disease (Httexp), forms a signaling complex with the InsP3R, an intracellular calcium channel, and Htt-associated protein 1A (HAP1A). polyglutamine 33-46 huntingtin Homo sapiens 0-10 12873381-1 2003 Huntington"s disease (HD) is caused by polyglutamine expansion (exp) in huntingtin (Htt). polyglutamine 39-52 huntingtin Homo sapiens 72-82 12873381-1 2003 Huntington"s disease (HD) is caused by polyglutamine expansion (exp) in huntingtin (Htt). polyglutamine 39-52 huntingtin Homo sapiens 84-87 12783847-2 2003 CAG DNA expansion results in a polyglutamine tract expansion in mutant huntingtin protein. polyglutamine 31-44 huntingtin Homo sapiens 71-81 12797118-2 2003 The repeat encodes an expanded polyglutamine tract in the protein huntingtin. polyglutamine 31-44 huntingtin Homo sapiens 66-76 12747895-1 2003 CONTEXT: Huntington"s disease is a late onset neurodegenerative disorder for which the mutation is a CAG/polyglutamine (polyQ) repeat expansion in the gene encoding the huntingtin protein. polyglutamine 105-118 huntingtin Homo sapiens 169-179 12747895-1 2003 CONTEXT: Huntington"s disease is a late onset neurodegenerative disorder for which the mutation is a CAG/polyglutamine (polyQ) repeat expansion in the gene encoding the huntingtin protein. polyglutamine 120-125 huntingtin Homo sapiens 169-179 12711212-1 2003 Huntington disease (HD) is caused by a CAG repeat expansion that is translated into an abnormally long polyglutamine (polyQ) tract in the huntingtin protein. polyglutamine 103-116 huntingtin Homo sapiens 138-148 12711212-1 2003 Huntington disease (HD) is caused by a CAG repeat expansion that is translated into an abnormally long polyglutamine (polyQ) tract in the huntingtin protein. polyglutamine 118-123 huntingtin Homo sapiens 138-148 12641738-1 2003 Huntington"s disease (HD) is caused by an expansion of a polyglutamine (polyQ) tract within huntingtin (htt) protein. polyglutamine 57-70 huntingtin Homo sapiens 92-102 12641738-1 2003 Huntington"s disease (HD) is caused by an expansion of a polyglutamine (polyQ) tract within huntingtin (htt) protein. polyglutamine 57-70 huntingtin Homo sapiens 104-107 12641738-1 2003 Huntington"s disease (HD) is caused by an expansion of a polyglutamine (polyQ) tract within huntingtin (htt) protein. polyglutamine 72-77 huntingtin Homo sapiens 92-102 12641738-1 2003 Huntington"s disease (HD) is caused by an expansion of a polyglutamine (polyQ) tract within huntingtin (htt) protein. polyglutamine 72-77 huntingtin Homo sapiens 104-107 12641738-2 2003 To examine the cytotoxic effects of polyQ-expanded htt, we overexpressed an enhanced green fluorescent protein (EGFP)-tagged N-terminal fragment of htt with 150 glutamine residues (Nhtt150Q-EGFP) in Aplysia neurons. polyglutamine 36-41 huntingtin Homo sapiens 51-54 12641738-2 2003 To examine the cytotoxic effects of polyQ-expanded htt, we overexpressed an enhanced green fluorescent protein (EGFP)-tagged N-terminal fragment of htt with 150 glutamine residues (Nhtt150Q-EGFP) in Aplysia neurons. polyglutamine 36-41 huntingtin Homo sapiens 148-151 12604778-1 2003 Huntington"s disease (HD) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). polyglutamine 67-80 huntingtin Homo sapiens 114-124 12604778-1 2003 Huntington"s disease (HD) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). polyglutamine 67-80 huntingtin Homo sapiens 126-129 12604778-1 2003 Huntington"s disease (HD) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). polyglutamine 82-87 huntingtin Homo sapiens 114-124 12604778-1 2003 Huntington"s disease (HD) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). polyglutamine 82-87 huntingtin Homo sapiens 126-129 12895502-6 2003 These observations suggest that expression of expanded polyglutamine-containing huntingtin does not acutely alter the vulnerability of cortical neurons to excitotoxic, oxidative or apoptotic insults. polyglutamine 55-68 huntingtin Homo sapiens 80-90 14585171-2 2003 The expanded repeats are translated into an abnormally long polyglutamine tract close to the N-terminus of the HD gene product ("huntingtin"). polyglutamine 60-73 huntingtin Homo sapiens 129-140 14585171-4 2003 Several studies have suggested that the large huntingtin protein is cleaved to produce a shorter N-terminal fragment containing the polyglutamine expansion, and that the polyglutamine expansion causes the protein fragment to misfold and form aggregates (inclusions) in the nuclei and processes of neurons. polyglutamine 132-145 huntingtin Homo sapiens 46-56 12932731-1 2003 Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormally elongated polyglutamine (polyQ) tract in the large protein huntingtin (htt). polyglutamine 92-105 huntingtin Homo sapiens 141-151 12932731-1 2003 Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormally elongated polyglutamine (polyQ) tract in the large protein huntingtin (htt). polyglutamine 92-105 huntingtin Homo sapiens 153-156 12932731-1 2003 Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormally elongated polyglutamine (polyQ) tract in the large protein huntingtin (htt). polyglutamine 107-112 huntingtin Homo sapiens 141-151 12791042-2 2003 The diagnosis of HD is based on family history, characteristic clinical findings, and the detection of an expansion of a CAG polyglutamine tract in the Huntingtin gene. polyglutamine 125-138 huntingtin Homo sapiens 152-162 15206726-1 2003 Huntington"s Disease (HD), an inherited neurodegenerative disorder, is caused by an abnormal polyglutamine extension of a protein named huntingtin. polyglutamine 93-106 huntingtin Homo sapiens 136-146 14528049-2 2003 Molecular genetics has revealed the disease trigger, an inherited unstable CAG expansion in a novel 4p16.3 gene (HD), that lengthens a polyglutamine segment in huntingtin. polyglutamine 135-148 huntingtin Homo sapiens 160-170 12486229-1 2002 Huntington"s disease is a progressive neurodegenerative disease caused by a polyglutamine (polyQ) repeat expansion in the huntingtin protein [Huntington"s Disease Collaborative Research Group (1993) Cell 72, 971-983]. polyglutamine 76-89 huntingtin Homo sapiens 122-132 12486229-1 2002 Huntington"s disease is a progressive neurodegenerative disease caused by a polyglutamine (polyQ) repeat expansion in the huntingtin protein [Huntington"s Disease Collaborative Research Group (1993) Cell 72, 971-983]. polyglutamine 91-96 huntingtin Homo sapiens 122-132 12486229-3 2002 In our model, expression of N-terminal fragments of human huntingtin causes polyQ-dependent degeneration of neurons. polyglutamine 76-81 huntingtin Homo sapiens 58-68 12171927-0 2002 Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. polyglutamine 55-68 huntingtin Homo sapiens 0-10 12466534-1 2002 Expansion of a CAG tract within the huntingtin gene, leading to the production of a protein with an expanded polyglutamine tract, is responsible for Huntington"s disease. polyglutamine 109-122 huntingtin Homo sapiens 36-46 12200414-1 2002 Huntington"s disease (HD) is caused by a polyglutamine expansion in the amino-terminal region of huntingtin. polyglutamine 41-54 huntingtin Homo sapiens 97-107 12354780-1 2002 Huntington"s disease (HD) is caused by a pathological expansion of a CAG repeat in the first exon of the gene coding for huntingtin, resulting in an abnormally long polyglutamine stretch. polyglutamine 165-178 huntingtin Homo sapiens 121-131 12460551-0 2002 Polyglutamine repeat length-dependent proteolysis of huntingtin. polyglutamine 0-13 huntingtin Homo sapiens 53-63 12460551-1 2002 Amino-terminal fragments of huntingtin, which contain the expanded polyglutamine repeat, have been proposed to contribute to the pathology of Huntington"s disease (HD). polyglutamine 67-80 huntingtin Homo sapiens 28-38 12460551-2 2002 Data supporting this claim have been generated from patients with HD in which truncated amino-terminal fragments forming intranuclear inclusions have been observed, and from animal and cell-based models of HD where it has been demonstrated that truncated polyglutamine-containing fragments of htt are more toxic than full-length huntingtin. polyglutamine 255-268 huntingtin Homo sapiens 293-296 12460551-2 2002 Data supporting this claim have been generated from patients with HD in which truncated amino-terminal fragments forming intranuclear inclusions have been observed, and from animal and cell-based models of HD where it has been demonstrated that truncated polyglutamine-containing fragments of htt are more toxic than full-length huntingtin. polyglutamine 255-268 huntingtin Homo sapiens 329-339 12460551-4 2002 