PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
23853009-4	2013	Initially the clinical picture suggested the diagnosis of a dominant SCA, but finally a diagnosis of HD was made based on the molecular evidence of abnormal 39 Cytosine-Adenine-Guanine (CAG) repeats in exon 1 of Huntingtin gene.	cytosine-adenine-guanine	160-184	huntingtin	Homo sapiens	212-222
23853009-4	2013	Initially the clinical picture suggested the diagnosis of a dominant SCA, but finally a diagnosis of HD was made based on the molecular evidence of abnormal 39 Cytosine-Adenine-Guanine (CAG) repeats in exon 1 of Huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	186-189	huntingtin	Homo sapiens	212-222
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
23853712-2	2013	Mutant huntingtin is known to aggregate, a process that can be inhibited by the eukaryotic chaperonin TRiC (TCP1-ring complex) in vitro and in vivo.	tric	102-106	huntingtin	Homo sapiens	7-17
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
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
23861941-3	2013	Indeed, wild-type Huntingtin plays a protective role with respect to polyQ-hHtt induced defects.	polyq-hhtt	69-79	huntingtin	Homo sapiens	18-28
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
23557875-3	2013	Huntington disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat expansion in the coding region of the huntingtin (HTT) gene.	cytosine-adenine-guanine	98-122	huntingtin	Homo sapiens	182-192
23557875-3	2013	Huntington disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat expansion in the coding region of the huntingtin (HTT) gene.	cytosine-adenine-guanine	98-122	huntingtin	Homo sapiens	194-197
23557875-3	2013	Huntington disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat expansion in the coding region of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	124-127	huntingtin	Homo sapiens	182-192
23557875-3	2013	Huntington disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat expansion in the coding region of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	124-127	huntingtin	Homo sapiens	194-197
23570994-3	2013	We hypothesized that ozone exposure alters the normal pattern of serotonin, its transporter (5-HTT), and two key receptors (5-HT2A and 5-HT4), a pathway involved in postnatal airway neural, epithelial, and immune processes.	Serotonin	65-74	huntingtin	Homo sapiens	95-98
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
22993450-2	2013	Differentiating among these HD-like syndromes is necessary when a patient with a combination of movement disorders, cognitive decline, behavioural abnormalities and progressive disease course proves negative to the genetic testing for HD causative mutations, that is, IT15 gene trinucleotide-repeat expansion.	trinucleotide	278-291	huntingtin	Homo sapiens	268-272
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
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
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
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.	trinucleotide	78-91	huntingtin	Homo sapiens	123-126
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	93-96	huntingtin	Homo sapiens	123-126
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
23370273-0	2013	Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues.	Histidine	129-138	huntingtin	Homo sapiens	76-86
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
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 ].	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	171-174	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 ].	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	171-174	huntingtin	Homo sapiens	132-135
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
23819039-6	2013	Tissue transglutaminase is another factor that promotes the aggregation of mutant proteins; the inhibition of its activity with cystamine was found to prevent aggregate formation of mutant huntingtin and SOD1.	Cystamine	128-137	huntingtin	Homo sapiens	189-199
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
23458159-1	2013	Huntington"s disease is caused by a polyglutamine expansion in huntingtin.	polyglutamine	36-49	huntingtin	Homo sapiens	63-73
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
23319588-7	2013	Nuclear export of Htt is sensitive to leptomycin B and is reduced by knockdown of exportin 1.	leptomycin B	38-50	huntingtin	Homo sapiens	18-21
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
22422149-3	2013	According to previous studies, the exon 1 region of the huntingtin (HTT) gene with expanded CAG trinucleotide repeats plays a critical role in causing HD.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	92-95	huntingtin	Homo sapiens	68-71
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
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
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
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
22422149-3	2013	According to previous studies, the exon 1 region of the huntingtin (HTT) gene with expanded CAG trinucleotide repeats plays a critical role in causing HD.	trinucleotide	96-109	huntingtin	Homo sapiens	68-71
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
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
24209441-2	2013	The cause of HD is an expanded CAG trinucleotide repeat in the Htt gene.	trinucleotide	35-48	huntingtin	Homo sapiens	63-66
25062673-0	2013	Huntingtin interactions with membrane phospholipids: strategic targets for therapeutic intervention?	Phospholipids	38-51	huntingtin	Homo sapiens	0-10
25062673-4	2013	Recent investigations prove that Htt associates with membranes by direct interactions with phospholipids in membranes.	Phospholipids	91-104	huntingtin	Homo sapiens	33-36
25062673-6	2013	Htt has a particular affinity for a specific class of phospholipids called phosphatidylinositol phosphates; individual species of these phospholipids propagate signals promoting cell survival and regulating changes in morphology.	Phospholipids	54-67	huntingtin	Homo sapiens	0-3
25062673-6	2013	Htt has a particular affinity for a specific class of phospholipids called phosphatidylinositol phosphates; individual species of these phospholipids propagate signals promoting cell survival and regulating changes in morphology.	Phosphatidylinositol Phosphates	75-106	huntingtin	Homo sapiens	0-3
25062673-6	2013	Htt has a particular affinity for a specific class of phospholipids called phosphatidylinositol phosphates; individual species of these phospholipids propagate signals promoting cell survival and regulating changes in morphology.	Phospholipids	136-149	huntingtin	Homo sapiens	0-3
25062673-7	2013	Mutant Htt fragments can disrupt synthetic phospholipid bilayers and full-length mutant Htt shows increased binding to numerous phospholipids, supporting the idea that mutant Htt can introduce pathology at the level of phospholipid interactions.	Phospholipids	43-55	huntingtin	Homo sapiens	7-10
25062673-7	2013	Mutant Htt fragments can disrupt synthetic phospholipid bilayers and full-length mutant Htt shows increased binding to numerous phospholipids, supporting the idea that mutant Htt can introduce pathology at the level of phospholipid interactions.	Phospholipids	128-141	huntingtin	Homo sapiens	88-91
25062673-7	2013	Mutant Htt fragments can disrupt synthetic phospholipid bilayers and full-length mutant Htt shows increased binding to numerous phospholipids, supporting the idea that mutant Htt can introduce pathology at the level of phospholipid interactions.	Phospholipids	128-141	huntingtin	Homo sapiens	88-91
25062673-9	2013	Understanding the relationship of Htt with membrane phospholipids, and the impact of mutant Htt on membrane-related functions and lipid metabolism, may help identify new modes of therapeutic intervention for Huntington"s disease.	Phospholipids	52-65	huntingtin	Homo sapiens	34-37
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
25062733-1	2013	BACKGROUND: Huntington"s disease is caused by expansion of CAG trinucleotide repeats in the first exon of the huntingtin gene, which is essential for both development and neurogenesis.	trinucleotide	63-76	huntingtin	Homo sapiens	110-120
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
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
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
23157165-10	2012	This work highlights the innate ability of CAG/CTG repeats to incorporate and to position in nucleosomes and how that behavior is modulated by the htt flanking sequence.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	43-46	huntingtin	Homo sapiens	147-150
24217578-2	2013	However, growing evidence implicates soluble oligomeric polyglutamine-expanded huntingtin in cytotoxicity.	polyglutamine	56-69	huntingtin	Homo sapiens	79-89
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
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
23157165-10	2012	This work highlights the innate ability of CAG/CTG repeats to incorporate and to position in nucleosomes and how that behavior is modulated by the htt flanking sequence.	ctg	47-50	huntingtin	Homo sapiens	147-150
22627493-1	2012	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a CAG trinucleotide expansion in the Huntingtin (Htt) gene.	trinucleotide	93-106	huntingtin	Homo sapiens	124-134
22627493-1	2012	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a CAG trinucleotide expansion in the Huntingtin (Htt) gene.	trinucleotide	93-106	huntingtin	Homo sapiens	136-139
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
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
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
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
23042244-1	2012	Huntington"s disease is an incurable neurodegenerative disorder caused by expansion of a CAG trinucleotide repeat within one allele of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	89-92	huntingtin	Homo sapiens	139-149
23042244-1	2012	Huntington"s disease is an incurable neurodegenerative disorder caused by expansion of a CAG trinucleotide repeat within one allele of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	89-92	huntingtin	Homo sapiens	151-154
23042244-1	2012	Huntington"s disease is an incurable neurodegenerative disorder caused by expansion of a CAG trinucleotide repeat within one allele of the huntingtin (HTT) gene.	trinucleotide	93-106	huntingtin	Homo sapiens	139-149
23042244-1	2012	Huntington"s disease is an incurable neurodegenerative disorder caused by expansion of a CAG trinucleotide repeat within one allele of the huntingtin (HTT) gene.	trinucleotide	93-106	huntingtin	Homo sapiens	151-154
23042244-3	2012	We have previously demonstrated that mismatch-containing duplex RNAs complementary to the expanded trinucleotide repeat are potent and allele-selective inhibitors of mutant HTT expression, but the mechanism of allele selectivity was not explored.	trinucleotide	99-112	huntingtin	Homo sapiens	173-176
22999956-4	2012	Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice.	Serine	0-7	huntingtin	Homo sapiens	72-82
23012356-0	2012	Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin protein.	Proline	44-51	huntingtin	Homo sapiens	92-102
23012356-0	2012	Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin protein.	Tyrosine	52-60	huntingtin	Homo sapiens	92-102
23012356-3	2012	Here, using a live cell assay and affinity chromatography, we show that huntingtin has a karyopherin beta2-dependent proline-tyrosine (PY)-NLS in the amino terminus of the protein.	Proline	117-124	huntingtin	Homo sapiens	72-82
