PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11163963-1 2000 PQBP-1 has been identified as a protein that binds to huntingtin, androgen receptor and transcription factor Brain-2 through their homopolymeric glutamine repeats. Glutamine 145-154 huntingtin Homo sapiens 54-64 10961047-7 2000 The mutation of huntingtin produces an expanded stretch of glutamine (Gln) residues. Glutamine 59-68 huntingtin Homo sapiens 16-26 10958656-1 2000 An elongated glutamine tract in mutant huntingtin initiates Huntington"s disease (HD) pathogenesis via a novel structural property that displays neuronal selectivity, glutamine progressivity and dominance over the normal protein based on genetic criteria. Glutamine 13-22 huntingtin Homo sapiens 39-49 10958656-1 2000 An elongated glutamine tract in mutant huntingtin initiates Huntington"s disease (HD) pathogenesis via a novel structural property that displays neuronal selectivity, glutamine progressivity and dominance over the normal protein based on genetic criteria. Glutamine 167-176 huntingtin Homo sapiens 39-49 10961047-7 2000 The mutation of huntingtin produces an expanded stretch of glutamine (Gln) residues. Glutamine 70-73 huntingtin Homo sapiens 16-26 9700202-6 1998 This interaction is mediated by huntingtin"s proline-rich region and is enhanced by lengthening the adjacent glutamine tract. Glutamine 109-118 huntingtin Homo sapiens 32-42 10502825-1 1999 Huntington disease (HD) is a genetically dominant condition caused by expanded CAG repeats coding for glutamine in the HD gene product huntingtin. Glutamine 102-111 huntingtin Homo sapiens 135-145 10527804-7 1999 However, the observation of soluble complexes in which an HD-specific pathogenic conformation of the glutamine tract remains accessible suggests that pathogenesis could also be triggered at the level of full-length huntingtin by abnormal aggregation with normal or abnormal protein partners. Glutamine 101-110 huntingtin Homo sapiens 215-225 10363492-4 1999 The gene (IT15) is localized in the short arm of chromosome 4 in the telemaric region 4p16.3 and it is known that the mutation is produced by an increase in the number of trinucleotides CAG (glutamine) localized in the 5" end of the gene, in the first exon. Glutamine 191-200 huntingtin Homo sapiens 10-14 9768849-5 1998 Amino-terminal fragments of human huntingtin containing tracts of 2, 75, and 120 glutamine residues were expressed in photoreceptor neurons in the compound eye. Glutamine 81-90 huntingtin Homo sapiens 34-44 9285789-1 1997 Huntington"s disease (HD) occurs when the widely expressed protein huntingtin contains an expanded glutamine repeat. Glutamine 99-108 huntingtin Homo sapiens 67-77 9606203-3 1998 We have created numerous deletion constructs expressing successively smaller fragments of huntingtin and show that these smaller proteins containing 128 glutamines form both intranuclear and perinuclear aggregates. Glutamine 153-163 huntingtin Homo sapiens 90-100 9606203-4 1998 In contrast, larger NH2-terminal fragments of huntingtin proteins with 128 glutamines form exclusively perinuclear aggregates. Glutamine 75-85 huntingtin Homo sapiens 46-56 9668110-2 1998 Huntington"s disease (HD) is caused by the expansion of a glutamine repeat in the protein huntingtin. Glutamine 58-67 huntingtin Homo sapiens 90-100 9668110-3 1998 The expanded glutamine repeat is thought to mediate a gain of function by causing huntingtin to abnormally interact with other proteins. Glutamine 13-22 huntingtin Homo sapiens 82-92 10410676-1 1998 Huntington"s disease (HD) is caused by an expanded CAG trinucleotide repeat encoding a tract of consecutive glutamines near the amino terminus of huntingtin, a large protein of unknown function. Glutamine 108-118 huntingtin Homo sapiens 146-156 9536080-0 1998 Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats. Glutamine 71-80 huntingtin Homo sapiens 26-36 9536080-1 1998 Huntington"s disease (HD) is caused by expansion of a glutamine repeat in huntingtin. Glutamine 54-63 huntingtin Homo sapiens 74-84 9536080-6 1998 By expressing a series of huntingtin constructs encoding various glutamine repeats (23-150 units) in cultured cells we observed N-terminal fragments of huntingtin (amino acids 1-67 and 1-212), but not full-length huntingtins, with glutamine repeats >/=66 units formed protein aggregates. Glutamine 65-74 huntingtin Homo sapiens 26-36 9536080-6 1998 By expressing a series of huntingtin