Importantly, proteolytic cleavage within this region appears dependent upon the length of the polyglutamine repeat within huntingtin, with pathological polyglutamine repeat-containing huntingtin being more efficiently cleaved than huntingtin containing polyglutamine repeats of nonpathological size. polyglutamine 94-107 huntingtin Homo sapiens 122-132 12460551-4 2002 Importantly, proteolytic cleavage within this region appears dependent upon the length of the polyglutamine repeat within huntingtin, with pathological polyglutamine repeat-containing huntingtin being more efficiently cleaved than huntingtin containing polyglutamine repeats of nonpathological size. polyglutamine 94-107 huntingtin Homo sapiens 184-194 12460551-4 2002 Importantly, proteolytic cleavage within this region appears dependent upon the length of the polyglutamine repeat within huntingtin, with pathological polyglutamine repeat-containing huntingtin being more efficiently cleaved than huntingtin containing polyglutamine repeats of nonpathological size. polyglutamine 94-107 huntingtin Homo sapiens 184-194 12460551-4 2002 Importantly, proteolytic cleavage within this region appears dependent upon the length of the polyglutamine repeat within huntingtin, with pathological polyglutamine repeat-containing huntingtin being more efficiently cleaved than huntingtin containing polyglutamine repeats of nonpathological size. polyglutamine 152-165 huntingtin Homo sapiens 122-132 12460551-4 2002 Importantly, proteolytic cleavage within this region appears dependent upon the length of the polyglutamine repeat within huntingtin, with pathological polyglutamine repeat-containing huntingtin being more efficiently cleaved than huntingtin containing polyglutamine repeats of nonpathological size. polyglutamine 152-165 huntingtin Homo sapiens 184-194 12460551-4 2002 Importantly, proteolytic cleavage within this region appears dependent upon the length of the polyglutamine repeat within huntingtin, with pathological polyglutamine repeat-containing huntingtin being more efficiently cleaved than huntingtin containing polyglutamine repeats of nonpathological size. polyglutamine 152-165 huntingtin Homo sapiens 184-194 12223539-1 2002 Huntington"s disease (HD) results from polyglutamine expansion in huntingtin (htt), a protein with several consensus caspase cleavage sites. polyglutamine 39-52 huntingtin Homo sapiens 66-76 12270644-5 2002 The reduction in aggregation of mutant huntingtin by GroEL/GroES was associated with protection against polyglutamine-induced cell death. polyglutamine 104-117 huntingtin Homo sapiens 39-49 12223539-1 2002 Huntington"s disease (HD) results from polyglutamine expansion in huntingtin (htt), a protein with several consensus caspase cleavage sites. polyglutamine 39-52 huntingtin Homo sapiens 78-81 12106904-1 2002 The presence of an expanded polyglutamine produces a toxic gain of function in huntingtin. polyglutamine 28-41 huntingtin Homo sapiens 79-89 12091468-8 2002 In juvenile HD lymphoblasts, the presence of a 66-kDa, instead of the 63-64 kDa N-domain htt fragment, may be consistent with the larger polyglutamine expansion of mutant htt in the juvenile case of HD. polyglutamine 137-150 huntingtin Homo sapiens 171-174 12077181-8 2002 The rate of cleavage of Htt by calpain was polyglutamine-length-dependent. polyglutamine 43-56 huntingtin Homo sapiens 24-27 12165556-7 2002 These findings suggest that htt protein length influences the ability of an expanded polyglutamine domain to alter gene expression. polyglutamine 85-98 huntingtin Homo sapiens 28-31 11988536-1 2002 Huntington"s disease (HD) is an inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein. polyglutamine 93-106 huntingtin Homo sapiens 120-130 11739372-6 2002 Full-length huntingtin co-immunoprecipitated with the transcriptional corepressor C-terminal binding protein, and polyglutamine expansion in huntingtin reduced this interaction. polyglutamine 114-127 huntingtin Homo sapiens 12-22 11739372-6 2002 Full-length huntingtin co-immunoprecipitated with the transcriptional corepressor C-terminal binding protein, and polyglutamine expansion in huntingtin reduced this interaction. polyglutamine 114-127 huntingtin Homo sapiens 141-151 11788820-1 2002 In Huntington disease, polyglutamine expansion of the protein huntingtin (Htt) leads to selective neurodegenerative loss of medium spiny neurons throughout the striatum by an unknown apoptotic mechanism. polyglutamine 23-36 huntingtin Homo sapiens 62-72 11788820-1 2002 In Huntington disease, polyglutamine expansion of the protein huntingtin (Htt) leads to selective neurodegenerative loss of medium spiny neurons throughout the striatum by an unknown apoptotic mechanism. polyglutamine 23-36 huntingtin Homo sapiens 74-77 11788820-2 2002 Binding of Hip-1, a protein normally associated with Htt, is reduced by polyglutamine expansion. polyglutamine 72-85 huntingtin Homo sapiens 53-56 11788820-4 2002 The availability of free Hip-1 is modulated by polyglutamine length within Htt, with disease-associated polyglutamine expansion favouring the formation of pro-apoptotic Hippi-Hip-1 heterodimers. polyglutamine 47-60 huntingtin Homo sapiens 75-78 11788820-4 2002 The availability of free Hip-1 is modulated by polyglutamine length within Htt, with disease-associated polyglutamine expansion favouring the formation of pro-apoptotic Hippi-Hip-1 heterodimers. polyglutamine 104-117 huntingtin Homo sapiens 75-78 11788820-6 2002 We propose that Htt polyglutamine expansion liberates Hip-1 so that it can form a caspase-8 recruitment complex with Hippi. polyglutamine 20-33 huntingtin Homo sapiens 16-19 11738471-4 2002 Huntington"s disease is a genetic disorder caused by an expansion of the polyglutamine domain in the huntingtin protein. polyglutamine 73-86 huntingtin Homo sapiens 101-111 11792860-1 2002 We have generated eight mAbs (MW1-8) that bind the epitopes polyglutamine (polyQ), polyproline (polyP), or the C terminus of exon 1 in huntingtin (htt) protein. polyglutamine 75-80 huntingtin Homo sapiens 135-145 11792860-7 2002 In contrast, MW1 and MW2 scFvs, recognizing the polyQ stretch, stimulate htt aggregation and apoptosis. polyglutamine 48-53 huntingtin Homo sapiens 73-76 11319238-0 2001 Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95. polyglutamine 0-13 huntingtin Homo sapiens 23-33 11719262-1 2001 Extended tracts of polyglutamine (PG) have been implicated in the pathogenicity of the mutant protein huntingtin and have been shown to form ion channels in planar lipid bilayers. polyglutamine 19-32 huntingtin Homo sapiens 102-112 11719262-1 2001 Extended tracts of polyglutamine (PG) have been implicated in the pathogenicity of the mutant protein huntingtin and have been shown to form ion channels in planar lipid bilayers. polyglutamine 34-36 huntingtin Homo sapiens 102-112 11739625-1 2001 Pathological-length polyglutamine (Q(n)) expansions, such as those that occur in the huntingtin protein (htt) in Huntington"s disease (HD), are excellent substrates for tissue transglutaminase in vitro, and transglutaminase activity is increased in post-mortem HD brain. polyglutamine 20-33 huntingtin Homo sapiens 85-95 11739625-1 2001 Pathological-length polyglutamine (Q(n)) expansions, such as those that occur in the huntingtin protein (htt) in Huntington"s disease (HD), are excellent substrates for tissue transglutaminase in vitro, and transglutaminase activity is increased in post-mortem HD brain. polyglutamine 20-33 huntingtin Homo sapiens 105-108 11687635-1 2001 Huntington"s disease (HD) is a dominant neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). polyglutamine 76-89 huntingtin Homo sapiens 135-138 11687635-1 2001 Huntington"s disease (HD) is a dominant neurodegenerative disease caused by polyglutamine (polyQ) expansion in the protein huntingtin (htt). polyglutamine 91-96 huntingtin Homo sapiens 135-138 11687635-4 2001 To explore polyQ-mediated neuronal toxicity, we expressed the first 57 amino acids of human htt containing normal [19 Gln residues (Glns)] and expanded (88 or 128 Glns) polyQ fused to fluorescent marker proteins in the six touch receptor neurons of Caenorhabditis elegans. polyglutamine 169-174 huntingtin Homo sapiens 92-95 11675509-1 2001 The Huntington"s disease (HD) mutation is a polyglutamine expansion in the N-terminal region of huntingtin (N-htt). polyglutamine 44-57 huntingtin Homo sapiens 96-106 11517213-1 2001 Polyglutamine expansion in huntingtin is the underlying mutation leading to neurodegeneration in Huntington disease. polyglutamine 0-13 