23012356-3	2012	Here, using a live cell assay and affinity chromatography, we show that huntingtin has a karyopherin beta2-dependent proline-tyrosine (PY)-NLS in the amino terminus of the protein.	Tyrosine	125-133	huntingtin	Homo sapiens	72-82
23012356-3	2012	Here, using a live cell assay and affinity chromatography, we show that huntingtin has a karyopherin beta2-dependent proline-tyrosine (PY)-NLS in the amino terminus of the protein.	py	135-137	huntingtin	Homo sapiens	72-82
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
22835760-0	2012	Length of polyglutamine tract affects secondary and tertiary structures of huntingtin protein.	polyglutamine	10-23	huntingtin	Homo sapiens	75-85
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
22921802-6	2012	We demonstrate that FUS can non-invasively deliver siRNA-Htt directly to the striatum leading to a significant reduction of Htt expression in a dose dependent manner.	fusarubin	20-23	huntingtin	Homo sapiens	57-60
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.	trinucleotide	100-113	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.	trinucleotide	100-113	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	135-148	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	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
22921802-6	2012	We demonstrate that FUS can non-invasively deliver siRNA-Htt directly to the striatum leading to a significant reduction of Htt expression in a dose dependent manner.	fusarubin	20-23	huntingtin	Homo sapiens	124-127
22891249-4	2012	Here we focus upon aggregation of huntingtin (HTT), which causes a neurodegenerative disorder, Huntington disease, and we show that oxidation of a methionine residue in HTT occurs in vitro and also in vivo.	Methionine	147-157	huntingtin	Homo sapiens	34-44
22978784-0	2012	All-atom stability and oligomerization simulations of polyglutamine nanotubes with and without the 17-amino-acid N-terminal fragment of the Huntingtin protein.	17-amino-acid	99-112	huntingtin	Homo sapiens	140-150
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
22978784-4	2012	Its aggregation is modulated by the number of glutamine residues as well as by the surrounding amino acid sequences such as the 17-amino-acid N-terminal fragment of Huntingtin which increases the aggregation rate.	17-amino-acid	128-141	huntingtin	Homo sapiens	165-175
22891249-4	2012	Here we focus upon aggregation of huntingtin (HTT), which causes a neurodegenerative disorder, Huntington disease, and we show that oxidation of a methionine residue in HTT occurs in vitro and also in vivo.	Methionine	147-157	huntingtin	Homo sapiens	46-49
22891249-4	2012	Here we focus upon aggregation of huntingtin (HTT), which causes a neurodegenerative disorder, Huntington disease, and we show that oxidation of a methionine residue in HTT occurs in vitro and also in vivo.	Methionine	147-157	huntingtin	Homo sapiens	169-172
22891249-5	2012	Copper ions as well as added hydrogen peroxide are found to oxidize the methionine residue, but notably, this oxidative modification occurs only in the aggregated HTT but not in the soluble state.	Copper	0-6	huntingtin	Homo sapiens	163-166
22891249-5	2012	Copper ions as well as added hydrogen peroxide are found to oxidize the methionine residue, but notably, this oxidative modification occurs only in the aggregated HTT but not in the soluble state.	Hydrogen Peroxide	29-46	huntingtin	Homo sapiens	163-166
22891249-5	2012	Copper ions as well as added hydrogen peroxide are found to oxidize the methionine residue, but notably, this oxidative modification occurs only in the aggregated HTT but not in the soluble state.	Methionine	72-82	huntingtin	Homo sapiens	163-166
22891249-6	2012	Furthermore, the methionine oxidation creates additional interactions among HTT aggregates and alters overall morphologies of the aggregates.	Methionine	17-27	huntingtin	Homo sapiens	76-79
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
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
22773688-5	2012	Moreover, mitochondrial fission molecules, e.g., protein dynamin-related protein 1, as well as Htt, associated with mitochondrial raft-like microdomains, glycosphingolipid-enriched structures detectable in mitochondria.	Glycosphingolipids	154-171	huntingtin	Homo sapiens	95-98
22709585-4	2012	Striatal cells expressing mutant huntingtin show higher basal levels of mitochondrial-generated ROS and mtDNA lesions and a lower spare respiratory capacity.	ros	96-99	huntingtin	Homo sapiens	33-43
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
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).	trinucleotide	57-70	huntingtin	Homo sapiens	0-5
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
23235761-1	2012	AIM: To evaluate the role of 18F-fluorodeoxyglucose (FDG) PET/CT in: a) the selection of patients with locally advanced pancreatic cancer for helical tomotherapy with concurrent chemotherapy (HTT-ChT); b) monitoring HTT-ChT treatment efficacy in comparison with contrast-enhanced CT (c.e.CT).	Fluorodeoxyglucose F18	29-51	huntingtin	Homo sapiens	192-195
22306738-3	2012	In situ, monoclonal antibody 3B5H10 binds to different htt fragments in neurons in proportion to their toxicity.	3b5h10	29-35	huntingtin	Homo sapiens	55-58
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
22875942-0	2012	Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington"s disease models.	Methylene Blue	0-14	huntingtin	Homo sapiens	25-35
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
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
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
22974690-1	2012	Huntington"s Disease (HD) is a neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat-expansion in the Huntingtin (HTT) gene.	cytosine-adenine-guanine	70-94	huntingtin	Homo sapiens	133-143
22589249-6	2012	In cultured WT and mutant Htt striatal cells, small hairpin RNA-mediated TORC1 knockdown resulted in decreased PGC-1alpha expression and increased susceptibility to 3-NP-induced toxicity.	3-nitropropionic acid	165-169	huntingtin	Homo sapiens	26-29
22974690-1	2012	Huntington"s Disease (HD) is a neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat-expansion in the Huntingtin (HTT) gene.	cytosine-adenine-guanine	70-94	huntingtin	Homo sapiens	145-148
22974690-1	2012	Huntington"s Disease (HD) is a neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat-expansion in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	96-99	huntingtin	Homo sapiens	133-143
22974690-1	2012	Huntington"s Disease (HD) is a neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) triplet repeat-expansion in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	96-99	huntingtin	Homo sapiens	145-148
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
22648412-7	2012	trans-(-)-epsilon-Viniferin (viniferin), a natural product among our 22 collected naturally occurring and semisynthetic stilbenic compounds, significantly attenuated mutant Htt-induced depletion of SIRT3 and protected cells from mutant Htt.	trans-(-)-epsilon-viniferin	0-27	huntingtin	Homo sapiens	173-176
22648412-7	2012	trans-(-)-epsilon-Viniferin (viniferin), a natural product among our 22 collected naturally occurring and semisynthetic stilbenic compounds, significantly attenuated mutant Htt-induced depletion of SIRT3 and protected cells from mutant Htt.	trans-(-)-epsilon-viniferin	0-27	huntingtin	Homo sapiens	236-239
22648412-7	2012	trans-(-)-epsilon-Viniferin (viniferin), a natural product among our 22 collected naturally occurring and semisynthetic stilbenic compounds, significantly attenuated mutant Htt-induced depletion of SIRT3 and protected cells from mutant Htt.	Viniferin	29-38	huntingtin	Homo sapiens	173-176
22648412-7	2012	trans-(-)-epsilon-Viniferin (viniferin), a natural product among our 22 collected naturally occurring and semisynthetic stilbenic compounds, significantly attenuated mutant Htt-induced depletion of SIRT3 and protected cells from mutant Htt.	Viniferin	29-38	huntingtin	Homo sapiens	236-239
22648412-7	2012	trans-(-)-epsilon-Viniferin (viniferin), a natural product among our 22 collected naturally occurring and semisynthetic stilbenic compounds, significantly attenuated mutant Htt-induced depletion of SIRT3 and protected cells from mutant Htt.	stilbenic compounds	120-139	huntingtin	Homo sapiens	173-176
22648412-8	2012	We demonstrate that viniferin decreases levels of reactive oxygen species and prevents loss of mitochondrial membrane potential in cells expressing mutant Htt.	Viniferin	20-29	huntingtin	Homo sapiens	155-158
22648412-9	2012	Expression of mutant Htt results in decreased deacetylase activity of SIRT3 and further leads to reduction in cellular NAD(+) levels and mitochondrial biogenesis in cells.	NAD	119-125	huntingtin	Homo sapiens	21-24
22722716-10	2012	DMSO reduced not only soluble but also insoluble mtHTT (mutant huntingtin aggregates) expressions, which were masked in the presence of autophagy inhibitor.	Dimethyl Sulfoxide	0-4	huntingtin	Homo sapiens	63-73
22722716-10	2012	DMSO reduced not only soluble but also insoluble mtHTT (mutant huntingtin aggregates) expressions, which were masked in the presence of autophagy inhibitor.	mthtt	49-54	huntingtin	Homo sapiens	63-73
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
22905336-6	2012	Although mutant HTT interferes with the operation of multiple proteins related to glutamate transmission, consistent evidence links the expression of mutant HTT with reduced activity of glutamate transporter 1 (rodent GLT1 or human EAAT2), the astrocytic protein responsible for the bulk of glutamate uptake.	Glutamic Acid	82-91	huntingtin	Homo sapiens	16-19
22905336-6	2012	Although mutant HTT interferes with the operation of multiple proteins related to glutamate transmission, consistent evidence links the expression of mutant HTT with reduced activity of glutamate transporter 1 (rodent GLT1 or human EAAT2), the astrocytic protein responsible for the bulk of glutamate uptake.	Glutamic Acid	186-195	huntingtin	Homo sapiens	157-160
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
26307259-0	2012	Red/ET recombination with chimeric oligonucleotides allows rapid generation of BAC transgenes harboring full-length or truncated huntingtin cDNA.	Oligonucleotides	35-51	huntingtin	Homo sapiens	129-139
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
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
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
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
22649062-2	2012	HD is caused by a cytosine-adenine-guanine triplet-repeat expansion mutation in the Huntingtin gene, allowing early diagnosis by genetic testing.	cytosine-adenine-guanine	18-42	huntingtin	Homo sapiens	84-94
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
22415443-6	2012	3-nitropropionic acid, on the aggregation of mutant huntingtin (mthtt) protein, whose misfolding and aggregation results in cellular abnormalities characteristic of HD.	3-nitropropionic acid	0-21	huntingtin	Homo sapiens	52-62
22415443-6	2012	3-nitropropionic acid, on the aggregation of mutant huntingtin (mthtt) protein, whose misfolding and aggregation results in cellular abnormalities characteristic of HD.	mthtt	64-69	huntingtin	Homo sapiens	52-62
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.	trinucleotide	55-68	huntingtin	Homo sapiens	99-109