constructs encoding various glutamine repeats (23-150 units) in cultured cells we observed N-terminal fragments of huntingtin (amino acids 1-67 and 1-212), but not full-length huntingtins, with glutamine repeats >/=66 units formed protein aggregates. Glutamine 65-74 huntingtin Homo sapiens 152-162 9536080-6 1998 By expressing a series of huntingtin constructs encoding various glutamine repeats (23-150 units) in cultured cells we observed N-terminal fragments of huntingtin (amino acids 1-67 and 1-212), but not full-length huntingtins, with glutamine repeats >/=66 units formed protein aggregates. Glutamine 231-240 huntingtin Homo sapiens 26-36 9536080-6 1998 By expressing a series of huntingtin constructs encoding various glutamine repeats (23-150 units) in cultured cells we observed N-terminal fragments of huntingtin (amino acids 1-67 and 1-212), but not full-length huntingtins, with glutamine repeats >/=66 units formed protein aggregates. Glutamine 231-240 huntingtin Homo sapiens 152-162 9536080-8 1998 This study suggests that various N-terminal fragments of mutant huntingtin can form aggregates and that aggregation is prompted by lengthening the glutamine repeat. Glutamine 147-156 huntingtin Homo sapiens 64-74 9536081-0 1998 Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Glutamine 59-68 huntingtin Homo sapiens 34-44 9536081-4 1998 We have now developed a cell culture model demonstrating that N-terminal fragments of huntingtin with expanded glutamine repeats aggregate both in the cytoplasm and in the nucleus. Glutamine 111-120 huntingtin Homo sapiens 86-96 9536081-10 1998 These data indicate that N-terminal truncated fragments of huntingtin with expanded glutamine repeats can aggregate in cells in culture and that this aggregation can be toxic to cells. Glutamine 84-93 huntingtin Homo sapiens 59-69 9666478-3 1998 Specific morphological markers of affected cells have not been identified in patients with HD, although a unique itranuclear inclusion was recently reported in neurons of transgenic animals expressing a construct encoding the N-terminal part (including the glutamine repeat) of huntingtin (Davies et al., 1997). Glutamine 257-266 huntingtin Homo sapiens 278-288 34880419-1 2021 Huntington"s disease results from expansion of a glutamine-coding CAG tract in the huntingtin (HTT) gene, producing an aberrantly functioning form of HTT. Glutamine 49-58 huntingtin Homo sapiens 83-93 7581375-1 1995 Huntington"s disease (HD) is an inherited, neurodegenerative disorder caused by expansion of a CAG repeat in the IT15 gene, leading to an expanded glutamine repeat in the HD protein. Glutamine 147-156 huntingtin Homo sapiens 113-117 7581375-9 1995 These data suggest the possibility of altered structure, abnormal processing or abnormality of protein-protein interactions involving the IT15 protein with the expanded glutamine repeat. Glutamine 169-178 huntingtin Homo sapiens 138-142 34880419-1 2021 Huntington"s disease results from expansion of a glutamine-coding CAG tract in the huntingtin (HTT) gene, producing an aberrantly functioning form of HTT. Glutamine 49-58 huntingtin Homo sapiens 95-98 34880419-1 2021 Huntington"s disease results from expansion of a glutamine-coding CAG tract in the huntingtin (HTT) gene, producing an aberrantly functioning form of HTT. Glutamine 49-58 huntingtin Homo sapiens 150-153 32995988-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG nucleotide expansion, which encodes the amino acid glutamine, in the huntingtin gene. Glutamine 125-134 huntingtin Homo sapiens 143-153 34831058-2 2021 One of these diseases is Huntington"s, which is caused by increased glutamine-encoding trinucleotide repeats within the Huntingtin gene. Glutamine 68-77 huntingtin Homo sapiens 120-130 34201610-3 2021 The huntingtin protein is characterised by a segment of consecutive glutamines which, when exceeding ~ 37 residues, results in the occurrence of the disease. Glutamine 68-78 huntingtin Homo sapiens 4-14 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. Glutamine 44-53 huntingtin Homo sapiens 86-96 33827396-6 2021 HspB7 is ineffective in suppression of amorphous aggregation of model proteins induced by heating or reduction of disulfide bonds, however it is very effective in prevention of aggregation of huntingtin fragments enriched with Gln residues. Glutamine 227-230 huntingtin Homo sapiens 192-202 33070471-1 2021 BACKGROUND: Huntington"s disease (HD) is a heritable