huntingtin Homo sapiens 27-37 11319238-4 2001 However, how polyglutamine expansion in huntingtin promotes glutamate-mediated excitotoxicity remains a mystery. polyglutamine 13-26 huntingtin Homo sapiens 40-50 11319238-5 2001 In this study we provide evidence that (i) normal huntingtin is associated with N-methyl-d-aspartate (NMDA) and kainate receptors via postsynaptic density 95 (PSD-95), (ii) the SH3 domain of PSD-95 mediates its binding to huntingtin, and (iii) polyglutamine expansion interferes with the ability of huntingtin to interact with PSD-95. polyglutamine 244-257 huntingtin Homo sapiens 50-60 11319238-6 2001 The expression of polyglutamine-expanded huntingtin causes sensitization of NMDA receptors and promotes neuronal apoptosis induced by glutamate. polyglutamine 18-31 huntingtin Homo sapiens 41-51 11319238-7 2001 The addition of the NMDA receptor antagonist significantly attenuates neuronal toxicity induced by glutamate and polyglutamine-expanded huntingtin. polyglutamine 113-126 huntingtin Homo sapiens 136-146 11319238-9 2001 Our results demonstrate that polyglutamine expansion impairs the ability of huntingtin to bind PSD-95 and inhibits glutamate-mediated excitotoxicity. polyglutamine 29-42 huntingtin Homo sapiens 76-86 11442349-1 2001 The cause of Huntington"s disease (HD) is a pathological expansion of the polyglutamine domain within the N-terminal region of huntingtin. polyglutamine 74-87 huntingtin Homo sapiens 127-137 11442349-3 2001 However, how the expanded polyglutamine repeats of mutant huntingtin cause HD is not known. polyglutamine 26-39 huntingtin Homo sapiens 58-68 11296304-2 2001 HD is characterized by abnormally elongated polyglutamine near the N terminus of the huntingtin protein, which induces pathological protein-protein interactions and aggregate formation by huntingtin or its exon 1-containing fragments. polyglutamine 44-57 huntingtin Homo sapiens 85-95 11389766-1 2001 In Huntington"s Disease (HD), the huntingtin protein (Htt) includes an expanded polyglutamine domain. polyglutamine 80-93 huntingtin Homo sapiens 34-44 11389766-1 2001 In Huntington"s Disease (HD), the huntingtin protein (Htt) includes an expanded polyglutamine domain. polyglutamine 80-93 huntingtin Homo sapiens 54-57 11389766-5 2001 Considering that polyglutamine tracts stimulate caspase activation, mutant Htt is therefore poised to enter the nucleus. polyglutamine 17-30 huntingtin Homo sapiens 75-78 11375494-4 2001 Transient expression of two unrelated aggregation-prone proteins, a huntingtin fragment containing a pathogenic polyglutamine repeat and a folding mutant of cystic fibrosis transmembrane conductance regulator, caused nearly complete inhibition of the ubiquitin-proteasome system. polyglutamine 112-125 huntingtin Homo sapiens 68-78 11352944-2 2001 In several neurodegenerative diseases, such IBs can be formed by proteins with expanded polyglutamine (polyQ) domains (e.g., huntingtin). polyglutamine 88-101 huntingtin Homo sapiens 125-135 11352944-2 2001 In several neurodegenerative diseases, such IBs can be formed by proteins with expanded polyglutamine (polyQ) domains (e.g., huntingtin). polyglutamine 103-108 huntingtin Homo sapiens 125-135 11352944-7 2001 The polyQ-containing huntingtin fragment exists in cells in two distinct forms: (a) in a discrete soluble complex, and (b) in association with insoluble fraction. polyglutamine 4-9 huntingtin Homo sapiens 21-31 11278258-2 2001 The disease is caused by the expansion of a polyglutamine sequence in the N terminus of Huntingtin (Htt), a widely expressed protein. polyglutamine 44-57 huntingtin Homo sapiens 88-98 11278258-2 2001 The disease is caused by the expansion of a polyglutamine sequence in the N terminus of Huntingtin (Htt), a widely expressed protein. polyglutamine 44-57 huntingtin Homo sapiens 100-103 11359930-1 2001 The huntingtin exon 1 proteins with a polyglutamine repeat in the pathological range (51 or 83 glutamines), but not with a polyglutamine tract in the normal range (20 glutamines), form aggresome-like perinuclear inclusions in human 293 Tet-Off cells. polyglutamine 38-51 huntingtin Homo sapiens 4-14 11278395-8 2001 Furthermore, dominant-negative MLK2 blocked apoptosis induced by polyglutamine-expanded huntingtin protein, the product of the mutant Huntington"s disease gene. polyglutamine 65-78 huntingtin Homo sapiens 88-98 11296304-2 2001 HD is characterized by abnormally elongated polyglutamine near the N terminus of the huntingtin protein, which induces pathological protein-protein interactions and aggregate formation by huntingtin or its exon 1-containing fragments. polyglutamine 44-57 huntingtin Homo sapiens 188-198 11296304-3 2001 Selection from a large human phage display library yielded a single-chain Fv (sFv) antibody specific for the 17 N-terminal residues of huntingtin, adjacent to the polyglutamine in HD exon 1. polyglutamine 163-176 huntingtin Homo sapiens 135-145 11285271-1 2001 The cause of Huntington"s disease (HD) is a pathological expansion of the polyglutamine domain within the NH(2)-terminal region of huntingtin. polyglutamine 74-87 huntingtin Homo sapiens 131-141 22034471-2 2001 The disease is caused by a polyglutamine repeat expansion located in the N-terminal region of the huntingtin protein. polyglutamine 27-40 huntingtin Homo sapiens 98-108 11035034-1 2001 Huntington"s disease is caused by an expanded CAG trinucleotide repeat coding for a polyglutamine stretch within the huntingtin protein. polyglutamine 84-97 huntingtin Homo sapiens 117-127 11172033-1 2001 Huntington"s disease (HD) is a neurodegenerative disease caused by polyglutamine expansion in the protein huntingtin (htt). polyglutamine 67-80 huntingtin Homo sapiens 106-116 11172033-1 2001 Huntington"s disease (HD) is a neurodegenerative disease caused by polyglutamine expansion in the protein huntingtin (htt). polyglutamine 67-80 huntingtin Homo sapiens 118-121 11172033-9 2001 Our data suggest that abnormal expression of CA150, mediated by interaction with polyglutamine-expanded htt, may alter transcription and have a role in HD pathogenesis. polyglutamine 81-94 huntingtin Homo sapiens 104-107 11298997-2 2001 Unstable CAG expansion in the IT15 gene, responsible for disease, is translated into an abnormally long polyglutamine (polyQ) tract near the N-terminus of the huntingtin protein. polyglutamine 104-117 huntingtin Homo sapiens 30-34 11298997-2 2001 Unstable CAG expansion in the IT15 gene, responsible for disease, is translated into an abnormally long polyglutamine (polyQ) tract near the N-terminus of the huntingtin protein. polyglutamine 104-117 huntingtin Homo sapiens 159-169 11298997-2 2001 Unstable CAG expansion in the IT15 gene, responsible for disease, is translated into an abnormally long polyglutamine (polyQ) tract near the N-terminus of the huntingtin protein. polyglutamine 119-124 huntingtin Homo sapiens 30-34 11298997-2 2001 Unstable CAG expansion in the IT15 gene, responsible for disease, is translated into an abnormally long polyglutamine (polyQ) tract near the N-terminus of the huntingtin protein. polyglutamine 119-124 huntingtin Homo sapiens 159-169 11007884-1 2000 An expansion of polyglutamines in the N terminus of huntingtin causes Huntington"s disease (HD) and results in the accrual of mutant protein in the nucleus and cytoplasm of affected neurons. polyglutamine 16-30 huntingtin Homo sapiens 52-62 11007884-4 2000 Here we show that the huntingtin-enriched cytoplasmic vacuoles formed in vitro internalized the lysosomal enzyme cathepsin D in proportion to the polyglutamine-length in huntingtin. polyglutamine 146-159 huntingtin Homo sapiens 22-32 11007884-4 2000 Here we show that the huntingtin-enriched cytoplasmic vacuoles formed in vitro internalized the lysosomal enzyme cathepsin D in proportion to the polyglutamine-length in huntingtin. polyglutamine 146-159 huntingtin Homo sapiens 170-180 10801775-0 2000 Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin. polyglutamine 50-63 huntingtin Homo sapiens 73-83 10899401-0 2000 Alpha-synuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington"s disease patients and transgenic mouse models. polyglutamine 47-60 huntingtin Homo sapiens 36-46 10899401-5 2000 Our findings demonstrate that alpha-synuclein can be used as a marker for huntingtin polyglutamine aggregates in both human and mice. polyglutamine 85-98 huntingtin Homo sapiens 74-84 10770929-1 2000 Huntington"s disease is a neurodegenerative disorder caused by CAG expansion that results in expansion of a polyglutamine tract at the extreme N terminus