PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 Mus musculus 154-158 9949199-1 1999 Huntington"s disease (HD) is an inherited, neurodegenerative disorder caused by the expansion of a glutamine repeat in the N-terminus of the huntingtin protein. Glutamine 99-108 huntingtin Mus musculus 141-151 9949199-2 1999 To gain insight into the pathogenesis of HD, we generated transgenic mice that express a cDNA encoding an N-terminal fragment (171 amino acids) of huntingtin with 82, 44 or 18 glutamines. Glutamine 176-186 huntingtin Mus musculus 147-157 9599014-1 1998 HAP1 (huntingtin associated protein) has previously been found to interact with huntingtin (htt) in a glutamine length dependent manner and has been proposed to play a role in the cell specific neurodegeneration observed in Huntington"s disease (HD). Glutamine 102-111 huntingtin Mus musculus 6-16 9599014-1 1998 HAP1 (huntingtin associated protein) has previously been found to interact with huntingtin (htt) in a glutamine length dependent manner and has been proposed to play a role in the cell specific neurodegeneration observed in Huntington"s disease (HD). Glutamine 102-111 huntingtin Mus musculus 92-95 8009370-6 1994 Despite the overall high level of conservation, Hdh possesses an imperfect CAG repeat encoding only seven consecutive glutamines, compared to the 13-36 residues that are normal in man. Glutamine 118-128 huntingtin Mus musculus 48-51 35305696-1 2022 BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder whereby mutated huntingtin protein (mHTT) aggregates when polyglutamine repeats in the N-terminal of mHTT exceeds 36 glutamines (Q). Glutamine 187-197 huntingtin Mus musculus 86-96 35246273-4 2022 Although the sequence with expanded polyglutamine could not be identified by liquid-chromatography mass spectrometry, amino acid analysis revealed that glutamine of the huntingtin inclusion-rich fraction increased significantly. Glutamine 152-161 huntingtin Mus musculus 169-179 32754987-1 2021 Huntington"s disease (HD) is a neurodegenerative disorder caused by a glutamine expansion at the first exon of the huntingtin gene. Glutamine 70-79 huntingtin Mus musculus 115-125 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 Mus musculus 98-102 28270748-3 2017 This results in the production of mutant HTT protein with an increased stretch of glutamines near the N-terminus. Glutamine 82-92 huntingtin Mus musculus 41-44 29233555-2 2018 Expansion of the glutamine-encoding repeat in the Huntingtin (HTT) gene causes broad effects that are a challenge for single treatment strategies. Glutamine 17-26 huntingtin Mus musculus 50-60 29233555-2 2018 Expansion of the glutamine-encoding repeat in the Huntingtin (HTT) gene causes broad effects that are a challenge for single treatment strategies. Glutamine 17-26 huntingtin Mus musculus 62-65 30902619-1 2019 Huntington"s disease (HD) is a progressive ultimately fatal disorder caused by a glutamine-encoding CAG expansion in the huntingtin (HTT) gene that results in degeneration mainly in striatal and cerebro-cortical brain regions. Glutamine 81-90 huntingtin Mus musculus 121-131 30902619-1 2019 Huntington"s disease (HD) is a progressive ultimately fatal disorder caused by a glutamine-encoding CAG expansion in the huntingtin (HTT) gene that results in degeneration mainly in striatal and cerebro-cortical brain regions. Glutamine 81-90 huntingtin Mus musculus 133-136 29713895-9 2018 Furthermore, we found that only SV2C expression was progressively inhibited in N2a cells expressing a mutant Htt containing 120 glutamine repeats. Glutamine 128-137 huntingtin Mus musculus 109-112 26691307-8 2015 Both of the cell lines expressing huntingtin with 111 glutamines showed a large reduction in nearly all of the peptides detected in the cells, relative to levels of these peptides in cells homozygous for 7 glutamines. Glutamine 54-64 huntingtin Mus musculus 34-44 27147652-1 2016 UNLABELLED: Huntington"s disease (HD) is a heritable