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
22580459-0	2012	Huntingtin protein interactions altered by polyglutamine expansion as determined by quantitative proteomic analysis.	polyglutamine	43-56	huntingtin	Homo sapiens	0-10
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
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
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
22508027-11	2012	Upon differentiation, the Htt(7Q/7Q) and Htt(140Q/140Q) generated numerous Beta(III)-Tubulin- and GABA-positive neurons; however, after 15 days the cellular architecture of the differentiated Htt(140Q/140Q) cultures changed compared to Htt(7Q/7Q) cultures and included a marked increase of GFAP-positive cells.	gamma-Aminobutyric Acid	98-102	huntingtin	Homo sapiens	26-29
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
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.	cytosine-adenine-guanine	27-51	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.	cytosine-adenine-guanine	27-51	huntingtin	Homo sapiens	152-162
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	53-56	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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	53-56	huntingtin	Homo sapiens	152-162
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
22508027-11	2012	Upon differentiation, the Htt(7Q/7Q) and Htt(140Q/140Q) generated numerous Beta(III)-Tubulin- and GABA-positive neurons; however, after 15 days the cellular architecture of the differentiated Htt(140Q/140Q) cultures changed compared to Htt(7Q/7Q) cultures and included a marked increase of GFAP-positive cells.	gamma-Aminobutyric Acid	98-102	huntingtin	Homo sapiens	41-44
22508027-11	2012	Upon differentiation, the Htt(7Q/7Q) and Htt(140Q/140Q) generated numerous Beta(III)-Tubulin- and GABA-positive neurons; however, after 15 days the cellular architecture of the differentiated Htt(140Q/140Q) cultures changed compared to Htt(7Q/7Q) cultures and included a marked increase of GFAP-positive cells.	gamma-Aminobutyric Acid	98-102	huntingtin	Homo sapiens	41-44
22508027-11	2012	Upon differentiation, the Htt(7Q/7Q) and Htt(140Q/140Q) generated numerous Beta(III)-Tubulin- and GABA-positive neurons; however, after 15 days the cellular architecture of the differentiated Htt(140Q/140Q) cultures changed compared to Htt(7Q/7Q) cultures and included a marked increase of GFAP-positive cells.	gamma-Aminobutyric Acid	98-102	huntingtin	Homo sapiens	41-44
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
22375012-7	2012	A soluble mutant htt fragment of about 180 kDa was detected with anti-htt antibody Ab1 (htt-(1-17)) and increased when lysates were treated with denaturants (SDS, 8 M urea, DTT, or trypsin) before BNP.	denaturants	145-156	huntingtin	Homo sapiens	17-20
22375012-7	2012	A soluble mutant htt fragment of about 180 kDa was detected with anti-htt antibody Ab1 (htt-(1-17)) and increased when lysates were treated with denaturants (SDS, 8 M urea, DTT, or trypsin) before BNP.	Sodium Dodecyl Sulfate	158-161	huntingtin	Homo sapiens	17-20
22375012-7	2012	A soluble mutant htt fragment of about 180 kDa was detected with anti-htt antibody Ab1 (htt-(1-17)) and increased when lysates were treated with denaturants (SDS, 8 M urea, DTT, or trypsin) before BNP.	Urea	167-171	huntingtin	Homo sapiens	17-20
22375012-7	2012	A soluble mutant htt fragment of about 180 kDa was detected with anti-htt antibody Ab1 (htt-(1-17)) and increased when lysates were treated with denaturants (SDS, 8 M urea, DTT, or trypsin) before BNP.	Dithiothreitol	173-176	huntingtin	Homo sapiens	17-20
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
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
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
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
22371559-6	2012	Although synthetically polyubiquitinated N-htt competed with other Ub conjugates for access to the proteasome, the vast majority of mutant N-htt in cells was not Ub conjugated.	Nitrogen	41-42	huntingtin	Homo sapiens	43-46
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
22198539-1	2012	Huntington"s disease (HD) is a fatal, autosomal dominant neurodegenerative disorder caused by an expanded trinucleotide (CAG) repeat in exon 1 of the huntingtin gene (Htt).	trinucleotide	106-119	huntingtin	Homo sapiens	150-160
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
22198539-1	2012	Huntington"s disease (HD) is a fatal, autosomal dominant neurodegenerative disorder caused by an expanded trinucleotide (CAG) repeat in exon 1 of the huntingtin gene (Htt).	trinucleotide	106-119	huntingtin	Homo sapiens	167-170
22198539-1	2012	Huntington"s disease (HD) is a fatal, autosomal dominant neurodegenerative disorder caused by an expanded trinucleotide (CAG) repeat in exon 1 of the huntingtin gene (Htt).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	121-124	huntingtin	Homo sapiens	150-160
22198539-1	2012	Huntington"s disease (HD) is a fatal, autosomal dominant neurodegenerative disorder caused by an expanded trinucleotide (CAG) repeat in exon 1 of the huntingtin gene (Htt).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	121-124	huntingtin	Homo sapiens	167-170
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
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
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
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
22178474-0	2012	Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.	polyglutamine	79-92	huntingtin	Homo sapiens	104-114
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	76-79
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.	17-amino-acid	4-17	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.	17-amino-acid	4-17	huntingtin	Homo sapiens	133-143
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	96-106
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.	17-amino-acid	4-17	huntingtin	Homo sapiens	145-148
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
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	108-111
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
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	108-111
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).	Proline	59-66	huntingtin	Homo sapiens	109-112
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
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
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
22334892-8	2012	Mutant Htt also hinders glutamate uptake from the synaptic cleft by down-regulating ERK-dependent expression of glutamate transporters, leaving cells vulnerable to excitotoxicity.	Glutamic Acid	24-33	huntingtin	Homo sapiens	7-10
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
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
22123826-12	2012	Our data suggest that Htt is an Hsp90 client protein and that Hsp90 inhibition may provide a means to reduce mHtt in HD.	mhtt	109-113	huntingtin	Homo sapiens	22-25
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
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
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
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
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
23293686-0	2012	Poly-glutamine expanded huntingtin dramatically alters the genome wide binding of HSF1.	polyglutamine	0-14	huntingtin	Homo sapiens	24-34
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
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
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
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
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
22970194-1	2012	The CAG trinucleotide repeat mutation in the Huntington"s disease gene (HTT) exhibits age-dependent tissue-specific expansion that correlates with disease onset in patients, implicating somatic expansion as a disease modifier and potential therapeutic target.	trinucleotide	8-21	huntingtin	Homo sapiens	72-75
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
22359536-3	2012	We collected demographic and clinical data, conducted the Unified Huntington"s Disease Rating Scale and Mini-Mental State Examination, and determined Huntingtin trinucleotide CAG repeat length.	trinucleotide	161-174	huntingtin	Homo sapiens	150-160
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
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
22276192-9	2012	Expression of mutant huntingtin in primary neurons induced superoxide/ROS, an effect that was significantly reduced by constitutively active PPARgamma.	Superoxides	59-69	huntingtin	Homo sapiens	21-31
22276192-9	2012	Expression of mutant huntingtin in primary neurons induced superoxide/ROS, an effect that was significantly reduced by constitutively active PPARgamma.	ros	70-73	huntingtin	Homo sapiens	21-31
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
23440000-1	2012	BACKGROUND: There is emerging evidence that clinical and neuro-pathological manifestations of Huntington"s disease (HD) may occur in individuals with intermediate length cytosine-adenine-guanine (CAG) repeats (27-35 CAG repeats) in the Huntingtin (HTT) gene.	cytosine-adenine-guanine	170-194	huntingtin	Homo sapiens	236-246
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
23440000-1	2012	BACKGROUND: There is emerging evidence that clinical and neuro-pathological manifestations of Huntington"s disease (HD) may occur in individuals with intermediate length cytosine-adenine-guanine (CAG) repeats (27-35 CAG repeats) in the Huntingtin (HTT) gene.	cytosine-adenine-guanine	170-194	huntingtin	Homo sapiens	248-251
23440000-1	2012	BACKGROUND: There is emerging evidence that clinical and neuro-pathological manifestations of Huntington"s disease (HD) may occur in individuals with intermediate length cytosine-adenine-guanine (CAG) repeats (27-35 CAG repeats) in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	196-199	huntingtin	Homo sapiens	236-246
23440000-1	2012	BACKGROUND: There is emerging evidence that clinical and neuro-pathological manifestations of Huntington"s disease (HD) may occur in individuals with intermediate length cytosine-adenine-guanine (CAG) repeats (27-35 CAG repeats) in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	196-199	huntingtin	Homo sapiens	248-251
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
21984825-0	2011	In vitro and in vivo aggregation of a fragment of huntingtin protein directly causes free radical production.	Free Radicals	85-97	huntingtin	Homo sapiens	50-60
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
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.	Reactive Oxygen Species	110-113	huntingtin	Homo sapiens	47-57
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
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
22056561-7	2011	We tested 2-APB analogs in an attempt to identify less toxic and more IP3R1-specific compounds and found that the effect of these analogs on the reduction of the mutant htt aggregation did weakly correlate with their inhibitory action toward the IP3-induced Ca(2+) release (IICR).	2-aminoethyl diphenylborinate	10-15	huntingtin	Homo sapiens	169-172
22056561-7	2011	We tested 2-APB analogs in an attempt to identify less toxic and more IP3R1-specific compounds and found that the effect of these analogs on the reduction of the mutant htt aggregation did weakly correlate with their inhibitory action toward the IP3-induced Ca(2+) release (IICR).	Inositol 1,4,5-Trisphosphate	70-73	huntingtin	Homo sapiens	169-172