of huntingtin (htt). polyglutamine 108-121 huntingtin Homo sapiens 157-167 10770929-1 2000 Huntington"s disease is a neurodegenerative disorder caused by CAG expansion that results in expansion of a polyglutamine tract at the extreme N terminus of huntingtin (htt). polyglutamine 108-121 huntingtin Homo sapiens 169-172 10770929-2 2000 htt with polyglutamine expansion is proapoptotic in different cell types. polyglutamine 9-22 huntingtin Homo sapiens 0-3 10770929-5 2000 In contrast to cleavable htt, caspase-resistant htt with an expanded polyglutamine tract has reduced toxicity in apoptotically stressed neuronal and nonneuronal cells and forms aggregates at a much reduced frequency. polyglutamine 69-82 huntingtin Homo sapiens 48-51 10801775-1 2000 We previously reported that expression of polyglutamine-expanded huntingtin induces apoptosis via c-Jun amino-terminal kinase (JNK) activation in HN33 cells (Liu, Y. F. (1998) J. Biol. polyglutamine 42-55 huntingtin Homo sapiens 65-75 10801775-4 2000 Extending this study, we now demonstrate a role of mixed-lineage kinase 2 (MLK2), a JNK activator, in polyglutamine-expanded huntingtin-mediated neuronal toxicity. polyglutamine 102-115 huntingtin Homo sapiens 125-135 10801775-6 2000 Similar to the expression of polyglutamine-expanded huntingtin, expression of MLK2 also induces JNK activation and apoptosis in HN33 cells. polyglutamine 29-42 huntingtin Homo sapiens 52-62 10801775-9 2000 Our results suggest that activation of MLK2-mediated signaling cascades may be partially involved in neuronal death induced by polyglutamine-expanded huntingtin. polyglutamine 127-140 huntingtin Homo sapiens 150-160 10829068-3 2000 Here we show by using a filter retardation assay that the mAb 1C2, which specifically recognizes the elongated polyglutamine (polyQ) stretch in huntingtin, and the chemical compounds Congo red, thioflavine S, chrysamine G, and Direct fast yellow inhibit HD exon 1 protein aggregation in a dose-dependent manner. polyglutamine 111-124 huntingtin Homo sapiens 144-154 10829068-3 2000 Here we show by using a filter retardation assay that the mAb 1C2, which specifically recognizes the elongated polyglutamine (polyQ) stretch in huntingtin, and the chemical compounds Congo red, thioflavine S, chrysamine G, and Direct fast yellow inhibit HD exon 1 protein aggregation in a dose-dependent manner. polyglutamine 126-131 huntingtin Homo sapiens 144-154 10814708-1 2000 To understand gene expression changes mediated by a polyglutamine repeat expansion in the human huntingtin protein, we used oligonucleotide DNA arrays to profile approximately 6000 striatal mRNAs in the R6/2 mouse, a transgenic Huntington"s disease (HD) model. polyglutamine 52-65 huntingtin Homo sapiens 96-106 10804212-1 2000 Expansion of a polyglutamine sequence in the N terminus of huntingtin is the gain-of-function event that causes Huntington"s disease. polyglutamine 15-28 huntingtin Homo sapiens 59-69 10639135-1 2000 Spinobulbar muscular atrophy and Huntington"s disease are caused by polyglutamine expansion in the androgen receptor and huntingtin, respectively, and their pathogenesis has been associated with abnormal nuclear localization and aggregation of truncated forms of these proteins. polyglutamine 68-81 huntingtin Homo sapiens 121-131 10733228-3 2000 Caspases appear to be involved in the molecular pathology of HD by directly cleaving huntingtin and generating toxic protein fragments containing the polyglutamine tract, and by being recruited and activated by polyglutamine-containing aggregates composed mainly of truncated huntingtin fragments. polyglutamine 211-224 huntingtin Homo sapiens 276-286 10479410-1 1999 Huntington"s disease is a neurodegenerative disorder resulting from expansion of the polyglutamine region in huntingtin. polyglutamine 85-98 huntingtin Homo sapiens 109-119 10589536-9 1999 Rather than a harbinger of neuronal death, mutant huntingtin aggregation may be a cytoprotective mechanism against polyglutamine-induced neurotoxicity. polyglutamine 115-128 huntingtin Homo sapiens 50-60 10537061-1 1999 The polyglutamine-expanded N-terminal region of mutant huntingtin causes neurodegeneration in Huntington"s disease (HD). polyglutamine 4-17 huntingtin Homo sapiens 55-65 10527804-0 1999 Mutant huntingtin forms in vivo complexes with distinct context-dependent conformations of the polyglutamine segment. polyglutamine 95-108 huntingtin Homo sapiens 7-17 10527804-2 1999 Using specific antibodies, we have probed the structure of the polyglutamine segment in mutant huntingtin complexes formed in cell culture from either truncated or full-length protein. polyglutamine 63-76 huntingtin Homo sapiens 95-105 10966117-5 1999 Recent studies have shown that polyglutamine expansion causes huntingtin to aggregate, to accumulate in the nucleus, and to interact abnormally with other proteins. polyglutamine 31-44 huntingtin Homo sapiens 62-72 10479410-2 1999 Although huntingtin is normally cytoplasmic, in affected brain regions proteolytic fragments of mutant huntingtin containing the polyglutamine repeat form intranuclear inclusions. polyglutamine 129-142 huntingtin Homo sapiens 9-19 10479410-2 1999 Although huntingtin is normally cytoplasmic, in affected brain regions proteolytic fragments of mutant huntingtin containing the polyglutamine repeat form intranuclear inclusions. polyglutamine 129-142 huntingtin Homo sapiens 103-113 10434302-1 1999 Polyglutamine (polyQ) extension in the coding sequence of mutant huntingtin causes neuronal degeneration associated with the formation of insoluble polyQ aggregates in Huntington"s disease. polyglutamine 0-13 huntingtin Homo sapiens 65-75 10434302-1 1999 Polyglutamine (polyQ) extension in the coding sequence of mutant huntingtin causes neuronal degeneration associated with the formation of insoluble polyQ aggregates in Huntington"s disease. polyglutamine 15-20 huntingtin Homo sapiens 65-75 10377424-4 1999 More TGase-catalyzed aggregates formed when the polyglutamine domain of htt exceeded the pathologic threshold of polyQ36. polyglutamine 48-61 huntingtin Homo sapiens 72-75 10434302-1 1999 Polyglutamine (polyQ) extension in the coding sequence of mutant huntingtin causes neuronal degeneration associated with the formation of insoluble polyQ aggregates in Huntington"s disease. polyglutamine 148-153 huntingtin Homo sapiens 65-75 10434302-9 1999 In susceptible cells, extended polyQ tracts in huntingtin might interact with and sequester or deplete certain endogenous polyQ-containing cellular proteins. polyglutamine 31-36 huntingtin Homo sapiens 47-57 10434302-9 1999 In susceptible cells, extended polyQ tracts in huntingtin might interact with and sequester or deplete certain endogenous polyQ-containing cellular proteins. polyglutamine 122-127 huntingtin Homo sapiens 47-57 9920660-1 1999 Neuronal intranuclear inclusions are found in the brains of patients with Huntington"s disease and form from the polyglutamine-expanded N-terminal region of mutant huntingtin. polyglutamine 113-126 huntingtin Homo sapiens 164-174 10353249-3 1999 The mutation in patients with Huntington"s disease is an expanded CAG/polyglutamine repeat in huntingtin, a protein of unknown function with a relative molecular mass of 350,000 (M(r) 350K). polyglutamine 70-83 huntingtin Homo sapiens 94-104 10353249-6 1999 Transgenic mice expressing exon 1 of the human huntingtin gene with an expanded CAG/polyglutamine repeat develop a progressive syndrome with many of the characteristics of human Huntington"s disease. polyglutamine 84-97 huntingtin Homo sapiens 47-57 9920660-4 1999 Only mutant huntingtin formed nuclear and cytoplasmic inclusions, which increased with polyglutamine expansion and with time after transfection. polyglutamine 87-100 huntingtin Homo sapiens 12-22 9679147-6 1998 In some human proteins, e.g., Huntingtin, abnormal amplification of such poly-glutamine regions causes late-onset neurodegeneration. polyglutamine 73-87 huntingtin Homo sapiens 30-40 9888310-1 1999 Huntingtin, the protein product of the Huntington"s disease (HD) gene, is expressed with an expanded polyglutamine domain in the brain and in nonneuronal tissues in patients with HD. polyglutamine 101-114 huntingtin Homo sapiens 0-10 9700202-1 1998 The hallmark neuropathology of Huntington"s disease (HD) is due to elongation of a polyglutamine segment in huntingtin, a novel approximately 350 kDa protein of unknown function. polyglutamine 83-96 huntingtin Homo sapiens 108-118 9768849-0 1998 Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. polyglutamine 