neurodegenerative disorder caused by expansion of CAG (glutamine) repeats in the HTT gene. Glutamine 108-117 huntingtin Mus musculus 134-137 26691307-8 2015 Both of the cell lines expressing huntingtin with 111 glutamines showed a large reduction in nearly all of the peptides detected in the cells, relative to levels of these peptides in cells homozygous for 7 glutamines. Glutamine 206-216 huntingtin Mus musculus 34-44 24381308-1 2014 Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by abnormal expansion of glutamine repeats in the protein huntingtin. Glutamine 101-110 huntingtin Mus musculus 134-144 26048156-1 2015 Huntington"s disease (HD) is caused by an expansion of glutamine repeats in the huntingtin protein (mHtt) that invokes early and prominent damage of the striatum, a region that controls motor behaviors. Glutamine 55-64 huntingtin Mus musculus 80-90 25348412-2 2014 The resulting elongated glutamine (poly-Q) sequence of mutant huntingtin (mhtt) affects both central neurons and skeletal muscle. Glutamine 24-33 huntingtin Mus musculus 62-72 25268775-1 2014 Huntington"s disease (HD) is neurodegenerative disorder for which the mutation results in an extra-long tract of glutamines that causes the huntingtin protein to aggregate. Glutamine 113-123 huntingtin Mus musculus 140-150 24938402-3 2014 Using the BACHD mice that express the full-length mutant huntingtin (mHtt) protein with 97 glutamine repeats, we first demonstrated localized in vivo changes in brain glucose use reminiscent of what is observed in premanifest HD carriers. Glutamine 91-100 huntingtin Mus musculus 57-67 22698685-4 2012 A role for TG2 in HD has been suggested because a polypeptide-bound glutamine is a rate-limiting factor for a TG2-catalyzed reaction, and TG2 can cross-link mutant huntingtin in vitro. Glutamine 68-77 huntingtin Mus musculus 164-174 23549885-1 2013 Huntington"s disease (HD) is an autosomal dominant hereditary disease caused by a trinucleotide repeat mutation in the huntingtin gene that results in an increased number of glutamine residues in the N terminus of huntingtin protein. Glutamine 174-183 huntingtin Mus musculus 119-129 23549885-1 2013 Huntington"s disease (HD) is an autosomal dominant hereditary disease caused by a trinucleotide repeat mutation in the huntingtin gene that results in an increased number of glutamine residues in the N terminus of huntingtin protein. Glutamine 174-183 huntingtin Mus musculus 214-224 22045254-2 2012 Previously we found that primary neurons from embryonic cortex of mice bearing the Huntington"s disease mutation (140 glutamines inserted into exon 1 of huntingtin) showed higher levels of reactive oxygen species before cell death. Glutamine 118-128 huntingtin Mus musculus 153-163 21272613-1 2012 Huntington"s disease is caused by a single mutation on the HTT gene which produces an expansion in the number of glutamine repeats present in the huntingtin protein. Glutamine 113-122 huntingtin Mus musculus 59-62 21272613-1 2012 Huntington"s disease is caused by a single mutation on the HTT gene which produces an expansion in the number of glutamine repeats present in the huntingtin protein. Glutamine 113-122 huntingtin Mus musculus 146-156 22649225-1 2012 Huntington"s disease (HD) is caused by a mutation in the huntingtin (htt) gene encoding an expansion of glutamine repeats at the N terminus of the Htt protein. Glutamine 104-113 huntingtin Mus musculus 57-67 22649225-1 2012 Huntington"s disease (HD) is caused by a mutation in the huntingtin (htt) gene encoding an expansion of glutamine repeats at the N terminus of the Htt protein. Glutamine 104-113 huntingtin Mus musculus 69-72 22649225-1 2012 Huntington"s disease (HD) is caused by a mutation in the huntingtin (htt) gene encoding an expansion of glutamine repeats at the N terminus of the Htt protein. Glutamine 104-113 huntingtin Mus musculus 147-150 22589249-1 2012 Huntington"s disease (HD) is an incurable neurological disorder caused by