degenerative brain disease caused by a mutation in the huntingtin gene with excessive repeats of the base triplet cytosine-adenine-guanine (CAG), which codes for the aminoacid glutamine. Glutamine 229-238 huntingtin Homo sapiens 108-118 33224521-3 2020 Its genetic basis is an expansion of the CAG triplet repeat in the HTT gene, leading to extra glutamines in the huntingtin protein. Glutamine 94-104 huntingtin Homo sapiens 67-70 33224521-3 2020 Its genetic basis is an expansion of the CAG triplet repeat in the HTT gene, leading to extra glutamines in the huntingtin protein. Glutamine 94-104 huntingtin Homo sapiens 112-122 33920936-1 2021 Huntington"s disease (HD) is a rare hereditary autosomal dominant neurodegenerative disorder, which is caused by expression of mutant huntingtin protein (mHTT) with an abnormal number of glutamine repeats in its N terminus, and characterized by intracellular mHTT aggregates (inclusions) in the brain. Glutamine 187-196 huntingtin Homo sapiens 134-144 32402249-0 2020 Flanking Regions Determine the Structure of the Poly-Glutamine in Huntingtin through Mechanisms Common among Glutamine-Rich Human Proteins. Glutamine 53-62 huntingtin Homo sapiens 66-76 31226569-4 2019 Herein, we have synthesized biocompatible MnFe2O4 nanoparticles (NPs) and demonstrated their unique effect in accelerating the clearance of mutant huntingtin (Htt) protein exhibiting 74 glutamine repeats [Htt(Q74)]. Glutamine 186-195 huntingtin Homo sapiens 147-157 31297710-6 2019 In HD, abnormal expansion of glutamine repeats in the protein huntingtin leads to toxic aggregation of huntingtin which in turn impairs the quality control mechanism of cells through damaging the machineries involved in removal of aggregated abnormal protein. Glutamine 29-38 huntingtin Homo sapiens 62-72 31297710-6 2019 In HD, abnormal expansion of glutamine repeats in the protein huntingtin leads to toxic aggregation of huntingtin which in turn impairs the quality control mechanism of cells through damaging the machineries involved in removal of aggregated abnormal protein. Glutamine 29-38 huntingtin Homo sapiens 103-113 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. Glutamine 2-11 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. Glutamine 2-11 huntingtin Homo sapiens 157-160 31226569-4 2019 Herein, we have synthesized biocompatible MnFe2O4 nanoparticles (NPs) and demonstrated their unique effect in accelerating the clearance of mutant huntingtin (Htt) protein exhibiting 74 glutamine repeats [Htt(Q74)]. Glutamine 186-195 huntingtin Homo sapiens 159-162 29601786-3 2018 Here, we performed systematic experimental and theoretical studies to examine the self-assembly of an aggregation-prone N-terminal HTT exon-1 fragment with 49 glutamines (Ex1Q49). Glutamine 159-169 huntingtin Homo sapiens 131-134 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. Glutamine 10-19 huntingtin Homo sapiens 94-97 30842263-2 2019 Pathogenic HD CAG-expansion mutations create a polyglutamine (polyQ) tract at the N terminus of HTT that expands above a critical threshold of ~35 glutamine residues. Glutamine 51-60 huntingtin Homo sapiens 96-99 30672003-9 2019 From our simulations, we suggest that at least 34 glutamines are required for initiating aggregation and 40 residues length is critical for the aggregation of huntingtin exon 1 protein for disease onset. Glutamine 50-60 huntingtin Homo sapiens 159-169 30279700-3 2018 We demonstrate that expression of an aggregation-prone Htt construct with 103 glutamine residues (103Q), but not the non-expanded form (25Q), results in severe growth defects in slx5Delta and slx8Delta cells. Glutamine 78-87 huntingtin Homo sapiens 55-58 29377621-2 2018 The cytosine-adenine-guanine (CAG) triplet expansion encoding glutamine present in the protein huntingtin (Htt), produces widespread neuronal and glial pathology. Glutamine 62-71 huntingtin Homo sapiens 95-105 29377621-2 2018 The cytosine-adenine-guanine (CAG) triplet expansion encoding glutamine present in the protein huntingtin (Htt), produces widespread neuronal and glial pathology. Glutamine 62-71 huntingtin Homo sapiens 107-110 29359503-4 2018 The generality of the strategy was demonstrated by introducing a labeled glutamine into a pathological version of huntingtin with 46 glutamines. Glutamine 73-82 huntingtin Homo sapiens 114-124 29359503-4 2018 The generality of the strategy was demonstrated by introducing a labeled glutamine