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
22071633-2	2011	HD is caused by a highly polymorphic CAG trinucleotide repeat expansion in the exon-1 of the gene encoding for huntingtin protein.	trinucleotide	41-54	huntingtin	Homo sapiens	111-121
21968397-0	2011	A disulfide-free single-domain V(L) intrabody with blocking activity towards huntingtin reveals a novel mode of epitope recognition.	Disulfides	2-11	huntingtin	Homo sapiens	77-87
21968397-1	2011	We present the crystal structure and biophysical characterization of a human V(L) [variable domain immunoglobulin (Ig) light chain] single-domain intrabody that binds to the huntingtin (Htt) protein and has been engineered for antigen recognition in the absence of its intradomain disulfide bond, otherwise conserved in the Ig fold.	Disulfides	281-290	huntingtin	Homo sapiens	174-184
21968397-1	2011	We present the crystal structure and biophysical characterization of a human V(L) [variable domain immunoglobulin (Ig) light chain] single-domain intrabody that binds to the huntingtin (Htt) protein and has been engineered for antigen recognition in the absence of its intradomain disulfide bond, otherwise conserved in the Ig fold.	Disulfides	281-290	huntingtin	Homo sapiens	186-189
21968397-3	2011	Using peptide SPOT arrays, we identified the minimal binding epitope to be EKLMKAFESLKSFQ, comprising the N-terminal residues 5-18 of Htt and including the first residue of the poly-Gln stretch.	poly-gln	177-185	huntingtin	Homo sapiens	134-137
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.	trinucleotide	18-31	huntingtin	Homo sapiens	56-59
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
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
21971427-0	2011	Potent and selective antisense oligonucleotides targeting single-nucleotide polymorphisms in the Huntington disease gene / allele-specific silencing of mutant huntingtin.	Oligonucleotides	31-47	huntingtin	Homo sapiens	159-169
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
21360185-2	2011	Expansion of polyglutamine tracts in htt results in neurodegenerative Huntington disease.	polyglutamine	13-26	huntingtin	Homo sapiens	37-40
22170268-2	2011	An age of onset in the late sixties and a negative family history suggest a relatively small expanded trinucleotide repeat in the HTT gene in the patient and reduced penetrance of an even shorter repeat allele in one of his parents.	trinucleotide	102-115	huntingtin	Homo sapiens	130-133
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
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
21519949-1	2011	Huntington"s Disease (HD) is caused by trinucleotide CAG repeat expansion >36 in huntingtin (htt), a protein with several documented functions.	trinucleotide	39-52	huntingtin	Homo sapiens	81-91
21519949-1	2011	Huntington"s Disease (HD) is caused by trinucleotide CAG repeat expansion >36 in huntingtin (htt), a protein with several documented functions.	trinucleotide	39-52	huntingtin	Homo sapiens	93-96
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
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
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
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
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
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
21896647-2	2011	Mutant Htt (mHtt) in the cytoplasm has been linked to induction of the luminal endoplasmic reticulum (ER) stress pathway, the unfolded protein response (UPR).	Phenobarbital	71-78	huntingtin	Homo sapiens	7-10
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).	trinucleotide	61-74	huntingtin	Homo sapiens	193-203
21854390-1	2011	Huntington"s disease is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin gene.	trinucleotide	81-94	huntingtin	Homo sapiens	119-129
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).	trinucleotide	61-74	huntingtin	Homo sapiens	205-208
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
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
21983719-6	2011	CONCLUSION: This family showed reduced CAG trinucleotide repeats of IT15 gene during maternal transmission.	trinucleotide	43-56	huntingtin	Homo sapiens	68-72
21659333-0	2011	Minocycline inhibits cell death and decreases mutant Huntingtin aggregation by targeting Apaf-1.	Minocycline	0-11	huntingtin	Homo sapiens	53-63
21659333-5	2011	As a consequence, minocycline-treated cells as well as Apaf-1 knock-out cells are resistant to the development of mutant huntingtin-dependent protein aggregation.	Minocycline	18-29	huntingtin	Homo sapiens	121-131
21685499-0	2011	Mass spectrometric identification of novel lysine acetylation sites in huntingtin.	Lysine	43-49	huntingtin	Homo sapiens	71-81
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
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
21685499-4	2011	Lysine acetylation of Htt is of particular importance in HD as this modification regulates disease progression and toxicity.	Lysine	0-6	huntingtin	Homo sapiens	22-25
21685499-11	2011	This report represents the first comprehensive mapping of lysine acetylation sites in N-terminal region of Htt.	Lysine	58-64	huntingtin	Homo sapiens	107-110
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.	cystosine adenine guanine	38-63	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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	65-68	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.	tri-nucleotide	70-84	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	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
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.	Cholesterol	212-223	huntingtin	Homo sapiens	153-163
21894212-4	2011	Emerging evidence from human and animal studies indicates that attenuated brain sterol synthesis and accumulation of cholesterol in neuronal membranes represent two distinct mechanisms occurring in the presence of mutant huntingtin that influence neuronal survival.	Sterols	80-86	huntingtin	Homo sapiens	221-231
21894212-4	2011	Emerging evidence from human and animal studies indicates that attenuated brain sterol synthesis and accumulation of cholesterol in neuronal membranes represent two distinct mechanisms occurring in the presence of mutant huntingtin that influence neuronal survival.	Cholesterol	117-128	huntingtin	Homo sapiens	221-231
21757738-8	2011	Thus we investigated its role in a Huntington disease cellular model and found that FAT10 molecules were covalently attached to huntingtin through their C terminus glycine.	Glycine	164-171	huntingtin	Homo sapiens	128-138
21774998-4	2011	In this review, we provide an overview of current studies that have begun to address these issues and discuss recent findings suggesting that normal huntingtin protein might participate in regulating cholesterol biosynthesis.	Cholesterol	200-211	huntingtin	Homo sapiens	149-159
21897361-5	2011	We recently developed a novel application of TC tags as sensors of oligomerization in cells expressing mutant huntingtin, which when mutated aggregates in neurons in Huntington disease.	Technetium	45-47	huntingtin	Homo sapiens	110-120
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	4-14
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
22832526-5	2011	Among the three genes we obtained as candidate regions showing distinct difference of DNA methylation between one of the two pairs, hypermethylation of SLC6A4, encoding HTT, in the bipolar twin was only confirmed by bisulfite sequencing.	hydrogen sulfite	216-225	huntingtin	Homo sapiens	169-172
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
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
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
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
21454471-5	2011	Transient overexpression of TRAF6 promotes WT and mutant N-HTT atypical ubiquitination with Lys(6), Lys(27), and Lys(29) linkage formation.	Lysine	92-95	huntingtin	Homo sapiens	59-62
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
21454471-5	2011	Transient overexpression of TRAF6 promotes WT and mutant N-HTT atypical ubiquitination with Lys(6), Lys(27), and Lys(29) linkage formation.	Lysine	100-103	huntingtin	Homo sapiens	59-62
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
21566141-3	2011	Besides the pathogenic polyQ expansion, Htt also contains a proline-rich region (PRR) located exactly in the C terminus to the polyQ tract.	Proline	60-67	huntingtin	Homo sapiens	40-43
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
21454471-5	2011	Transient overexpression of TRAF6 promotes WT and mutant N-HTT atypical ubiquitination with Lys(6), Lys(27), and Lys(29) linkage formation.	Lysine	100-103	huntingtin	Homo sapiens	59-62
21454471-8	2011	Mutant N-HTT inclusions are enriched for ubiquitin staining only when TRAF6 and Lys(6), Lys(27), and Lys(29) ubiquitin mutants are expressed.	Lysine	80-83	huntingtin	Homo sapiens	9-12
21454471-8	2011	Mutant N-HTT inclusions are enriched for ubiquitin staining only when TRAF6 and Lys(6), Lys(27), and Lys(29) ubiquitin mutants are expressed.	Lysine	88-91	huntingtin	Homo sapiens	9-12
21454471-8	2011	Mutant N-HTT inclusions are enriched for ubiquitin staining only when TRAF6 and Lys(6), Lys(27), and Lys(29) ubiquitin mutants are expressed.	Lysine	88-91	huntingtin	Homo sapiens	9-12
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
21562226-4	2011	Cells lacking Htt showed slower migration toward the chemoattractant cAMP and contained lower levels of cortical myosin II, which is likely due to defects in dephosphorylation of myosin II mediated by protein phosphatase 2A (PP2A).	Cyclic AMP	69-73	huntingtin	Homo sapiens	14-17
21432905-1	2011	Huntington"s disease (HD) is a neurodegenerative disease caused by a cytosine adenosine guanine (CAG) expansion in the huntingtin gene.	Adenosine	78-87	huntingtin	Homo sapiens	119-129
21432905-1	2011	Huntington"s disease (HD) is a neurodegenerative disease caused by a cytosine adenosine guanine (CAG) expansion in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	97-100	huntingtin	Homo sapiens	119-129
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
21416120-5	2011	Concerning protein aggregation, inclusions of mutant huntingtin were reduced in the presence of diglycerol phosphate and di-myo-inositol phosphate, increased with mannosylglycerate, while mannosyl-lactate and mannosylglyceramide had no significant effect.	diglycerol phosphate	96-116	huntingtin	Homo sapiens	53-63
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
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
21220021-8	2011	Moreover, astrocytes and SH-SY5Y cells expressing mutant huntingtin (mHttQ74) accumulated less aggregates when treated with clioquinol, and this effect was reversed by TPEN.	mhttq74	69-76	huntingtin	Homo sapiens	57-67
21220021-8	2011	Moreover, astrocytes and SH-SY5Y cells expressing mutant huntingtin (mHttQ74) accumulated less aggregates when treated with clioquinol, and this effect was reversed by TPEN.	Clioquinol	124-134	huntingtin	Homo sapiens	57-67
21220021-8	2011	Moreover, astrocytes and SH-SY5Y cells expressing mutant huntingtin (mHttQ74) accumulated less aggregates when treated with clioquinol, and this effect was reversed by TPEN.	N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine	168-172	huntingtin	Homo sapiens	57-67