0-13 huntingtin Homo sapiens 29-39 9768849-2 1998 Disease alleles contain a trinucleotide repeat expansion of variable length, which encodes polyglutamine tracts near the amino terminus of the HD protein, huntingtin. polyglutamine 91-104 huntingtin Homo sapiens 155-165 9768849-3 1998 Polyglutamine-expanded huntingtin, but not normal huntingtin, forms nuclear inclusions. polyglutamine 0-13 huntingtin Homo sapiens 23-33 9768849-6 1998 As in human neurons, polyglutamine-expanded huntingtin induced neuronal degeneration. polyglutamine 21-34 huntingtin Homo sapiens 44-54 9682010-2 1998 In patients with Huntington"s disease (HD), the NH2-terminal region of huntingtin has an expanded polyglutamine tract. polyglutamine 98-111 huntingtin Homo sapiens 71-81 10410676-2 1998 It has been proposed that the expanded polyglutamine stretch confers a new property on huntingtin and thereby causes cell and region-specific neurodegeneration. polyglutamine 39-52 huntingtin Homo sapiens 87-97 10410676-3 1998 Genotype-phenotype correlations predict that this novel property appears above a threshold length (approximately 38 glutamines), becomes progressively more evident with increasing polyglutamine length, is completely dominant over normal huntingtin and is not appreciably worsened by a double genetic dose in HD homozygotes. polyglutamine 180-193 huntingtin Homo sapiens 237-247 10410676-11 1998 Our data support the view that the expanded polyglutamine segment confers on huntingtin a new property that plays a determining role in HD pathogenesis and could be a target for treatment. polyglutamine 44-57 huntingtin Homo sapiens 77-87 9536081-1 1998 Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an expanding CAG repeat coding for polyglutamine in the huntingtin protein. polyglutamine 115-128 huntingtin Homo sapiens 136-146 9606203-6 1998 Furthermore, expression of mutant huntingtin results in increased susceptibility to apoptotic stress that is greater with decreasing protein length and increasing polyglutamine size. polyglutamine 163-176 huntingtin Homo sapiens 34-44 9783215-4 1998 The system was applied to the polyglutamine (poly-Q) repeat in the first exon of huntingtin, the gene implicated in Huntington"s disease. polyglutamine 30-43 huntingtin Homo sapiens 81-91 9587422-4 1998 In the presence of tissue transglutaminase, purified glyceraldehyde-3-phosphate dehydrogenase (a key glycolytic enzyme that binds tightly to the polyglutamine domains of both huntingtin and dentatorubral-pallidoluysian atrophy proteins) is covalently attached to polyglutamine peptides in vitro, resulting in the formation of high-M(r) aggregates. polyglutamine 145-158 huntingtin Homo sapiens 175-185 9527890-2 1998 The gene encodes the protein huntingtin with a polyglutamine tract encoded by the CAG repeat at the N-terminus. polyglutamine 47-60 huntingtin Homo sapiens 29-39 9660943-0 1998 Transglutaminase action imitates Huntington"s disease: selective polymerization of Huntingtin containing expanded polyglutamine. polyglutamine 114-127 huntingtin Homo sapiens 83-93 9660943-2 1998 In parts of the brain affected by Huntington"s disease, the amount of the huntingtin with expanded polyglutamine is reduced and there appear huntingtin-containing polymers of larger molecular weight. polyglutamine 99-112 huntingtin Homo sapiens 74-84 9660943-3 1998 We show here that huntingtin is a substrate of transglutaminase in vitro and that the rate constant of the reaction increases with length of the polyglutamine over a range of an order of magnitude. polyglutamine 145-158 huntingtin Homo sapiens 18-28 9660943-4 1998 As a result, huntingtin with expanded polyglutamine is preferentially incorporated into polymers. polyglutamine 38-51 huntingtin Homo sapiens 13-23 9660943-5 1998 Both disappearance of the huntingtin with expanded polyglutamine and its replacement by polymeric forms are prevented by inhibitors of transglutaminase. polyglutamine 51-64 huntingtin Homo sapiens 26-36 10488448-3 1998 The genetic defect causing HD is an expansion of a CAG repeat encoding a polyglutamine stretch in the target protein, named huntingtin. polyglutamine 73-86 huntingtin Homo sapiens 124-134 9666478-1 1998 Huntington"s disease (HD) is caused by CAG triplet repeat expansion in IT15 which leads to polyglutamine stretches in the HD protein product, huntingtin. polyglutamine 91-104 huntingtin Homo sapiens 71-75 9666478-1 1998 Huntington"s disease (HD) is caused by CAG triplet repeat expansion in IT15 which leads to polyglutamine stretches in the HD protein product, huntingtin. polyglutamine 91-104 huntingtin Homo sapiens 142-152 9783215-4 1998 The system was applied to the polyglutamine (poly-Q) repeat in the first exon of huntingtin, the gene implicated in Huntington"s disease. polyglutamine 45-51 huntingtin Homo sapiens 81-91 8757264-1 1996 Huntington"s disease (HD) is caused by a genetic mutation that results in a polyglutamine expansion in huntingtin. polyglutamine 76-89 huntingtin Homo sapiens 103-113 9392570-1 1997 Huntington"s disease is an inherited disorder caused by expansion of a CAG trinucleotide repeat in the IT15 gene, which leads to expansion of a polyglutamine tract within the protein called huntingtin. polyglutamine 144-157 huntingtin Homo sapiens 103-107 9392570-1 1997 Huntington"s disease is an inherited disorder caused by expansion of a CAG trinucleotide repeat in the IT15 gene, which leads to expansion of a polyglutamine tract within the protein called huntingtin. polyglutamine 144-157 huntingtin Homo sapiens 190-200 9302293-2 1997 Patients with HD have an expanded NH2-terminal polyglutamine region in huntingtin. polyglutamine 47-60 huntingtin Homo sapiens 71-81 9302293-3 1997 An NH2-terminal fragment of mutant huntingtin was localized to neuronal intranuclear inclusions (NIIs) and dystrophic neurites (DNs) in the HD cortex and striatum, which are affected in HD, and polyglutamine length influenced the extent of huntingtin accumulation in these structures. polyglutamine 194-207 huntingtin Homo sapiens 35-45 9147654-2 1997 For the interaction in vivo, a protein region downstream of the polyglutamine stretch in huntingtin is essential. polyglutamine 64-77 huntingtin Homo sapiens 89-99 8696339-0 1996 Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. polyglutamine 89-102 huntingtin Homo sapiens 12-22 8696339-4 1996 The rate of cleavage increases with the length of the huntingtin polyglutamine tract, providing an explanation for the gain-of-function associated with CAG expansion. polyglutamine 65-78 huntingtin Homo sapiens 54-64 8643525-0 1996 Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin. polyglutamine 13-26 huntingtin Homo sapiens 37-47 8643525-11 1996 These results suggest that huntingtin interacts with other proteins including CAM and that the expansion of polyGln alters this interaction. polyglutamine 108-115 huntingtin Homo sapiens 27-37 34958078-1 2021 Full-length huntingtin (FL HTT) is a large (aa 1-3,144), ubiquitously expressed, polyglutamine (polyQ)-containing protein with a mass of approximately 350 kDa. polyglutamine 81-94 huntingtin Homo sapiens 12-22 7477378-1 1995 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an expanding polyglutamine repeat in the IT15 or huntingtin gene. polyglutamine 101-114 huntingtin Homo sapiens 129-133 7477378-1 1995 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an expanding polyglutamine repeat in the IT15 or huntingtin gene. polyglutamine 101-114 huntingtin Homo sapiens 137-147 7477378-3 1995 The huntingtin gene product is expressed at similar levels in patients and controls, and the genetics of the disorder suggest that the expansion of the polyglutamine repeat induces a toxic gain of function, perhaps through interactions with other cellular proteins. polyglutamine 152-165 huntingtin Homo sapiens 4-14 8521295-5 1995 The difference in the length of the N-terminal polyglutamine segment is sufficient to distinguish normal and HD huntingtin in a Western blot assay. polyglutamine 47-60 huntingtin Homo sapiens 112-122 33941067-1 2021 Huntington"s disease (HD) is a neurodegenerative, dominantly inherited genetic disease caused by expansion of the polyglutamine tract in the huntingtin gene. polyglutamine 114-127 huntingtin Homo sapiens 141-151 33767215-1 2021 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an expanded polyglutamine repeat in the huntingtin gene. polyglutamine 100-113 huntingtin Homo sapiens 128-138 33809947-3 2021 The result is the production of a mutant Htt with an abnormally long polyglutamine repeat that leads