into a pathological version of huntingtin with 46 glutamines. Glutamine 133-143 huntingtin Homo sapiens 114-124 26846325-1 2016 Huntington"s Disease (HD) is an autosomal dominant disease that occurs as a result of expansion of the trinucleotide repeat CAG (glutamine) on the HTT gene. Glutamine 129-138 huntingtin Homo sapiens 147-150 27514446-2 2017 HD is caused by inheritance of an expanded CAG repeat in the HTT gene, resulting in a mutant huntingtin (mHtt) protein containing extra glutamine residues. Glutamine 136-145 huntingtin Homo sapiens 61-64 27514446-2 2017 HD is caused by inheritance of an expanded CAG repeat in the HTT gene, resulting in a mutant huntingtin (mHtt) protein containing extra glutamine residues. Glutamine 136-145 huntingtin Homo sapiens 93-103 28968242-4 2017 That is, studies performed before and after the identification of the genetic defect underlying HD (CAG: encoding glutamine >=36 repeats located in exon 1 of the HTT gene) and with the development and evolution of HD animal models. Glutamine 114-123 huntingtin Homo sapiens 162-165 28674979-3 2017 HD is caused by a CAG repeat expansion encoding an extended tract of the amino acid glutamine in the huntingtin protein. Glutamine 84-93 huntingtin Homo sapiens 101-111 26601664-2 2016 The disorder is typified by an expansion of more than 35 repeats of the nucleotide triplet cytosine- adenine-guanosine (CAG) which codes for the amino acid glutamine in the huntingtin gene. Glutamine 156-165 huntingtin Homo sapiens 173-183 26863614-6 2016 By combining SNP-targeting allele-specific silencing and gain-of-function approaches, we showed that a 46-glutamine expansion in human HTT was sufficient for a dominant-negative effect on spindle orientation and changes in the distribution within the spindle pole and the cell cortex of dynein, p150Glued and NuMA in neural cells. Glutamine 106-115 huntingtin Homo sapiens 135-138 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. Glutamine 79-89 huntingtin Homo sapiens 114-124 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. Glutamine 84-94 huntingtin Homo sapiens 98-108 26673834-2 2015 In a yeast model, an N-terminal fragment of mutant huntingtin with a stretch of 103 glutamine residues aggregates and causes toxicity, while its non-toxic wild type variant with a sequence of 25 glutamines (Htt25Q) does not aggregate. Glutamine 84-93 huntingtin Homo sapiens 51-61 26673834-2 2015 In a yeast model, an N-terminal fragment of mutant huntingtin with a stretch of 103 glutamine residues aggregates and causes toxicity, while its non-toxic wild type variant with a sequence of 25 glutamines (Htt25Q) does not aggregate. Glutamine 195-205 huntingtin Homo sapiens 51-61 26210848-1 2015 UNLABELLED: Huntington"s disease (HD) is an autosomal dominant, progressive neurodegenerative disorder, caused by an expanded trinucleotide CAG sequence of the huntingtin (Htt) gene, which encodes a stretch of glutamines in the Htt protein. Glutamine 210-220 huntingtin Homo sapiens 160-170 26210848-1 2015 UNLABELLED: Huntington"s disease (HD) is an autosomal dominant, progressive neurodegenerative disorder, caused by an expanded trinucleotide CAG sequence of the huntingtin (Htt) gene, which encodes a stretch of glutamines in the Htt protein. Glutamine 210-220 huntingtin Homo sapiens 172-175 26210848-1 2015 UNLABELLED: Huntington"s disease (HD) is an autosomal dominant, progressive neurodegenerative disorder, caused by an expanded trinucleotide CAG sequence of the huntingtin (Htt) gene, which encodes a stretch of glutamines in the Htt protein. Glutamine 210-220 huntingtin Homo sapiens 228-231 26195796-1 2015 Huntington"s disease (HD) is a progressive neurodegenerative disease caused by a glutamine repeat expansion in mutant huntingtin (mHtt). Glutamine 81-90 huntingtin Homo sapiens 118-128 25687118-2 2015 This results in the addition of a poly-glutamine tract within the Huntingtin protein, resulting in its pathological form. Glutamine 39-48 huntingtin Homo sapiens 66-76 25761110-4 2015 Here, we report the effects of the specifically-neuronal human glucose transporter expression in neurons of a Drosophila model carrying the exon 1 of the human huntingtin gene with 93 glutamine repeats (HQ93). Glutamine 184-193 huntingtin Homo sapiens 160-170 25995452-6 2015 Using an aggregation suppression assay and cryoelectron tomography coupled with a novel computational classification method, we uncover the