an abnormal glutamine repeat expansion in the huntingtin (Htt) protein. Glutamine 86-95 huntingtin Mus musculus 120-130 22589249-1 2012 Huntington"s disease (HD) is an incurable neurological disorder caused by an abnormal glutamine repeat expansion in the huntingtin (Htt) protein. Glutamine 86-95 huntingtin Mus musculus 132-135 22508027-3 2012 HD is a heritable neurodegenerative disease caused by a mutation resulting in an increased number of glutamines (Q) within a polyglutamine tract in Huntingtin (Htt). Glutamine 101-111 huntingtin Mus musculus 148-158 22508027-3 2012 HD is a heritable neurodegenerative disease caused by a mutation resulting in an increased number of glutamines (Q) within a polyglutamine tract in Huntingtin (Htt). Glutamine 101-111 huntingtin Mus musculus 160-163 22227000-1 2012 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an excessive expansion of a CAG trinucleotide repeat in the gene encoding the protein huntingtin, resulting in an elongated stretch of glutamines near the N-terminus of the protein. Glutamine 223-233 huntingtin Mus musculus 174-184 21059370-3 2011 We tested this hypothesis in striatal cells from the expanded glutamine huntingtin knock-in mouse (STHdh(Q111/Q111)) and wild type (STHdh(Q7/Q7)) striatal neurons. Glutamine 62-71 huntingtin Mus musculus 72-82 21245084-1 2011 An expanded polyglutamine tract (>37 glutamines) in the N-terminal region of huntingtin (htt) causes htt to accumulate in the nucleus, leading to transcriptional dysregulation in Huntington disease (HD). Glutamine 37-47 huntingtin Mus musculus 77-87 21245084-1 2011 An expanded polyglutamine tract (>37 glutamines) in the N-terminal region of huntingtin (htt) causes htt to accumulate in the nucleus, leading to transcriptional dysregulation in Huntington disease (HD). Glutamine 37-47 huntingtin Mus musculus 89-92 21245084-1 2011 An expanded polyglutamine tract (>37 glutamines) in the N-terminal region of huntingtin (htt) causes htt to accumulate in the nucleus, leading to transcriptional dysregulation in Huntington disease (HD). Glutamine 37-47 huntingtin Mus musculus 101-104 22179316-2 2011 Here we show that Sirt1 has a neuroprotective role in models of Huntington"s disease, an inherited neurodegenerative disorder caused by a glutamine repeat expansion in huntingtin protein (HTT). Glutamine 138-147 huntingtin Mus musculus 168-178 22179316-2 2011 Here we show that Sirt1 has a neuroprotective role in models of Huntington"s disease, an inherited neurodegenerative disorder caused by a glutamine repeat expansion in huntingtin protein (HTT). Glutamine 138-147 huntingtin Mus musculus 188-191 21044321-1 2010 Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain. Glutamine 49-58 huntingtin Mus musculus 111-121 21044321-1 2010 Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain. Glutamine 49-58 huntingtin Mus musculus 123-126 21044321-1 2010 Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain. Glutamine 71-81 huntingtin Mus musculus 111-121 21044321-1 2010 Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain. Glutamine 71-81 huntingtin Mus musculus 123-126 21044321-2 2010 N171-82Q mice that express N-terminal 171 amino acids of htt with an 82-glutamine repeat show severe neurological phenotypes and die early, suggesting that N-terminal mutant htt is pathogenic. Glutamine 72-81 huntingtin Mus musculus 57-60 21044321-2 2010 N171-82Q mice that express N-terminal 171 amino acids of htt with an 82-glutamine repeat show severe neurological phenotypes and die early, suggesting that N-terminal mutant htt is pathogenic. Glutamine 72-81 huntingtin Mus musculus 174-177 18537673-1 2008 Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by the expansion of a polymorphic CAG trinucleotide repeat encoding a poly-glutamine tract within the Huntingtin protein. Glutamine 161-170 huntingtin Mus musculus 188-198 20519964-1 2010 Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD). Glutamine 79-89 huntingtin Mus