to pathological Htt aggregates. polyglutamine 69-82 huntingtin Homo sapiens 41-44 33809947-3 2021 The result is the production of a mutant Htt with an abnormally long polyglutamine repeat that leads to pathological Htt aggregates. polyglutamine 69-82 huntingtin Homo sapiens 117-120 28094373-1 2017 Huntington"s disease is caused by a CAG trinucleotide expansion mutation in the Huntingtin gene that leads to an artificially long polyglutamine sequence in the Huntingtin protein. polyglutamine 131-144 huntingtin Homo sapiens 80-90 28094373-1 2017 Huntington"s disease is caused by a CAG trinucleotide expansion mutation in the Huntingtin gene that leads to an artificially long polyglutamine sequence in the Huntingtin protein. polyglutamine 131-144 huntingtin Homo sapiens 161-171 21163446-1 2011 Huntington"s disease is a progressive, fatal, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene, which encodes an abnormally long polyglutamine repeat in the huntingtin protein. polyglutamine 163-176 huntingtin Homo sapiens 113-123 21163446-1 2011 Huntington"s disease is a progressive, fatal, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene, which encodes an abnormally long polyglutamine repeat in the huntingtin protein. polyglutamine 163-176 huntingtin Homo sapiens 191-201 34880419-0 2021 Huntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1. polyglutamine 58-71 huntingtin Homo sapiens 0-10 34880419-6 2021 The exon 1 region of HTT is dynamic but shows greater conformational variety in the polyglutamine expanded mutant than wildtype exon 1. polyglutamine 84-97 huntingtin Homo sapiens 21-24 34880419-7 2021 Our data provide a foundation for future functional and drug discovery studies targeting Huntington"s disease and illuminate the structural consequences of HTT polyglutamine expansion. polyglutamine 160-173 huntingtin Homo sapiens 156-159 7581375-7 1995 Both alleles of the IT15 protein were expressed at similar levels in HD lymphoblastoid cell lines and HD post-mortem hippocampus and cerebellum (regions relatively spared in HD), indicating that even very long CAG repeats can be translated into polyglutamine. polyglutamine 245-258 huntingtin Homo sapiens 20-24 33809220-1 2021 Huntington"s disease (HD) is a monogenetic neurodegenerative disorder characterized by the accumulation of polyglutamine-expanded huntingtin (mHTT). polyglutamine 107-120 huntingtin Homo sapiens 130-140 34564830-1 2022 Huntington disease (HD) is a single-gene autosomal dominant inherited neurodegenerative disease caused by a polyglutamine expansion of the protein huntingtin (HTT). polyglutamine 108-121 huntingtin Homo sapiens 147-157 34564830-1 2022 Huntington disease (HD) is a single-gene autosomal dominant inherited neurodegenerative disease caused by a polyglutamine expansion of the protein huntingtin (HTT). polyglutamine 108-121 huntingtin Homo sapiens 159-162 34958078-1 2021 Full-length huntingtin (FL HTT) is a large (aa 1-3,144), ubiquitously expressed, polyglutamine (polyQ)-containing protein with a mass of approximately 350 kDa. polyglutamine 81-94 huntingtin Homo sapiens 27-30 34958078-1 2021 Full-length huntingtin (FL HTT) is a large (aa 1-3,144), ubiquitously expressed, polyglutamine (polyQ)-containing protein with a mass of approximately 350 kDa. polyglutamine 96-101 huntingtin Homo sapiens 12-22 34958078-1 2021 Full-length huntingtin (FL HTT) is a large (aa 1-3,144), ubiquitously expressed, polyglutamine (polyQ)-containing protein with a mass of approximately 350 kDa. polyglutamine 96-101 huntingtin Homo sapiens 27-30 34406601-4 2021 Previously, it has been reported that though clearance of wild-type huntingtin protein is mediated by chaperone-mediated autophagy (CMA), however, degradation of mutant huntingtin (mHtt with numerous poly Q repeats) remains impaired by this route as mutant Htt binds with high affinity to Hsc70 and LAMP-2A. polyglutamine 200-206 huntingtin Homo sapiens 169-179 34732320-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine (polyQ) tract in the N-terminal domain of the Huntingtin (Htt) protein product. polyglutamine 149-163 huntingtin Homo sapiens 114-117 34732320-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine (polyQ) tract in the N-terminal domain of the Huntingtin (Htt) protein product. polyglutamine 149-163 huntingtin Homo sapiens 210-220 34732320-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine (polyQ) tract in the N-terminal domain of the Huntingtin (Htt) protein product. polyglutamine 149-163 huntingtin Homo sapiens 222-225 34732320-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine (polyQ) tract in the N-terminal domain of the Huntingtin (Htt) protein product. polyglutamine 165-170 huntingtin Homo sapiens 114-117 34732320-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine (polyQ) tract in the N-terminal domain of the Huntingtin (Htt) protein product. polyglutamine 165-170 huntingtin Homo sapiens 210-220 34732320-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine (polyQ) tract in the N-terminal domain of the Huntingtin (Htt) protein product. polyglutamine 165-170 huntingtin Homo sapiens 222-225 34884540-5 2021 HD is caused by a polyglutamine repeat expansion in the Huntingtin protein that brings about a multifaceted pathogenesis affecting several cellular processes. polyglutamine 18-31 huntingtin Homo sapiens 56-66 34718744-5 2021 The tRNAPro mutant caused synthetic toxicity with a deleterious huntingtin poly-glutamine (polyQ) allele in neuronal cells. polyglutamine 75-89 huntingtin Homo sapiens 64-74 34718744-5 2021 The tRNAPro mutant caused synthetic toxicity with a deleterious huntingtin poly-glutamine (polyQ) allele in neuronal cells. polyglutamine 91-96 huntingtin Homo sapiens 64-74 34563643-1 2021 Huntington"s disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeat in the exon-1 of huntingtin protein (HTT). polyglutamine 105-118 huntingtin Homo sapiens 151-161 34563643-1 2021 Huntington"s disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeat in the exon-1 of huntingtin protein (HTT). polyglutamine 105-118 huntingtin Homo sapiens 171-174 34563643-1 2021 Huntington"s disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeat in the exon-1 of huntingtin protein (HTT). polyglutamine 120-125 huntingtin Homo sapiens 151-161 34563643-1 2021 Huntington"s disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeat in the exon-1 of huntingtin protein (HTT). polyglutamine 120-125 huntingtin Homo sapiens 171-174 34406601-9 2021 We observed that GAPDH knockdown cells transfected with N-terminal mutant huntingtin (103 poly Q residues) aggregate-prone protein exhibit diminished autophagy. polyglutamine 90-96 huntingtin Homo sapiens 74-84 34191328-3 2021 We used Saccharomyces cerevisiae to analyze how mitochondrial processes regulate the behavior of aggregation-prone polyQ protein derived from human huntingtin. polyglutamine 115-120 huntingtin Homo sapiens 148-158 34831058-3 2021 Like other misfolded proteins, mutated Huntingtin proteins with polyglutamine expansions are prone to aggregation. polyglutamine 64-77 huntingtin Homo sapiens 39-49 34089719-1 2021 Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 86-99 huntingtin Homo sapiens 141-151 34089719-1 2021 Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 86-99 huntingtin Homo sapiens 153-156 34089719-1 2021 Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 101-106 huntingtin Homo sapiens 141-151 34089719-1 2021 Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. polyglutamine 101-106 huntingtin Homo sapiens 153-156 34246856-1 2021 Huntington"s disease (HD) is a fatal neurodegenerative disease caused by an extended polyglutamine (polyQ) domain within the first exon of the huntingtin protein (htt). polyglutamine 85-98 huntingtin Homo sapiens 143-161 34246856-1 2021 Huntington"s disease (HD) is a fatal neurodegenerative disease caused by an extended polyglutamine (polyQ) domain within the first exon of the huntingtin protein (htt). polyglutamine 85-98 huntingtin Homo sapiens 163-166 34246856-1 2021 Huntington"s disease (HD) is a fatal neurodegenerative disease caused by an extended polyglutamine (polyQ) domain within the first exon of the huntingtin protein (htt). polyglutamine 100-105 huntingtin Homo sapiens 143-161 34246856-1 2021 Huntington"s disease (HD) is a fatal neurodegenerative disease caused by an extended polyglutamine (polyQ) domain within the first exon of the huntingtin protein (htt). polyglutamine 100-105 huntingtin Homo sapiens 163-166 34246856-2 2021 PolyQ expansion directly invokes the