interactions between the synthetic CCT5 complex (~ 1 MDa) and aggregates of mutant huntingtin exon 1 containing 46 glutamines (mHTTQ46-Ex1). Glutamine 255-265 huntingtin Homo sapiens 223-233 25316320-1 2014 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a mutation in the Huntingtin gene, where excessive (>= 36) CAG repeats encode for glutamine expansion in the huntingtin protein. Glutamine 170-179 huntingtin Homo sapiens 106-116 25316320-1 2014 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a mutation in the Huntingtin gene, where excessive (>= 36) CAG repeats encode for glutamine expansion in the huntingtin protein. Glutamine 170-179 huntingtin Homo sapiens 197-207 23819039-3 2013 The siRNA technology was used to show that the inhibition of GAPDH expression leads to a 45-50% reduction in the aggregation of mutant huntingtin, with a repeat of 103 glutamine residues in a model of Huntington"s disease (HD). Glutamine 168-177 huntingtin Homo sapiens 135-145 24415136-1 2014 The huntingtin protein is characterized by a segment of consecutive glutamines (Q(N)) that is responsible for its fibrillation. Glutamine 68-78 huntingtin Homo sapiens 4-14 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. Glutamine 121-130 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. Glutamine 121-130 huntingtin Homo sapiens 155-158 24184605-2 2014 Genetic mutation in HD is identified by an expansion of CAG repeats coding for glutamine (Q) in exon 1 of the huntingtin (htt) gene. Glutamine 79-88 huntingtin Homo sapiens 110-120 24184605-2 2014 Genetic mutation in HD is identified by an expansion of CAG repeats coding for glutamine (Q) in exon 1 of the huntingtin (htt) gene. Glutamine 79-88 huntingtin Homo sapiens 122-125 24006238-2 2013 HD is caused by an expansion of CAG repeats coding for glutamine (Q) in exon 1 of the huntingtin gene. Glutamine 55-64 huntingtin Homo sapiens 86-96 23847583-2 2013 Huntington"s disease (HD) is an autosomal dominant disorder caused by a tandem repeat expansion encoding an expanded tract of glutamines in the huntingtin protein. Glutamine 126-136 huntingtin Homo sapiens 144-154 25358787-1 2014 Huntington"s disease (HD) is a dominant neurodegenerative disorder caused by the expansion of glutamine residues in the N-terminal region of the huntingtin (HTT) protein. Glutamine 94-103 huntingtin Homo sapiens 145-155 25358787-1 2014 Huntington"s disease (HD) is a dominant neurodegenerative disorder caused by the expansion of glutamine residues in the N-terminal region of the huntingtin (HTT) protein. Glutamine 94-103 huntingtin Homo sapiens 157-160 24968783-3 2014 The cause is an expansion in CAG (glutamine) repeats in the HTT gene. Glutamine 34-43 huntingtin Homo sapiens 60-63 24330821-6 2013 The mitochondrial dysfunction in mutant cells was also observed in cortical neurons expressing exon 1 of the huntingtin protein with 104 Gln residues (Q104-GFP) when they were exposed to calcium stress. Glutamine 137-140 huntingtin Homo sapiens 109-119 23612654-5 2013 Chorea Huntington, one of the most well-known examples, is caused by triplet extensions that can lead to more than 100 glutamines in the N-terminal region of huntingtin, accompanied by huntingtin aggregation. Glutamine 119-129 huntingtin Homo sapiens 158-168 23394029-3 2012 IT-15 mutation includes multiple (36-250) repetitions of trinucleotide sequence (CAG) encoding a glutamine at the amino end of Huntington (mHtt). Glutamine 97-106 huntingtin Homo sapiens 0-5 23423362-1 2013 An expansion of glutamine repeats in the N-terminal domain of the huntingtin protein leads to Huntington"s disease (HD), a neurodegenerative condition characterized by the presence of involuntary movements, dementia, and psychiatric disturbances. Glutamine 16-25 huntingtin Homo sapiens 66-76 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. Glutamine 86-96 huntingtin Homo sapiens 36-46 22978784-2 2012 Huntington"s disease, for example, is related to the misfolding of the Huntingtin protein which occurs when the polyQ segment has more than approximately 36 glutamines. Glutamine 157-167 huntingtin Homo sapiens 71-81 25063429-6 2013 RESULTS: One copy of the human HTT transgene encoding 124 glutamines integrated into chromosome 1 q24-q25 and successful germ line transmission occurred through successive generations (F0, F1, F2 and F3 generations). Glutamine 58-68 huntingtin Homo sapiens 31-34 22773688-1 2012 Huntington"s disease (HD) is a