21447599-1	2011	The expanded CAG repeat that causes striatal cell vulnerability in Huntington"s disease (HD) encodes a polyglutamine tract in full-length huntingtin that is correlated with cellular [ATP] and [ATP/ADP].	Adenosine Triphosphate	183-186	huntingtin	Homo sapiens	138-148
21447599-1	2011	The expanded CAG repeat that causes striatal cell vulnerability in Huntington"s disease (HD) encodes a polyglutamine tract in full-length huntingtin that is correlated with cellular [ATP] and [ATP/ADP].	Adenosine Triphosphate	193-196	huntingtin	Homo sapiens	138-148
21447599-1	2011	The expanded CAG repeat that causes striatal cell vulnerability in Huntington"s disease (HD) encodes a polyglutamine tract in full-length huntingtin that is correlated with cellular [ATP] and [ATP/ADP].	Adenosine Diphosphate	197-200	huntingtin	Homo sapiens	138-148
21755114-1	2011	Huntington"s disease (HD) is a neurodegenerative disorder characterized by chorea, behavioral disturbances and dementia, caused by a pathological expansion of the CAG trinucleotide in the HTT gene.	cag trinucleotide	163-180	huntingtin	Homo sapiens	188-191
21416120-5	2011	Concerning protein aggregation, inclusions of mutant huntingtin were reduced in the presence of diglycerol phosphate and di-myo-inositol phosphate, increased with mannosylglycerate, while mannosyl-lactate and mannosylglyceramide had no significant effect.	di-myo-inositol phosphate	121-146	huntingtin	Homo sapiens	53-63
21416120-5	2011	Concerning protein aggregation, inclusions of mutant huntingtin were reduced in the presence of diglycerol phosphate and di-myo-inositol phosphate, increased with mannosylglycerate, while mannosyl-lactate and mannosylglyceramide had no significant effect.	mannosylglycerate	163-180	huntingtin	Homo sapiens	53-63
21416120-5	2011	Concerning protein aggregation, inclusions of mutant huntingtin were reduced in the presence of diglycerol phosphate and di-myo-inositol phosphate, increased with mannosylglycerate, while mannosyl-lactate and mannosylglyceramide had no significant effect.	mannosyl-lactate	188-204	huntingtin	Homo sapiens	53-63
21416120-5	2011	Concerning protein aggregation, inclusions of mutant huntingtin were reduced in the presence of diglycerol phosphate and di-myo-inositol phosphate, increased with mannosylglycerate, while mannosyl-lactate and mannosylglyceramide had no significant effect.	mannosylglyceramide	209-228	huntingtin	Homo sapiens	53-63
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
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.	trinucleotide	33-46	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.	trinucleotide	33-46	huntingtin	Homo sapiens	147-150
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
20649476-1	2011	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the Huntingtin gene Htt.	cytosine-adenine-guanine	103-127	huntingtin	Homo sapiens	149-159
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
21247881-2	2011	Huntington"s disease and spinobulbar muscular atrophy (SBMA) are examples of these diseases in which underlying mutations are localized near other trinucleotide repeats in the huntingtin (HTT) and androgen receptor (AR) genes, respectively.	trinucleotide	147-160	huntingtin	Homo sapiens	176-186
21247881-2	2011	Huntington"s disease and spinobulbar muscular atrophy (SBMA) are examples of these diseases in which underlying mutations are localized near other trinucleotide repeats in the huntingtin (HTT) and androgen receptor (AR) genes, respectively.	trinucleotide	147-160	huntingtin	Homo sapiens	188-191
21503105-2	2011	METHODS: The clinical data of HD cases from 2 Chinese families were analyzed and trinucleotide repeat in the IT15 gene were investigated in 9 of the two families by polymerase chain reaction and GeneScan.	trinucleotide	81-94	huntingtin	Homo sapiens	109-113
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
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
21332223-4	2011	Trimethylamine N-oxide (TMAO) and proline redirect amyloid fibrillogenesis of the pathological huntingtin exon 1 to nonamyloidogenic amorphous assemblies via two dissimilar molecular mechanisms.	trimethyloxamine	0-22	huntingtin	Homo sapiens	95-105
21332223-4	2011	Trimethylamine N-oxide (TMAO) and proline redirect amyloid fibrillogenesis of the pathological huntingtin exon 1 to nonamyloidogenic amorphous assemblies via two dissimilar molecular mechanisms.	trimethyloxamine	24-28	huntingtin	Homo sapiens	95-105
21332223-4	2011	Trimethylamine N-oxide (TMAO) and proline redirect amyloid fibrillogenesis of the pathological huntingtin exon 1 to nonamyloidogenic amorphous assemblies via two dissimilar molecular mechanisms.	Proline	34-41	huntingtin	Homo sapiens	95-105
21735602-0	2010	Identification of compounds which inhibit cytotoxicity associated with mutant Huntingtin protein expression In this report, we present data on a compound, ML168 (CID 2432214), which is able to protect cells from cytotoxicity induced by the expression of a large mutant poly-Q expansion Huntingtin (HTT) protein by inhibiting the activation of the intrinsic apoptotic pathway.	ML168	155-160	huntingtin	Homo sapiens	78-88
21735602-0	2010	Identification of compounds which inhibit cytotoxicity associated with mutant Huntingtin protein expression In this report, we present data on a compound, ML168 (CID 2432214), which is able to protect cells from cytotoxicity induced by the expression of a large mutant poly-Q expansion Huntingtin (HTT) protein by inhibiting the activation of the intrinsic apoptotic pathway.	ML168	155-160	huntingtin	Homo sapiens	286-296
21735602-0	2010	Identification of compounds which inhibit cytotoxicity associated with mutant Huntingtin protein expression In this report, we present data on a compound, ML168 (CID 2432214), which is able to protect cells from cytotoxicity induced by the expression of a large mutant poly-Q expansion Huntingtin (HTT) protein by inhibiting the activation of the intrinsic apoptotic pathway.	ML168	155-160	huntingtin	Homo sapiens	298-301
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.	trinucleotide	55-68	huntingtin	Homo sapiens	141-151
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	70-73	huntingtin	Homo sapiens	141-151
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
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
20649476-1	2011	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the Huntingtin gene Htt.	cytosine-adenine-guanine	103-127	huntingtin	Homo sapiens	165-168
20649476-1	2011	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the Huntingtin gene Htt.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	129-132	huntingtin	Homo sapiens	149-159
20649476-1	2011	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the Huntingtin gene Htt.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	129-132	huntingtin	Homo sapiens	165-168
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
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
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
21189122-4	2011	Although it is not clear how cytoplasmic/nuclear located mutant Huntingtin alters the function of the ER, several reports indicate that mutant Huntingtin affects many essential processes related to the secretory pathway, including inhibition of ER-associated degradation, altered ER/Golgi vesicular trafficking and axonal transport, disrupted autophagy and abnormal ER calcium homeostasis.	Calcium	369-376	huntingtin	Homo sapiens	143-153
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	74-77
21153060-4	2011	This review will overview recent findings concerning htt-promoted alterations in cell signaling that involve different neurotransmitters and trophic factor systems, especially involving mGluR1/5, as glutamate plays a crucial role in neuronal cell death.	Glutamic Acid	199-208	huntingtin	Homo sapiens	53-56
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
19756523-1	2011	BACKGROUND: The serotonin transporter (5-HTT) plays a critical role in the regulation of serotonin neurotransmission and has been implicated in the pathophysiology of major depression.	Serotonin	16-25	huntingtin	Homo sapiens	41-44
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
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
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].	trinucleotide	78-91	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	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
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
20929960-6	2011	Moreover, pharmacological administration of the cannabinoid Delta(9)-tetrahydrocannabinol to mice expressing human mutant huntingtin exon 1 exerted a therapeutic effect and ameliorated those parameters.	Dronabinol	60-89	huntingtin	Homo sapiens	122-132
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
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
21909428-3	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
21909428-5	2011	Here, we make use of modified 2"-O-methyl phosphorothioate (CUG)n triplet-repeat antisense oligonucleotides to effectively reduce mutant huntingtin transcript and protein levels in patient-derived Huntington"s disease fibroblasts and lymphoblasts.	2"-o-methyl phosphorothioate	30-58	huntingtin	Homo sapiens	137-147
21909428-5	2011	Here, we make use of modified 2"-O-methyl phosphorothioate (CUG)n triplet-repeat antisense oligonucleotides to effectively reduce mutant huntingtin transcript and protein levels in patient-derived Huntington"s disease fibroblasts and lymphoblasts.	3-Carboxyumbelliferyl beta-D-galactopyranoside	60-63	huntingtin	Homo sapiens	137-147
21909428-5	2011	Here, we make use of modified 2"-O-methyl phosphorothioate (CUG)n triplet-repeat antisense oligonucleotides to effectively reduce mutant huntingtin transcript and protein levels in patient-derived Huntington"s disease fibroblasts and lymphoblasts.	Oligonucleotides	91-107	huntingtin	Homo sapiens	137-147
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.	Oligonucleotides	15-30	huntingtin	Homo sapiens	89-99
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
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
21278900-1	2010	A means for measuring levels of soluble huntingtin proteins in clinical samples is essential for assessing the biological effects of potential mutant huntingtin (mtHtt) modifying treatments being developed for Huntington"s disease (HD).	mthtt	162-167	huntingtin	Homo sapiens	40-50
21278900-1	2010	A means for measuring levels of soluble huntingtin proteins in clinical samples is essential for assessing the biological effects of potential mutant huntingtin (mtHtt) modifying treatments being developed for Huntington"s disease (HD).	mthtt	162-167	huntingtin	Homo sapiens	150-160
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
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
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
21028906-1	2010	Huntington"s disease (HD) is a currently incurable neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat within the huntingtin (HTT) gene.	trinucleotide	110-123	huntingtin	Homo sapiens	142-152
21028906-1	2010	Huntington"s disease (HD) is a currently incurable neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat within the huntingtin (HTT) gene.	trinucleotide	110-123	huntingtin	Homo sapiens	154-157
21028906-3	2010	We have evaluated a series of antisense oligonucleotides (ASOs) targeted to the expanded CAG repeat within HTT mRNA for their ability to selectively inhibit expression of mutant HTT protein.	Oligonucleotides	40-56	huntingtin	Homo sapiens	107-110