formation of a heterogenous mixture of toxic htt aggregates, including fibrils and oligomers. polyglutamine 0-5 huntingtin Homo sapiens 82-85 34746859-1 2021 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. polyglutamine 92-105 huntingtin Homo sapiens 127-137 34746859-1 2021 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. polyglutamine 92-105 huntingtin Homo sapiens 139-142 34746859-1 2021 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. polyglutamine 107-112 huntingtin Homo sapiens 127-137 34746859-1 2021 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. polyglutamine 107-112 huntingtin Homo sapiens 139-142 34721539-1 2021 Huntington"s disease (HD) is a chronic neurodegenerative disorder caused by an expansion of polyglutamine repeats in exon 1 of the Huntingtin gene. polyglutamine 92-105 huntingtin Homo sapiens 131-141 34659371-1 2021 Huntington"s disease (HD) is caused by an expansion mutation of a CAG repeat in exon 1 of the huntingtin (HTT) gene, that encodes an expanded polyglutamine tract in the HTT protein. polyglutamine 142-155 huntingtin Homo sapiens 94-104 34659371-1 2021 Huntington"s disease (HD) is caused by an expansion mutation of a CAG repeat in exon 1 of the huntingtin (HTT) gene, that encodes an expanded polyglutamine tract in the HTT protein. polyglutamine 142-155 huntingtin Homo sapiens 106-109 34659371-1 2021 Huntington"s disease (HD) is caused by an expansion mutation of a CAG repeat in exon 1 of the huntingtin (HTT) gene, that encodes an expanded polyglutamine tract in the HTT protein. polyglutamine 142-155 huntingtin Homo sapiens 169-172 34659371-9 2021 Since MID1 is a translation regulator, association of the MID1 complex stimulates translation of mutant HTT mRNA, resulting in an overproduction of polyglutamine protein. polyglutamine 148-161 huntingtin Homo sapiens 104-107 34573100-1 2021 Huntington"s disease (HD) is caused by expansion of polyglutamine repeats in the protein huntingtin, which affects the corpus striatum of the brain. polyglutamine 52-65 huntingtin Homo sapiens 89-99 34573100-2 2021 The polyglutamine repeats in mutant huntingtin cause its aggregation and elicit toxicity by affecting several cellular processes, which include dysregulated organellar stress responses. polyglutamine 4-17 huntingtin Homo sapiens 36-46 34239038-1 2021 Huntington disease (HD) is a neurodegenerative trinucleotide repeat disorder caused by an expanded poly-glutamine (polyQ) tract in the mutant huntingtin (mHTT) protein. polyglutamine 99-113 huntingtin Homo sapiens 142-152 34239038-1 2021 Huntington disease (HD) is a neurodegenerative trinucleotide repeat disorder caused by an expanded poly-glutamine (polyQ) tract in the mutant huntingtin (mHTT) protein. polyglutamine 115-120 huntingtin Homo sapiens 142-152 34161085-1 2021 Huntington"s disease is a neurodegenerative disorder caused by the expansion of a polyglutamine repeat (>36Q) in the N-terminal domain of the huntingtin protein (Htt), which renders the protein or fragments thereof more prone to aggregate and form inclusions. polyglutamine 82-95 huntingtin Homo sapiens 142-152 34161085-1 2021 Huntington"s disease is a neurodegenerative disorder caused by the expansion of a polyglutamine repeat (>36Q) in the N-terminal domain of the huntingtin protein (Htt), which renders the protein or fragments thereof more prone to aggregate and form inclusions. polyglutamine 82-95 huntingtin Homo sapiens 162-165 34201610-0 2021 Membrane Interactions Accelerate the Self-Aggregation of Huntingtin Exon 1 Fragments in a Polyglutamine Length-Dependent Manner. polyglutamine 90-103 huntingtin Homo sapiens 57-67 34207177-1 2021 Huntington"s disease (HD) is a multi-system disorder that is caused by expanded CAG repeats within the exon-1 of the huntingtin (HTT) gene that translate to the polyglutamine stretch in the HTT protein. polyglutamine 161-174 huntingtin Homo sapiens 117-127 34207177-1 2021 Huntington"s disease (HD) is a multi-system disorder that is caused by expanded CAG repeats within the exon-1 of the huntingtin (HTT) gene that translate to the polyglutamine stretch in the HTT protein. polyglutamine 161-174 huntingtin Homo sapiens 129-132 34207177-1 2021 Huntington"s disease (HD) is a multi-system disorder that is caused by expanded CAG repeats within the exon-1 of the huntingtin (HTT) gene that translate to the polyglutamine stretch in the HTT protein. polyglutamine 161-174 huntingtin Homo sapiens 190-193 35200138-6 2022 Aggregation-prone model substrates, including Huntingtin exon 1 containing an expanded polyglutamine repeat, aggregate faster under these conditions. polyglutamine 87-100 huntingtin Homo sapiens 46-56 35550919-6 2022 This minireview focuses on aberrant cysteine and H2S metabolism in Huntington"s disease, a neurodegenerative disease caused by expansion of polyglutamine encoding repeats in the gene huntingtin, which leads to motor and cognitive deficits. polyglutamine 140-153 huntingtin Homo sapiens 183-193 35367225-3 2022 People carrying abnormally long expansions of CAGs (more than 35 CAG repeats) produce mutant huntingtin (mHtt), which encodes tracks of polyglutamines (polyQs). polyglutamine 136-150 huntingtin Homo sapiens 93-103 35367225-3 2022 People carrying abnormally long expansions of CAGs (more than 35 CAG repeats) produce mutant huntingtin (mHtt), which encodes tracks of polyglutamines (polyQs). polyglutamine 152-158 huntingtin Homo sapiens 93-103 35058188-2 2022 CAG repeat expansions in mutant Huntingtin (mHTT) exon 1 encode for polyglutamine (polyQ) stretches and influence age of onset and disease severity, depending on their length. polyglutamine 68-81 huntingtin Homo sapiens 32-42 35058188-2 2022 CAG repeat expansions in mutant Huntingtin (mHTT) exon 1 encode for polyglutamine (polyQ) stretches and influence age of onset and disease severity, depending on their length. polyglutamine 83-88 huntingtin Homo sapiens 32-42 35628660-1 2022 Huntington"s disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. polyglutamine 107-121 huntingtin Homo sapiens 66-76 35628660-1 2022 Huntington"s disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. polyglutamine 107-121 huntingtin Homo sapiens 78-81 35628660-1 2022 Huntington"s disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. polyglutamine 123-128 huntingtin Homo sapiens 66-76 35628660-1 2022 Huntington"s disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. polyglutamine 123-128 huntingtin Homo sapiens 78-81 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 27-32 huntingtin Homo sapiens 49-59 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 27-32 huntingtin Homo sapiens 66-69 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 27-32 huntingtin Homo sapiens 115-125 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 27-32 huntingtin Homo sapiens 135-138 35439000-1 2022 Huntington"s disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain within the huntingtin protein (htt) that initiates toxic protein aggregation. polyglutamine 75-88 huntingtin Homo sapiens 115-133 35439000-1 2022 Huntington"s disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain within the huntingtin protein (htt) that initiates toxic protein aggregation. polyglutamine 75-88 huntingtin Homo sapiens 135-138 35439000-1 2022 Huntington"s disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain within the huntingtin protein (htt) that initiates toxic protein aggregation. polyglutamine 90-95 huntingtin Homo sapiens 115-133 35439000-1 2022 Huntington"s disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain within the huntingtin protein (htt) that initiates toxic protein aggregation. polyglutamine 90-95 huntingtin Homo sapiens 135-138 35447076-0 2022 Group dynamics goes awry: PolyQ-expanded huntingtin gains unwanted partners. polyglutamine 26-31 huntingtin Homo sapiens 41-51 35447076-2 2022 define high-confidence polyglutamine-dependent huntingtin interactors using AP-MS and complementary approaches and categorize them based on their interaction abundance and stability. polyglutamine 23-36 huntingtin Homo sapiens 47-57 35447076-3 2022 The study reveals that a toxic gain of polyQ-dependent Htt interacting partners is a robust feature of HD pathogenesis. polyglutamine 39-44 huntingtin Homo sapiens 55-58 35395060-1 2022 Huntington"s disease (HD) is caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin gene that results in expression of a mutant huntingtin protein (mHTT) containing an expanded polyglutamine tract in the amino terminus. polyglutamine 202-215 huntingtin Homo sapiens 