genetic neurodegenerative disease characterized by an exceedingly high number of contiguous glutamine residues in the translated protein, huntingtin (Htt). Glutamine 123-132 huntingtin Homo sapiens 169-179 22773688-1 2012 Huntington"s disease (HD) is a genetic neurodegenerative disease characterized by an exceedingly high number of contiguous glutamine residues in the translated protein, huntingtin (Htt). Glutamine 123-132 huntingtin Homo sapiens 181-184 22801429-2 2012 Here we used site-directed spin labeling and electron paramagnetic resonance (EPR) spectroscopy to study the structural features of huntingtin exon 1 (HDx1) containing 46 glutamine residues in its polyglutamine (polyQ) region. Glutamine 171-180 huntingtin Homo sapiens 132-142 22905336-1 2012 Huntington"s Disease (HD) is a fatally inherited neurodegenerative disorder caused by an expanded glutamine repeat in the N-terminal region of the huntingtin (HTT) protein. Glutamine 98-107 huntingtin Homo sapiens 147-157 22905336-1 2012 Huntington"s Disease (HD) is a fatally inherited neurodegenerative disorder caused by an expanded glutamine repeat in the N-terminal region of the huntingtin (HTT) protein. Glutamine 98-107 huntingtin Homo sapiens 159-162 21909428-3 2011 It is caused by a CAG repeat expansion in the HTT gene, which results in an expansion of a glutamine stretch at the N-terminal end of the huntingtin protein. Glutamine 91-100 huntingtin Homo sapiens 46-49 23236391-7 2012 CONCLUSIONS: Our findings indicate that HEK293 cells express a protease that is capable of efficiently cleaving cp-B/2 like fragments of htt with normal or expanded glutamine repeats. Glutamine 165-174 huntingtin Homo sapiens 137-140 23236391-8 2012 For reasons that remain unclear, this protease cleaves longer htt fragments, with normal or expanded glutamine expansions, much less efficiently. Glutamine 101-110 huntingtin Homo sapiens 62-65 23225006-0 2012 Fibrillogenesis of huntingtin and other glutamine containing proteins. Glutamine 40-49 huntingtin Homo sapiens 19-29 23225006-1 2012 This chapter focuses on the aggregation of glutamine containing peptides and proteins with an emphasis on huntingtin protein, whose aggregation leads to the development of Huntington"s disease. Glutamine 43-52 huntingtin Homo sapiens 106-116 21896647-1 2011 Huntington"s disease (HD) is caused by expanded glutamine repeats within the huntingtin (Htt) protein. Glutamine 48-57 huntingtin Homo sapiens 77-87 21896647-1 2011 Huntington"s disease (HD) is caused by expanded glutamine repeats within the huntingtin (Htt) protein. Glutamine 48-57 huntingtin Homo sapiens 89-92 21278081-2 2011 HD is caused by the extension of trinucleotide repeats encoding a stretch of glutamine residues at the amino-terminal end of the large huntingtin (HTT) protein. Glutamine 77-86 huntingtin Homo sapiens 135-145 21278081-2 2011 HD is caused by the extension of trinucleotide repeats encoding a stretch of glutamine residues at the amino-terminal end of the large huntingtin (HTT) protein. Glutamine 77-86 huntingtin Homo sapiens 147-150 21882412-7 2011 This feature was an important clue for discovery of the causal mutation, as a trinucleotide repeat expansion encoding an elongated glutamine tract in the htt protein was determined to be responsible for HD in 1993, and a relationship between the length of the expanded glutamine tract and the severity of the HD phenotype was uncovered at that time [1]. Glutamine 131-140 huntingtin Homo sapiens 154-157 21882412-7 2011 This feature was an important clue for discovery of the causal mutation, as a trinucleotide repeat expansion encoding an elongated glutamine tract in the htt protein was determined to be responsible for HD in 1993, and a relationship between the length of the expanded glutamine tract and the severity of the HD phenotype was uncovered at that time [1]. Glutamine 269-278 huntingtin Homo sapiens 154-157 22052286-5 2012 Here, we developed a protein-aggregation reporter that uses huntingtin exon 1 containing 72 glutamines fused to the N-terminal end of firefly luciferase (httQ72-Luc). Glutamine 92-102 huntingtin Homo sapiens 60-70 23560303-2 2012 For example, the expansion of the glutamine repeat in huntingtin leads to the debilitating neurodegenerative disease, Huntington"s disease. Glutamine 34-43 huntingtin Homo sapiens 54-64 21909428-3 2011 It is caused by a CAG repeat expansion in the HTT gene, which results in an expansion of