21028906-3	2010	We have evaluated a series of antisense oligonucleotides (ASOs) targeted to the expanded CAG repeat within HTT mRNA for their ability to selectively inhibit expression of mutant HTT protein.	Oligonucleotides	40-56	huntingtin	Homo sapiens	178-181
21028906-3	2010	We have evaluated a series of antisense oligonucleotides (ASOs) targeted to the expanded CAG repeat within HTT mRNA for their ability to selectively inhibit expression of mutant HTT protein.	Oligonucleotides, Antisense	58-62	huntingtin	Homo sapiens	107-110
21028906-3	2010	We have evaluated a series of antisense oligonucleotides (ASOs) targeted to the expanded CAG repeat within HTT mRNA for their ability to selectively inhibit expression of mutant HTT protein.	Oligonucleotides, Antisense	58-62	huntingtin	Homo sapiens	178-181
21028906-7	2010	We observed cooperative binding of multiple ASO molecules to CAG repeat-containing HTT mRNA transcripts in vitro.	Oligonucleotides, Antisense	44-47	huntingtin	Homo sapiens	83-86
21028906-9	2010	ASOs targeted to the CAG repeat of HTT provide a starting point for the development of oligonucleotide-based therapeutics that can inhibit gene expression with allelic discrimination in patients with HD.	Oligonucleotides	87-102	huntingtin	Homo sapiens	35-38
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
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).	Glutamic Acid	0-9	huntingtin	Homo sapiens	155-165
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
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).	Glutamic Acid	0-9	huntingtin	Homo sapiens	167-170
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
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
20644995-2	2010	Overactivation of group I metabotropic glutamate receptors (mGluRs), which include mGluR1 as well as mGluR5 and are coupled via phospholipase C to the inositol phosphate pathway, is found to be involved in mutant htt-mediated neurotoxicity.	Inositol Phosphates	151-169	huntingtin	Homo sapiens	213-216
20663016-6	2010	In addition, cells expressing mutant huntingtin showed increased localization of NMDA receptors with cholesterol-enriched domains, contributing to increased NMDA receptor susceptibility to excitotoxic insults.	Cholesterol	101-112	huntingtin	Homo sapiens	37-47
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
20663016-8	2010	Taken together, our results indicate that mutant huntingtin produces accumulation of cholesterol and alters its cellular distribution that contributes to NMDA-mediated excitotoxicity.	Cholesterol	85-96	huntingtin	Homo sapiens	49-59
20663016-8	2010	Taken together, our results indicate that mutant huntingtin produces accumulation of cholesterol and alters its cellular distribution that contributes to NMDA-mediated excitotoxicity.	N-Methylaspartate	154-158	huntingtin	Homo sapiens	49-59
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
24868381-2	2010	It is caused by an unstable cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the gene IT15 in locus 4p16.3.	cytosine-adenine-guanine (cag) trinucleotide	28-72	huntingtin	Homo sapiens	102-106
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
20547568-2	2010	Furthermore, the HTT gene has been functionally linked to iron (Fe) metabolism, and HD patients show alterations in brain and peripheral Fe homeostasis.	Iron	58-62	huntingtin	Homo sapiens	17-20
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
20529957-8	2010	Finally, we demonstrate that ubiquilin protects cells against starvation-induced cell death propagated by overexpression of mutant Alzheimer"s disease PS2N141I protein and green fluorescent protein (GFP)-huntingtin exon-1 fusion protein containing 74 polyglutamines.	ubiquilin	29-38	huntingtin	Homo sapiens	204-214
20656845-4	2010	HTT, the time between the appearance of the microbubble contrast agent in the hepatic artery and its appearance in the hepatic vein, was measured in the contrast pulse sequencing mode after injection of a sulphur hexafluoride microbubble US contrast agent.	Sulfur Hexafluoride	205-225	huntingtin	Homo sapiens	0-3
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
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
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
19530012-3	2010	Genetic testing confirmed the presence of expanded trinucleotide repeats in huntingtin, consistent with a diagnosis of Huntington"s disease.	trinucleotide	51-64	huntingtin	Homo sapiens	76-86
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.	n-terminal	118-128	huntingtin	Homo sapiens	154-157
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
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
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
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
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
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
20552561-6	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.	polyglutamine	97-103	huntingtin	Homo sapiens	54-64
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
20454921-2	2010	Evidence from genetic HD models suggest that mutant huntingtin (mHtt) compromises mitochondrial bioenergetics and dynamics, preventing efficient calcium handling and ATP generation in neuronal networks.	Calcium	145-152	huntingtin	Homo sapiens	52-62
20454921-2	2010	Evidence from genetic HD models suggest that mutant huntingtin (mHtt) compromises mitochondrial bioenergetics and dynamics, preventing efficient calcium handling and ATP generation in neuronal networks.	Adenosine Triphosphate	166-169	huntingtin	Homo sapiens	52-62
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
19779024-0	2010	Interaction of child maltreatment and 5-HTT polymorphisms: suicidal ideation among children from low-SES backgrounds.	Selenium	101-104	huntingtin	Homo sapiens	40-43
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
20357106-6	2010	Here, we report that decreased levels of a major intracellular antioxidant glutathione coincide with accumulation of ROS in primary HD neurons prepared from embryos of HD knock-in mice (HD(140Q/140Q)), which have human huntingtin exon 1 with 140 CAG repeats inserted into the endogenous mouse huntingtin gene.	Glutathione	75-86	huntingtin	Homo sapiens	219-229
20127207-6	2010	The most impressive consequence of this deregulation is represented by anomalous sphingolipid-protein interactions that are at least, in part, responsible for the misfolding events that cause the fibrillogenic and amyloidogenic processing of disease-specific protein isoforms, such as amyloid beta peptide in Alzheimer"s disease, huntingtin in Huntington"s disease, alpha-synuclein in Parkinson"s disease, and prions in transmissible encephalopathies.	Sphingolipids	81-93	huntingtin	Homo sapiens	330-340
20154343-1	2010	Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by an expansion of a CAG trinucleotide repeat in the huntingtin (HTT) gene [Huntington"s Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington"s disease chromosomes.	trinucleotide	120-133	huntingtin	Homo sapiens	148-158
20154343-1	2010	Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by an expansion of a CAG trinucleotide repeat in the huntingtin (HTT) gene [Huntington"s Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington"s disease chromosomes.	trinucleotide	120-133	huntingtin	Homo sapiens	160-163
20154343-1	2010	Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by an expansion of a CAG trinucleotide repeat in the huntingtin (HTT) gene [Huntington"s Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington"s disease chromosomes.	trinucleotide	254-267	huntingtin	Homo sapiens	148-158
20154343-1	2010	Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disorder caused by an expansion of a CAG trinucleotide repeat in the huntingtin (HTT) gene [Huntington"s Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington"s disease chromosomes.	trinucleotide	254-267	huntingtin	Homo sapiens	160-163
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
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
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
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
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
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
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
20378838-4	2010	Whereas mutant huntingtin fragments increased sterols in neuronal cells, SIRT2 inhibition reduced sterol levels via decreased nuclear trafficking of SREBP-2.	Sterols	46-53	huntingtin	Homo sapiens	15-25
20378838-4	2010	Whereas mutant huntingtin fragments increased sterols in neuronal cells, SIRT2 inhibition reduced sterol levels via decreased nuclear trafficking of SREBP-2.	Sterols	46-52	huntingtin	Homo sapiens	15-25
20378838-5	2010	Importantly, manipulation of sterol biosynthesis at the transcriptional level mimicked SIRT2 inhibition, demonstrating that the metabolic effects of SIRT2 inhibition are sufficient to diminish mutant huntingtin toxicity.	Sterols	29-35	huntingtin	Homo sapiens	200-210
20416508-4	2010	Sensors for mutant huntingtin, which forms aggregates in Huntington"s disease, were made by introducing a tetracysteine motif into huntingtin that becomes occluded from binding biarsenical fluorophores in oligomers, but not monomers.	tetracysteine	106-119	huntingtin	Homo sapiens	19-29
20416508-4	2010	Sensors for mutant huntingtin, which forms aggregates in Huntington"s disease, were made by introducing a tetracysteine motif into huntingtin that becomes occluded from binding biarsenical fluorophores in oligomers, but not monomers.	tetracysteine	106-119	huntingtin	Homo sapiens	131-141
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
20298220-3	2010	Recent findings show that copper-regulatory genes are induced during HD and copper binds to an N-terminal fragment of huntingtin, supporting the involvement of abnormal copper metabolism in HD.	Copper	26-32	huntingtin	Homo sapiens	118-128
20298220-3	2010	Recent findings show that copper-regulatory genes are induced during HD and copper binds to an N-terminal fragment of huntingtin, supporting the involvement of abnormal copper metabolism in HD.	Copper	76-82	huntingtin	Homo sapiens	118-128
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).	Copper	35-41	huntingtin	Homo sapiens	102-112
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
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
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
20237277-5	2010	Administration of GM1 restores ganglioside levels in HD cells and promotes activation of AKT and phosphorylation of mutant Htt, leading to decreased mutant Htt toxicity and increased survival of HD cells.	G(M1) Ganglioside	18-21	huntingtin	Homo sapiens	123-126
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
19394403-3	2010	Set against a historical background, we review data supporting the idea that metabolites of the kynurenine pathway (KP) of tryptophan degradation provide a critical link between mutant htt and the pathophysiology of HD.	Kynurenine	96-106	huntingtin	Homo sapiens	185-188
19394403-3	2010	Set against a historical background, we review data supporting the idea that metabolites of the kynurenine pathway (KP) of tryptophan degradation provide a critical link between mutant htt and the pathophysiology of HD.	Tryptophan	123-133	huntingtin	Homo sapiens	185-188
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
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