musculus 7-17 20519964-1 2010 Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD). Glutamine 79-89 huntingtin Mus musculus 19-22 20519964-1 2010 Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD). Glutamine 79-89 huntingtin Mus musculus 129-132 19864571-1 2009 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease resulting from the expansion of a glutamine repeat in the huntingtin (Htt) protein. Glutamine 111-120 huntingtin Mus musculus 135-145 19864571-1 2009 Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease resulting from the expansion of a glutamine repeat in the huntingtin (Htt) protein. Glutamine 111-120 huntingtin Mus musculus 147-150 18650014-5 2008 We established stably transfected mouse neuroblastoma (N2a) cells that express soluble amino-terminal fragments of huntingtin containing 20 (20Q) or 150 (150Q) glutamine repeats. Glutamine 160-169 huntingtin Mus musculus 115-125 18558632-6 2008 Similarly, transgenic monkeys expressing exon-1 htt with a 147-glutamine repeat (147Q) died early and showed abundant neuropil aggregates in swelling neuronal processes. Glutamine 63-72 huntingtin Mus musculus 48-51 17947297-1 2008 Expansion of polymorphic glutamine (Q) numbers present at the protein Huntingtin (Htt) beyond 36Q results in its misfolding and aggregation, and the aggregates recruit several other proteins. Glutamine 25-34 huntingtin Mus musculus 70-80 17947297-1 2008 Expansion of polymorphic glutamine (Q) numbers present at the protein Huntingtin (Htt) beyond 36Q results in its misfolding and aggregation, and the aggregates recruit several other proteins. Glutamine 25-34 huntingtin Mus musculus 82-85 19860865-1 2009 BACKGROUND: Huntington"s disease (HD) is an inherited neurogenerative disease caused by an abnormal expansion of glutamine repeats in the huntingtin protein. Glutamine 113-122 huntingtin Mus musculus 138-148 17947297-0 2008 HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Glutamine 114-124 huntingtin Mus musculus 8-18 17947297-0 2008 HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Glutamine 114-124 huntingtin Mus musculus 95-105 17925440-1 2007 Huntington"s disease (HD) is a progressive neurodegenerative disease caused by a glutamine expansion within huntingtin protein. Glutamine 81-90 huntingtin Mus musculus 108-118 16443291-2 2006 Transgenic mice expressing the N-terminal of huntingtin, containing 82 glutamines, exhibit a progressive disorder, which resembles to the human disease. Glutamine 71-81 huntingtin Mus musculus 45-55 17708681-1 2007 The Huntington"s disease (HD) CAG repeat, encoding a polymorphic glutamine tract in huntingtin, is inversely correlated with cellular energy level, with alleles over approximately 37 repeats leading to the loss of striatal neurons. Glutamine 65-74 huntingtin Mus musculus 84-94 17396163-7 2007 The first 171 amino acids of wild-type huntingtin, and its glutamine expanded mutant form, interacted with copper, but not iron. Glutamine 59-68 huntingtin Mus musculus 39-49 17027958-1 2006 Hippi functions as an adapter protein that mediates pro-apoptotic signaling from poly-glutamine-expanded huntingtin, an established cause of Huntington disease, to the extrinsic cell death pathway. Glutamine 86-95 huntingtin Mus musculus 105-115 17018277-1 2006 Huntington"s disease (HD) is an inherited neurodegenerative disease caused by a glutamine repeat expansion in huntingtin protein. Glutamine 80-89 huntingtin Mus musculus 110-120 17272267-1 2007 Huntington disease (HD) is an autosomal dominant neurodegenerative disease that results from a CAG (glutamine) trinucleotide expansion in exon 1 of huntingtin (Htt). Glutamine 100-109 huntingtin Mus musculus 148-158 17272267-1 2007 Huntington disease (HD) is an autosomal dominant neurodegenerative disease that results from a CAG (glutamine) trinucleotide expansion in exon 1 of huntingtin (Htt). Glutamine 100-109 huntingtin Mus musculus 160-163 16403806-1 2006 Huntingtin (htt), the protein encoded by