a glutamine stretch at the N-terminal end of the huntingtin protein. Glutamine 91-100 huntingtin Homo sapiens 138-148 21095569-1 2010 Huntington"s Disease (HD) is characterized by a mutation in the huntingtin (Htt) gene encoding an expansion of glutamine repeats on the N terminus of the Htt protein. Glutamine 111-120 huntingtin Homo sapiens 64-74 21095569-1 2010 Huntington"s Disease (HD) is characterized by a mutation in the huntingtin (Htt) gene encoding an expansion of glutamine repeats on the N terminus of the Htt protein. Glutamine 111-120 huntingtin Homo sapiens 76-79 21095569-1 2010 Huntington"s Disease (HD) is characterized by a mutation in the huntingtin (Htt) gene encoding an expansion of glutamine repeats on the N terminus of the Htt protein. Glutamine 111-120 huntingtin Homo sapiens 154-157 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. Glutamine 116-126 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. Glutamine 118-127 huntingtin Homo sapiens 54-64 20873112-3 2010 Htt with an abnormal stretch of above 35 glutamines in the N terminus (mHtt) results in HD. Glutamine 41-51 huntingtin Homo sapiens 0-3 20219972-1 2010 Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin protein (with expanded polyQ), depend on a Gln or Asn (QN)-rich region for amyloid formation. Glutamine 133-136 huntingtin Homo sapiens 79-89 19338577-5 2010 In vitro, recombinant exon 1 of huntingtin with 44 glutamines (htt-exon1-44Q) binds to CaM-agarose; the addition of 10 microM of CaM-peptide significantly decreases the interaction of htt-exon1-44Q and CaM but not the binding between CaM and calcineurin, another CaM-binding protein. Glutamine 51-61 huntingtin Homo sapiens 32-42 19710014-3 2009 The first exon of Htt encodes 17 amino acids followed by a poly(Q) repeat of variable length and culminating with a proline-rich domain of 50 amino acids. Glutamine 63-66 huntingtin Homo sapiens 18-21 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. Glutamine 124-134 huntingtin Homo sapiens 86-96 20640815-1 2009 Huntington"s disease patients commonly have glutamine (Q) repeats longer than 37 residues in the Huntingtin protein. Glutamine 44-53 huntingtin Homo sapiens 97-107 19270310-2 2009 Huntington disease is caused by expansion of glutamine repeats in the huntingtin protein. Glutamine 45-54 huntingtin Homo sapiens 70-80 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. Glutamine 51-60 huntingtin Homo sapiens 80-90 19429504-1 2009 Huntington"s Disease (HD) is a rare neurodegenerative disease caused by mutation of the huntingtin gene that results in a protein with an expanded stretch of glutamine repeats (polyQ). Glutamine 158-167 huntingtin Homo sapiens 88-98 20396523-4 2006 Mutant huntingtin with abnormally long glutamine stretch aggregates and forms intranuclear inclusions. Glutamine 39-48 huntingtin Homo sapiens 7-17 18386172-1 2008 Huntington disease (HD) is a genetically dominant condition caused by expanded CAG repeats which code for glutamine in the HD gene product, huntingtin. Glutamine 106-115 huntingtin Homo sapiens 140-150 18488016-3 2008 HD is caused by the expansion of cytosine-adenine-guanine (CAG, translated into glutamine) trinucleotide repeats in the first exon of the human huntingtin (HTT) gene. Glutamine 80-89 huntingtin Homo sapiens 144-154 18488016-3 2008 HD is caused by the expansion of cytosine-adenine-guanine (CAG, translated into glutamine) trinucleotide repeats in the first exon of the human huntingtin (HTT) gene. Glutamine 80-89 huntingtin Homo sapiens 156-159 18279698-2 2008 Mutated htt (mhtt) is characterized by an increased number of glutamine repeats in the N-terminal end; when 40 or more glutamine residues are present, the disease is manifested. Glutamine 62-71 huntingtin Homo sapiens 8-11 18279698-2 2008 Mutated htt (mhtt) is characterized by an increased number of glutamine repeats in the N-terminal end; when 40 or more glutamine residues are present, the disease is manifested. Glutamine 119-128 huntingtin Homo sapiens 8-11 18243803-1 2008 It is known that Huntington"s disease patients commonly have glutamine (Q) repeat sequences longer than a critical length in the coding area of Huntingtin protein in their genes. Glutamine 61-70 huntingtin Homo sapiens 144-154 18077673-3 2007 In this regard, the YAC128 mouse model, expressing full-length human huntingtin with 128 glutamine repeats, has been the focus of much interest. Glutamine 89-98 huntingtin