98-108 35395060-1 2022 Huntington"s disease (HD) is caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin gene that results in expression of a mutant huntingtin protein (mHTT) containing an expanded polyglutamine tract in the amino terminus. polyglutamine 202-215 huntingtin Homo sapiens 153-163 35051614-2 2022 The disease is characterized by an abnormal polyglutamine expansion in the huntingtin gene, which drives the toxicity of the mutated form of the protein. polyglutamine 44-57 huntingtin Homo sapiens 75-85 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 84-97 huntingtin Homo sapiens 49-59 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 84-97 huntingtin Homo sapiens 66-69 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 84-97 huntingtin Homo sapiens 115-125 35631226-2 2022 The disease is caused by a polyQ mutation in the Huntingtin gene (HTT), producing a polyglutamine expansion in the Huntingtin protein (HTT). polyglutamine 84-97 huntingtin Homo sapiens 135-138 35563194-1 2022 A set of guanine-rich aptamers able to preferentially recognize full-length huntingtin with an expanded polyglutamine tract has been recently identified, showing high efficacy in modulating the functions of the mutated protein in a variety of cell experiments. polyglutamine 104-117 huntingtin Homo sapiens 76-86 35427742-1 2022 While Huntington disease (HD) is caused solely by a polyglutamine expansion in the huntingtin gene, environmental factors can influence HD onset and progression. polyglutamine 52-65 huntingtin Homo sapiens 83-93 35444517-0 2022 Polyglutamine Expansion in Huntingtin and Mechanism of DNA Damage Repair Defects in Huntington"s Disease. polyglutamine 0-13 huntingtin Homo sapiens 27-37 35444517-5 2022 Mutations in huntingtin (HTT) gene that lead to polyglutamine repeat expansion at the N-terminal of HTT protein has been shown to disrupt transcription-coupled DNA repair process, a specialized DNA repair process associated with transcription. polyglutamine 48-61 huntingtin Homo sapiens 13-23 35444517-5 2022 Mutations in huntingtin (HTT) gene that lead to polyglutamine repeat expansion at the N-terminal of HTT protein has been shown to disrupt transcription-coupled DNA repair process, a specialized DNA repair process associated with transcription. polyglutamine 48-61 huntingtin Homo sapiens 25-28 35444517-5 2022 Mutations in huntingtin (HTT) gene that lead to polyglutamine repeat expansion at the N-terminal of HTT protein has been shown to disrupt transcription-coupled DNA repair process, a specialized DNA repair process associated with transcription. polyglutamine 48-61 huntingtin Homo sapiens 100-103 35444517-6 2022 Due to the recent progress made in understanding the mechanisms of DNA repair in relation to HD, in this review, we will mainly focus on the mechanisms by which the wild-type huntingtin (HTT) protein helps in DNA repair during transcription, and the how polyglutamine expansions in HTT impedes this process in HD. polyglutamine 254-267 huntingtin Homo sapiens 282-285 35046408-1 2022 Huntington"s disease (HD) is a severe inherited neurological disorder caused by a CAG repeat expansion in the huntingtin gene (HTT), leading to the accumulation of mutant huntingtin with polyglutamine repeats. polyglutamine 187-200 huntingtin Homo sapiens 110-120 35108063-1 2022 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin (HTT) gene that encodes the pathologic mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) tract. polyglutamine 219-232 huntingtin Homo sapiens 126-136 35108063-1 2022 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin (HTT) gene that encodes the pathologic mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) tract. polyglutamine 219-232 huntingtin Homo sapiens 138-141 35108063-1 2022 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin (HTT) gene that encodes the pathologic mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) tract. polyglutamine 219-232 huntingtin Homo sapiens 183-186 35108063-1 2022 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin (HTT) gene that encodes the pathologic mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) tract. polyglutamine 234-239 huntingtin Homo sapiens 126-136 35108063-1 2022 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin (HTT) gene that encodes the pathologic mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) tract. polyglutamine 234-239 huntingtin Homo sapiens 138-141 35108063-1 2022 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin (HTT) gene that encodes the pathologic mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) tract. polyglutamine 234-239 huntingtin Homo sapiens 183-186 35013554-0 2022 Extreme conservation of the poly-glutamine tract in huntingtin is related to neurodevelopmental functions: the "better" may become the "enemy of the good" in the course of evolution. polyglutamine 28-42 huntingtin Homo sapiens 52-62 35046408-1 2022 Huntington"s disease (HD) is a severe inherited neurological disorder caused by a CAG repeat expansion in the huntingtin gene (HTT), leading to the accumulation of mutant huntingtin with polyglutamine repeats. polyglutamine 187-200 huntingtin Homo sapiens 127-130 35046408-1 2022 Huntington"s disease (HD) is a severe inherited neurological disorder caused by a CAG repeat expansion in the huntingtin gene (HTT), leading to the accumulation of mutant huntingtin with polyglutamine repeats. polyglutamine 187-200 huntingtin Homo sapiens 171-181 35069097-2 2021 Mutant huntingtin, the disease-causing entity in Huntington"s disease, has an expanded polyglutamine track at the N terminus that causes the protein to misfold and form toxic intracellular aggregates. polyglutamine 87-100 huntingtin Homo sapiens 7-17 35069097-7 2021 We demonstrate that the molecular chaperone, cysteine string protein (CSPalpha; DnaJC5), facilitates export of disease-causing-polyglutamine-expanded huntingtin cargo in 180-240 nm vesicles as well as larger 10-30 mum vesicles. polyglutamine 127-140 huntingtin Homo sapiens 150-160 35169703-4 2022 The polyQ mutation at the N-terminus of the huntingtin protein alters its natural interactions with neural phospholipids in vitro, suggesting that the specific lipid composition of brain regions could influence their vulnerability to interference by mutant huntingtin; however, this has not yet been demonstrated in vivo. polyglutamine 4-9 huntingtin Homo sapiens 44-54 35169703-4 2022 The polyQ mutation at the N-terminus of the huntingtin protein alters its natural interactions with neural phospholipids in vitro, suggesting that the specific lipid composition of brain regions could influence their vulnerability to interference by mutant huntingtin; however, this has not yet been demonstrated in vivo. polyglutamine 4-9 huntingtin Homo sapiens 257-267 33907289-1 2021 Huntington"s disease (HD) is a devastating neurodegenerative disorder, caused by a CAG/polyglutamine repeat expansion, that results in the aggregation of the huntingtin protein, culminating in the deposition of inclusion bodies in HD patient brains. polyglutamine 87-100 huntingtin Homo sapiens 158-168 33909994-2 2021 At the protein level, this translates into the expansion of a polyglutamine (polyQ) stretch located at the HTT N terminus, which renders HTT aggregation prone by unknown mechanisms. polyglutamine 62-75 huntingtin Homo sapiens 107-110 33909994-2 2021 At the protein level, this translates into the expansion of a polyglutamine (polyQ) stretch located at the HTT N terminus, which renders HTT aggregation prone by unknown mechanisms. polyglutamine 62-75 huntingtin Homo sapiens 137-140 33909994-2 2021 At the protein level, this translates into the expansion of a polyglutamine (polyQ) stretch located at the HTT N terminus, which renders HTT aggregation prone by unknown mechanisms. polyglutamine 77-82 huntingtin Homo sapiens 107-110 33909994-2 2021 At the protein level, this translates into the expansion of a polyglutamine (polyQ) stretch located at the HTT N terminus, which renders HTT aggregation prone by unknown mechanisms. polyglutamine 77-82 huntingtin Homo sapiens 137-140 33909994-3 2021 Here we investigated the effects of polyQ expansion on HTT in a complex with its stabilizing interaction partner huntingtin-associated protein 40 (HAP40). polyglutamine 36-41 huntingtin Homo sapiens 55-58 33874957-13 2021 Such stress appeared to be induced by supernatants from human PSC-derived striatal neurons expressing mutant HTT with a long polyglutamine tract. polyglutamine 125-138 huntingtin Homo sapiens 109-112