the Huntington"s disease (HD) gene, contains a polymorphic stretch of glutamines (polyQ) near its N-terminus. Glutamine 111-121 huntingtin Mus musculus 0-10 16403806-1 2006 Huntingtin (htt), the protein encoded by the Huntington"s disease (HD) gene, contains a polymorphic stretch of glutamines (polyQ) near its N-terminus. Glutamine 111-121 huntingtin Mus musculus 12-15 12969246-1 2003 Huntington"s disease (HD) is an autosomal dominant disorder caused by an expansion in the number of glutamine repeats in the N-terminal region of the huntingtin protein. Glutamine 100-109 huntingtin Mus musculus 150-160 16137562-1 2005 Huntington"s disease (HD) is a neurodegenerative disorder caused by an elongated glutamine repeat in huntingtin. Glutamine 81-90 huntingtin Mus musculus 101-111 15190011-1 2004 Huntington"s disease (HD) results from the expansion of a glutamine repeat near the N-terminus of huntingtin (htt). Glutamine 58-67 huntingtin Mus musculus 98-108 15190011-1 2004 Huntington"s disease (HD) results from the expansion of a glutamine repeat near the N-terminus of huntingtin (htt). Glutamine 58-67 huntingtin Mus musculus 110-113 15190011-3 2004 This pathology has been reproduced in transgenic mice expressing the first 171 amino acids of htt with 82 glutamines along with losses of motoric function, hypoactivity and abbreviated life-span. Glutamine 106-116 huntingtin Mus musculus 94-97 15280037-1 2004 Nuclear aggregates of enhanced green fluorescent protein and nuclear localization signal-fused truncated N-terminal huntingtin containing 150 repeats of glutamine residue were purified from ecdysine-inducible mutant neuro2A cell line by sequential extraction of nuclear soluble proteins. Glutamine 153-162 huntingtin Mus musculus 116-126 15654337-3 2005 N-terminal fragments of mutant htt, which contain a polyQ expansion (>37 glutamines), have no conserved nuclear localization sequences or nuclear export sequences but can accumulate in the nucleus and cause neurological problems in transgenic mice. Glutamine 73-83 huntingtin Mus musculus 31-34 11960015-1 2002 The exon-1 peptide of huntingtin has 51 Gln repeats and produces the symptoms of Huntington"s disease in transgenic mice. Glutamine 40-43 huntingtin Mus musculus 22-32 12657678-8 2003 Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments. Glutamine 132-141 huntingtin Mus musculus 43-53 12657678-8 2003 Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments. Glutamine 132-141 huntingtin Mus musculus 82-92 12657678-8 2003 Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments. Glutamine 132-141 huntingtin Mus musculus 82-92 12657678-8 2003 Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments. Glutamine 132-141 huntingtin Mus musculus 82-92 12417652-1 2002 Aggregates of green fluorescent protein (GFP)-fused truncated N-terminal huntingtin containing abnormally long polyglutamine tracts (150 repeats of glutamine residue) were purified from an ecdysone-inducible mutant neuro2A cell line (HD150Q-28) by using a fluorescence-activated cell sorter. Glutamine 115-124 huntingtin Mus musculus 73-83 12217951-1 2002 The hallmark striatal neurodegeneration of Huntington"s disease (HD) is first triggered by a dominant property of the expanded glutamine tract in mutant huntingtin that increases in severity with glutamine size. Glutamine 127-136 huntingtin Mus musculus 153-163 12217951-1 2002 The hallmark striatal neurodegeneration of Huntington"s disease (HD) is first triggered by a dominant property of the expanded glutamine tract in mutant huntingtin that increases in severity with glutamine size. Glutamine 196-205 huntingtin Mus musculus 153-163 12217951-2 2002 Indeed 111-glutamine murine huntingtin leads to a dominant cascade of phenotypes in Hdh(Q111) mice, although these abnormalities are not manifest in Hdh(Q50) mice, with 50-glutamine mutant protein. Glutamine 11-20 huntingtin Mus musculus 28-38 12217951-2 2002 Indeed 111-glutamine murine huntingtin leads to a