Homo sapiens 69-79 17409200-1 2007 Huntington disease is caused by the expansion of a CAG repeat encoding an extended glutamine tract in a protein called huntingtin. Glutamine 83-92 huntingtin Homo sapiens 119-129 19118173-2 2008 We show that sympathetic neurons containing cytoplasmic inclusions formed by 97 glutamines expressed within human huntingtin exon1-enhanced green fluorescent protein (Q97) undergo a protracted form of nonapoptotic death that is insensitive to Bax deletion or caspase inhibition but is characterized by mitochondrial dysfunction. Glutamine 80-90 huntingtin Homo sapiens 114-124 17413322-1 2007 Huntington disease (HD) is caused by the expansion of a glutamine (Q) repeat near the N terminus of huntingtin (htt), resulting in altered conformation of the mutant protein to produce, most prominently in brain neurons, nuclear and cytoplasmic inclusion pathology. Glutamine 56-65 huntingtin Homo sapiens 100-110 17413322-1 2007 Huntington disease (HD) is caused by the expansion of a glutamine (Q) repeat near the N terminus of huntingtin (htt), resulting in altered conformation of the mutant protein to produce, most prominently in brain neurons, nuclear and cytoplasmic inclusion pathology. Glutamine 56-65 huntingtin Homo sapiens 112-115 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. Glutamine 201-210 huntingtin Homo sapiens 10-13 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. Glutamine 94-104 huntingtin Homo sapiens 180-190 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. Glutamine 55-64 huntingtin Homo sapiens 83-93 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. Glutamine 84-94 huntingtin Homo sapiens 11-14 16043692-1 2005 Huntington"s disease (HD) is an autosomal dominant disorder caused by an expansion of glutamine repeats in ubiquitously distributed huntingtin protein. Glutamine 86-95 huntingtin Homo sapiens 132-142 11461154-1 2001 Neurodegeneration in Huntington"s disease (HD) is associated with an elongated glutamine tract in the widely expressed huntingtin protein. Glutamine 79-88 huntingtin Homo sapiens 119-129 12499864-1 2002 Human neuroblastoma SH-SY5Y cell lines stably expressing mutant truncated huntingtin with 82 (mutant) glutamine repeats (N63-82Q) were briefly exposed to hyperosmotic conditions which decrease cell volume and therefore transiently increased the concentration of N63-82Q, as well as activating specific stress-induced pathways. Glutamine 102-111 huntingtin Homo sapiens 74-84 12235581-8 2002 These studies have originated multiple hypotheses regarding the mechanism by which huntingtin with an expanded poly glutamine tract exerts its toxicity. Glutamine 116-125 huntingtin Homo sapiens 83-93 11870213-1 2002 Huntington"s disease results from an expansion of a series of glutamine repeats in the protein huntingtin. Glutamine 62-71 huntingtin Homo sapiens 95-105 11719265-2 2001 The transgenic mouse model R6/2 expresses exon 1 of the human huntingtin gene with >150 CAG repeats, which produces mutant HD protein with an expanded poly-glutamine tract. Glutamine 156-165 huntingtin Homo sapiens 62-72 15140195-7 2004 Huntingtin-EGFP with a pathogenic glutamine tract and a shorter half-life displayed a delayed onset of aggregate formation and was more toxic to transfected cells. Glutamine 34-43 huntingtin Homo sapiens 0-10 14570710-1 2003 Huntington disease is caused by the expansion of a CAG repeat encoding an extended glutamine tract in a protein called huntingtin. Glutamine 83-92 huntingtin Homo sapiens 119-129 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. Glutamine 117-127 huntingtin Homo sapiens 38-41 12486229-0 2002 Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans neurons from huntingtin polyglutamine neurotoxicity. Glutamine 0-9 huntingtin Homo sapiens 82-92 12518531-2 2002 Huntington"s gene, IT15, in chromosome 4p16.3, has 67 axons with 10,366 bp coding space and unstable CAG sequence that codes glutamine on 5" terminal. Glutamine 125-134 huntingtin Homo sapiens 19-23 11723754-7 2001 The mutated huntingtin has an elongated stretch of glutamines which leads to a gain of function such as overactivity, excitotoxicity, or to interactions with other proteins. Glutamine 51-61 huntingtin Homo sapiens 12-22 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. Glutamine 95-105 huntingtin Homo sapiens 4-14 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. Glutamine 167-177 huntingtin Homo sapiens 4-14