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.	Sodium Dodecyl Sulfate	148-151	huntingtin	Homo sapiens	95-98
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
20145031-1	2010	Huntington disease (HD) is a neurodegenerative disorder associated with an expanded CAG trinucleotide repeat length in the huntingtin gene.	trinucleotide	88-101	huntingtin	Homo sapiens	123-133
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).	guanosine-rich oligonucleotides	33-64	huntingtin	Homo sapiens	164-174
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
20152113-1	2010	The density of GABA(A) receptors (GABA(A)Rs) at synapses regulates brain excitability, and altered inhibition may contribute to Huntington"s disease, which is caused by a polyglutamine repeat in the protein huntingtin.	gamma-Aminobutyric Acid	15-19	huntingtin	Homo sapiens	207-217
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
20126661-4	2010	Mapping studies showed that the HEAT repeats 2&3 of htt interact with the cue domain of gp78.	Adenosine Monophosphate	47-50	huntingtin	Homo sapiens	56-59
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
20152113-6	2010	When huntingtin is mutated, as in Huntington"s disease, GABA(A)R transport and inhibitory synaptic currents are reduced.	gamma-Aminobutyric Acid	56-60	huntingtin	Homo sapiens	5-15
20802793-2	2010	The pathophysiology of Huntington disease is linked to an expanded trinucleotide repeat of cytosine-adenine-guanine (CAG) in the IT-15 gene on chromosome 4.	trinucleotide	67-80	huntingtin	Homo sapiens	129-134
19682570-10	2010	Also dopamine receptors modulate mutant Htt toxicity, at least in part through regulation of the expression of mitochondrial complex II.	Dopamine	5-13	huntingtin	Homo sapiens	40-43
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
19338577-2	2010	We previously demonstrated in HEK293 cells that a peptide containing amino acids 76-121 of CaM (CaM-peptide) interrupted the interaction between CaM and mutant huntingtin, reduced mutant huntingtin-induced cytotoxicity and reduced transglutaminase (TG)-modified mutant huntingtin.	Peptides	50-57	huntingtin	Homo sapiens	160-170
19338577-2	2010	We previously demonstrated in HEK293 cells that a peptide containing amino acids 76-121 of CaM (CaM-peptide) interrupted the interaction between CaM and mutant huntingtin, reduced mutant huntingtin-induced cytotoxicity and reduced transglutaminase (TG)-modified mutant huntingtin.	Peptides	50-57	huntingtin	Homo sapiens	187-197
19338577-2	2010	We previously demonstrated in HEK293 cells that a peptide containing amino acids 76-121 of CaM (CaM-peptide) interrupted the interaction between CaM and mutant huntingtin, reduced mutant huntingtin-induced cytotoxicity and reduced transglutaminase (TG)-modified mutant huntingtin.	Peptides	50-57	huntingtin	Homo sapiens	187-197
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
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.	Sepharose	91-98	huntingtin	Homo sapiens	32-42
20491647-2	2010	Mutated Htt (mHtt) causes the appearance of intracellular aggregates inducing alterations in mitochondrial metabolism in the form of reactive oxygen species (ROS) and ATP depletion.	Reactive Oxygen Species	133-156	huntingtin	Homo sapiens	8-11
20491647-2	2010	Mutated Htt (mHtt) causes the appearance of intracellular aggregates inducing alterations in mitochondrial metabolism in the form of reactive oxygen species (ROS) and ATP depletion.	Reactive Oxygen Species	158-161	huntingtin	Homo sapiens	8-11
20491647-2	2010	Mutated Htt (mHtt) causes the appearance of intracellular aggregates inducing alterations in mitochondrial metabolism in the form of reactive oxygen species (ROS) and ATP depletion.	Adenosine Triphosphate	167-170	huntingtin	Homo sapiens	8-11
20056037-1	2010	Expansion of an unstable trinucleotide (CAG)(n) repeat region within exon 1 of the gene IT15 causes autosomal, dominantly inherited Huntington"s disease (HD).	trinucleotide	25-38	huntingtin	Homo sapiens	88-92
20056037-1	2010	Expansion of an unstable trinucleotide (CAG)(n) repeat region within exon 1 of the gene IT15 causes autosomal, dominantly inherited Huntington"s disease (HD).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	40-43	huntingtin	Homo sapiens	88-92
20802793-2	2010	The pathophysiology of Huntington disease is linked to an expanded trinucleotide repeat of cytosine-adenine-guanine (CAG) in the IT-15 gene on chromosome 4.	cytosine-adenine-guanine	91-115	huntingtin	Homo sapiens	129-134
20802793-2	2010	The pathophysiology of Huntington disease is linked to an expanded trinucleotide repeat of cytosine-adenine-guanine (CAG) in the IT-15 gene on chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	117-120	huntingtin	Homo sapiens	129-134
20802793-5	2010	This lipid dysregulation has been linked to specific actions of the mutant huntingtin on sterol regulatory element binding proteins.	Sterols	89-95	huntingtin	Homo sapiens	75-85
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
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
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
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
20082975-5	2009	Therapeutic targets for HD include the huntingtin protein itself, either by reducing its levels with antisense oligonucleotides or siRNA, or potentially by intervening via posttranslational modifications such as phosphorylation, acetylation, SUMOylation, or proteolytic cleavage.	Oligonucleotides	111-127	huntingtin	Homo sapiens	39-49
20064390-0	2009	Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice.	Serine	0-7	huntingtin	Homo sapiens	72-82
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
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
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
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
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
19783436-0	2009	Cellular localization and allele-selective inhibition of mutant huntingtin protein by peptide nucleic acid oligomers containing the fluorescent nucleobase [bis-o-(aminoethoxy)phenyl]pyrrolocytosine.	nucleobase [bis-o-(aminoethoxy)phenyl]pyrrolocytosine	144-197	huntingtin	Homo sapiens	64-74
19860865-6	2009	RESULTS: The phosphorylation of huntingtin at serine 421 (S421) restores its function in axonal transport.	Serine	46-52	huntingtin	Homo sapiens	32-42
19860865-8	2009	We found that pharmacological inhibition of calcineurin by FK506 led to sustained phosphorylation of mutant huntingtin at S421.	Tacrolimus	59-64	huntingtin	Homo sapiens	108-118
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
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
19710014-3	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
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.	Proline	116-123	huntingtin	Homo sapiens	18-21
19710014-0	2009	Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity.	Threonine	19-28	huntingtin	Homo sapiens	49-59
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
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
19616561-1	2009	The polyphenol (-)-epigallocatechin-3-gallate (EGCG) has recently attracted much research interest in the field of protein-misfolding diseases because of its potent anti-amyloid activity against amyloid-beta, alpha-synuclein and huntingtin, the amyloid-fibril-forming proteins involved in Alzheimer"s, Parkinson"s and Huntington"s diseases, respectively.	Polyphenols	4-14	huntingtin	Homo sapiens	229-239
19816846-5	2009	DEVELOPMENT: The main characteristics of Huntington"s disease are: neuronal loss, glyosis, and accumulations of mutated Htt, all associated with different underlying channels in the pathogenesis of the disease, such as: excitotoxicity, energy deficit (ATP depletion), reduction in the synthesis and release of neurotrophic factors (BDNF and GDNF), and oxidative stress.	Adenosine Triphosphate	252-255	huntingtin	Homo sapiens	120-123
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
19628478-4	2009	We demonstrate that mutant huntingtin impairs glucose-stimulated insulin secretion in insulin-producing beta-cells, without altering stored levels of insulin.	Glucose	46-53	huntingtin	Homo sapiens	27-37
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
19607813-3	2009	Here we used differential scanning calorimetry to examine the effects of polyQ expansion in htt on its insertion into lipid bilayers.	Lipid Bilayers	118-132	huntingtin	Homo sapiens	92-95
19616561-1	2009	The polyphenol (-)-epigallocatechin-3-gallate (EGCG) has recently attracted much research interest in the field of protein-misfolding diseases because of its potent anti-amyloid activity against amyloid-beta, alpha-synuclein and huntingtin, the amyloid-fibril-forming proteins involved in Alzheimer"s, Parkinson"s and Huntington"s diseases, respectively.	epigallocatechin gallate	15-45	huntingtin	Homo sapiens	229-239
19616561-1	2009	The polyphenol (-)-epigallocatechin-3-gallate (EGCG) has recently attracted much research interest in the field of protein-misfolding diseases because of its potent anti-amyloid activity against amyloid-beta, alpha-synuclein and huntingtin, the amyloid-fibril-forming proteins involved in Alzheimer"s, Parkinson"s and Huntington"s diseases, respectively.	epigallocatechin gallate	47-51	huntingtin	Homo sapiens	229-239
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
19602103-5	2009	Furthermore, we expressed N-terminal huntingtin fragments with different polyglutamine lengths in an insulinoma-cell line (INS-1E) to investigate how mutant huntingtin influences glucose-stimulated insulin release in vitro.	Glucose	179-186	huntingtin	Homo sapiens	157-167
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
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
19566678-3	2009	Previously we reported that exogenously expressed huntingtin bound pure phospholipids using protein-lipid overlays.	Phospholipids	72-85	huntingtin	Homo sapiens	50-60
19602103-7	2009	However, the glucose-stimulated induction of insulin release was significantly reduced in the insulinoma-cell line expressing highly expanded huntingtin compared to cells expressing huntingtin with modestly elongated polyglutamine stretches.	Glucose	13-20	huntingtin	Homo sapiens	142-152
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
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
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
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
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
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
19523837-1	2009	Early studies led to the identification of 3beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid methyl ester (5) with high affinity at the DAT (IC(50)=6.5nM) and 5-HTT (K(i)=4.3nM), while having much less affinity at the NET (K(i)=1110nM).	CHEMBL574081	43-108	huntingtin	Homo sapiens	164-167
19523837-4	2009	With exception of the 4"-methylsulfonyl analogue 7h, all the tested compounds possessed high binding affinities at the 5-HTT.	4"-methylsulfonyl	22-39	huntingtin	Homo sapiens	121-124
19523837-6	2009	The 3beta-(4-methylthiophenyl)tropane 7a and its N-(3-fluoropropyl) analogue 9a and N-allyl analogue 10a are the most selective compounds for the 5-HTT over the NET (NET/5-HTT=314-364) in the series.	3beta-(4-methylthiophenyl)tropane 7a	4-40	huntingtin	Homo sapiens	148-151