dominant cascade of phenotypes in Hdh(Q111) mice, although these abnormalities are not manifest in Hdh(Q50) mice, with 50-glutamine mutant protein. Glutamine 11-20 huntingtin Mus musculus 84-87 12217951-2 2002 Indeed 111-glutamine murine huntingtin leads to a dominant cascade of phenotypes in Hdh(Q111) mice, although these abnormalities are not manifest in Hdh(Q50) mice, with 50-glutamine mutant protein. Glutamine 172-181 huntingtin Mus musculus 28-38 12193654-15 2002 Here we show that structural analyses of soluble huntingtin exon 1 fusion proteins with 16 to 46 glutamine residues reveal extended structures with random coil characteristics and no evidence for a global conformational change above 36 glutamines. Glutamine 97-106 huntingtin Mus musculus 49-59 12554681-4 2003 The absence of Msh2 also eliminated striatal mutant huntingtin with somatically expanded glutamine tracts and caused an approximately 5 month delay in nuclear mutant protein accumulation, but did not alter the striatal specificity of this early phenotype. Glutamine 89-98 huntingtin Mus musculus 52-62 12554681-5 2003 Thus, somatic HD CAG instability appears to be a consequence of a striatal-selective disease process that accelerates the timing of an early disease phenotype, via expansion of the glutamine tract in mutant huntingtin. Glutamine 181-190 huntingtin Mus musculus 207-217 11912178-3 2002 In young Hdh knock-in mice, CAGs that expand the glutamine tract in mouse huntingtin to childhood-onset HD lengths lead to nuclear accumulation of full-length mutant huntingtin and later accumulation of insoluble fragment. Glutamine 49-58 huntingtin Mus musculus 9-12 11912178-3 2002 In young Hdh knock-in mice, CAGs that expand the glutamine tract in mouse huntingtin to childhood-onset HD lengths lead to nuclear accumulation of full-length mutant huntingtin and later accumulation of insoluble fragment. Glutamine 49-58 huntingtin Mus musculus 74-84 11912178-3 2002 In young Hdh knock-in mice, CAGs that expand the glutamine tract in mouse huntingtin to childhood-onset HD lengths lead to nuclear accumulation of full-length mutant huntingtin and later accumulation of insoluble fragment. Glutamine 49-58 huntingtin Mus musculus 166-176 10699173-0 2000 Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice. Glutamine 5-14 huntingtin Mus musculus 68-78 11839795-2 2002 In HD, N-terminal fragments of huntingtin with an expanded glutamine tract are able to aggregate and accumulate in the nucleus. Glutamine 59-68 huntingtin Mus musculus 31-41 10932179-1 2000 Huntington disease (HD) is caused by expansion of a glutamine repeat in the amino-terminal region of huntingtin. Glutamine 52-61 huntingtin Mus musculus 101-111 10699173-1 2000 Huntington"s disease (HD) is caused by an expanded N-terminal glutamine tract that endows huntingtin with a striatal-selective structural property ultimately toxic to medium spiny neurons. Glutamine 62-71 huntingtin Mus musculus 90-100 10699173-3 2000 These changes show glutamine length dependence and dominant inheritance with recruitment of wild-type protein, critical features of the altered HD property that strongly implicate them in the HD disease process and that suggest alternative pathogenic scenarios: the effect of the glutamine tract may act by altering interaction with a critical cellular constituent or by depleting a form of huntingtin essential to medium spiny striatal neurons. Glutamine 19-28 huntingtin Mus musculus 391-401 10699173-3 2000 These changes show glutamine length dependence and dominant inheritance with recruitment of wild-type protein, critical features of the altered HD property that strongly implicate them in the HD disease process and that suggest alternative pathogenic scenarios: the effect of the glutamine tract may act by altering interaction with a critical cellular constituent or by depleting a form of huntingtin essential to medium spiny striatal neurons. Glutamine 280-289 huntingtin Mus musculus 391-401