19523837-6	2009	The 3beta-(4-methylthiophenyl)tropane 7a and its N-(3-fluoropropyl) analogue 9a and N-allyl analogue 10a are the most selective compounds for the 5-HTT over the NET (NET/5-HTT=314-364) in the series.	3beta-(4-methylthiophenyl)tropane 7a	4-40	huntingtin	Homo sapiens	172-175
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.	trinucleotide	36-49	huntingtin	Homo sapiens	97-107
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.	trinucleotide	36-49	huntingtin	Homo sapiens	109-112
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
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	56-70	huntingtin	Homo sapiens	18-28
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
19488402-5	2009	We report that treatment of neurons with the DNA damaging agent etoposide or gamma-irradiation promotes cleavage of wild type (WT) and mutant Htt, generating N-terminal fragments of 80-90 kDa.	Etoposide	64-73	huntingtin	Homo sapiens	142-145
19488402-7	2009	Elevated levels of IKKalpha, or inhibition of IKKbeta expression by a specific small hairpin RNA (shRNA) or its activity by sodium salicylate, prevents Htt proteolysis and increases neuronal resistance to DNA damage.	Sodium Salicylate	124-141	huntingtin	Homo sapiens	152-155
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
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
19278999-4	2009	ROCK inhibitors, including Y-27632 were reported to decrease aggregation of htt and androgen receptor (AR) through ROCK1 and protein kinase C-related protein kinase-2 (PRK-2).	Y 27632	27-34	huntingtin	Homo sapiens	76-79
19278999-8	2009	In this study, we show that Y-27632 not only reduced the mutant htt aggregation by enhancing its degradation, but surprisingly was able to activate the main cellular degradation pathways, proteasome, and macroautophagy.	Y 27632	28-35	huntingtin	Homo sapiens	64-67
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
19270310-2	2009	Huntington disease is caused by expansion of glutamine repeats in the huntingtin protein.	Glutamine	45-54	huntingtin	Homo sapiens	70-80
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
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
19204007-7	2009	Using mass spectrometry, we found that the cp-2 fragment is generated by cleavage of huntingtin at position Arg(167).	Arginine	108-111	huntingtin	Homo sapiens	85-95
19204007-10	2009	These data suggest that cleavage of huntingtin at residue Arg(167) may mediate mutant huntingtin toxicity in Huntington disease.	Arginine	58-61	huntingtin	Homo sapiens	36-46
19204007-10	2009	These data suggest that cleavage of huntingtin at residue Arg(167) may mediate mutant huntingtin toxicity in Huntington disease.	Arginine	58-61	huntingtin	Homo sapiens	86-96
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.	17-amino-acid	22-35	huntingtin	Homo sapiens	101-111
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
19240112-1	2009	Huntington"s disease is caused by a polyglutamine expansion in the huntingtin protein.	polyglutamine	36-49	huntingtin	Homo sapiens	67-77
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
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
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
19039036-1	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.	trinucleotide	61-74	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.	trinucleotide	61-74	huntingtin	Homo sapiens	138-141
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
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.	Adenosine Triphosphate	277-280	huntingtin	Homo sapiens	135-138
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
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
18984744-5	2009	Similarly to Huntington"s disease patients, mice expressing the mutated human huntingtin protein also exhibit neurodegenerative changes, motor dysfunction, perturbed energy metabolism, and elevated blood glucose levels.	Glucose	204-211	huntingtin	Homo sapiens	78-88
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	62-72
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
19199872-5	2009	Neurons made vulnerable to calcium dysregulation by overexpression of mutated presenilin-1 (PS1) or huntingtin (Q-111) proteins showed enhanced apoptosis upon isoflurane exposure.	Calcium	27-34	huntingtin	Homo sapiens	100-110
19199872-5	2009	Neurons made vulnerable to calcium dysregulation by overexpression of mutated presenilin-1 (PS1) or huntingtin (Q-111) proteins showed enhanced apoptosis upon isoflurane exposure.	Isoflurane	159-169	huntingtin	Homo sapiens	100-110
18992820-1	2009	Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinases Akt and SGK.	Serine	32-38	huntingtin	Homo sapiens	0-10
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.	Sirolimus	0-9	huntingtin	Homo sapiens	96-106
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
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
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
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
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
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
18772195-2	2008	Here, we demonstrate that phosphorylation of htt at serine 421 (S421) restores its function in axonal transport.	Serine	52-58	huntingtin	Homo sapiens	45-48
19053748-1	2008	Previous studies showed that the mixed monoamine transporter inhibitor (6, RTI-112) reduced cocaine self-administration at a high level of serotonin transporter (5-HTT) occupancy with no detectable dopamine transporter (DAT) occupancy.	RTI 112	75-82	huntingtin	Homo sapiens	164-167
19053748-4	2008	3Beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid 2-(3-iodo-4-aminophenyl)ethyl ester (8i) with an IC(50) value of 2.5 nM for the DAT and K(i) values of 3.5 and 2040 nM for the 5-HTT and NET, respectively, is the most potent and selective compound for the DAT and 5-HTT relative to the NET in this study.	3beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid	0-52	huntingtin	Homo sapiens	182-185
19053748-4	2008	3Beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid 2-(3-iodo-4-aminophenyl)ethyl ester (8i) with an IC(50) value of 2.5 nM for the DAT and K(i) values of 3.5 and 2040 nM for the 5-HTT and NET, respectively, is the most potent and selective compound for the DAT and 5-HTT relative to the NET in this study.	3beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid	0-52	huntingtin	Homo sapiens	269-272
19053748-4	2008	3Beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid 2-(3-iodo-4-aminophenyl)ethyl ester (8i) with an IC(50) value of 2.5 nM for the DAT and K(i) values of 3.5 and 2040 nM for the 5-HTT and NET, respectively, is the most potent and selective compound for the DAT and 5-HTT relative to the NET in this study.	2-(3-iodo-4-aminophenyl)ethyl ester	53-88	huntingtin	Homo sapiens	182-185
19053748-4	2008	3Beta-(4-methoxyphenyl)tropane-2beta-carboxylic acid 2-(3-iodo-4-aminophenyl)ethyl ester (8i) with an IC(50) value of 2.5 nM for the DAT and K(i) values of 3.5 and 2040 nM for the 5-HTT and NET, respectively, is the most potent and selective compound for the DAT and 5-HTT relative to the NET in this study.	2-(3-iodo-4-aminophenyl)ethyl ester	53-88	huntingtin	Homo sapiens	269-272
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
18951640-4	2008	Here, we highlight how mutant huntingtin (mtHtt) might cause mitochondrial dysfunction by either perturbing transcription of nuclear-encoded mitochondrial proteins or by direct interaction with the organelle and modulation of respiration, mitochondrial membrane potential and Ca(2+) buffering.	mthtt	42-47	huntingtin	Homo sapiens	30-40
19076433-2	2008	It is caused by an expanded trinucleotide CAG repeat in the gene coding for the protein, huntingtin.	trinucleotide	28-41	huntingtin	Homo sapiens	89-99
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
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
18440664-1	2008	The serotonin (5-hydroxytryptamine, or 5-HT) transporters (5-HTT) are target-sites for commonly used antidepressants.	Serotonin	4-13	huntingtin	Homo sapiens	61-64
18440664-1	2008	The serotonin (5-hydroxytryptamine, or 5-HT) transporters (5-HTT) are target-sites for commonly used antidepressants.	Serotonin	15-34	huntingtin	Homo sapiens	61-64
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
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
18775521-1	2008	Most of the disease causing proteins such as beta amyloid, amylin, and huntingtin protein, which are natively disordered, readily form fibrils consisting of beta-sheet polymers.	Polymers	168-176	huntingtin	Homo sapiens	71-81
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
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.	benzamil	0-3	huntingtin	Homo sapiens	25-35
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
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.	benzamil	0-3	huntingtin	Homo sapiens	51-54
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.	benzamil	35-38	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
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
18829967-2	2008	However, the precise mechanisms by which mutant huntingtin sensitize striatal cells to dopamine and glutamate inputs remain unclear.	Dopamine	87-95	huntingtin	Homo sapiens	48-58
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
18844975-0	2008	Mutant huntingtin activates Nrf2-responsive genes and impairs dopamine synthesis in a PC12 model of Huntington"s disease.	Dopamine	62-70	huntingtin	Homo sapiens	7-17
18829967-2	2008	However, the precise mechanisms by which mutant huntingtin sensitize striatal cells to dopamine and glutamate inputs remain unclear.	Glutamic Acid	100-109	huntingtin	Homo sapiens	48-58
18829967-3	2008	Here, we demonstrate in knock-in HD striatal cells that mutant huntingtin enhances dopamine-mediated striatal cell death via dopamine D(1) receptors.	Dopamine	83-91	huntingtin	Homo sapiens	63-73
18829967-3	2008	Here, we demonstrate in knock-in HD striatal cells that mutant huntingtin enhances dopamine-mediated striatal cell death via dopamine D(1) receptors.	Dopamine	125-133	huntingtin	Homo sapiens	63-73
18829967-4	2008	Moreover, we show that NMDA receptors specifically potentiate the vulnerability of mutant huntingtin striatal cells to dopamine toxicity as pretreatment with NMDA increased D(1)R-induced cell death in mutant but not wild-type cells.	Dopamine	119-127	huntingtin	Homo sapiens	90-100
18829967-4	2008	Moreover, we show that NMDA receptors specifically potentiate the vulnerability of mutant huntingtin striatal cells to dopamine toxicity as pretreatment with NMDA increased D(1)R-induced cell death in mutant but not wild-type cells.	N-Methylaspartate	23-27	huntingtin	Homo sapiens	90-100
18615096-4	2008	Huntingtin is phosphorylated at serine 421 by the kinase Akt but the role of this modification is unknown.	Serine	32-38	huntingtin	Homo sapiens	0-10
18640979-0	2008	Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease.	Rosiglitazone	0-13	huntingtin	Homo sapiens	69-79
18768695-0	2008	Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity.	Proline	24-31	huntingtin	Homo sapiens	55-65
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
18768695-3	2008	However, other parts of the protein, including the 17 N-terminal amino acids and two proline (polyP) repeat domains, regulate the toxicity of mutant Htt.	Proline	85-92	huntingtin	Homo sapiens	149-152
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
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
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
18573880-5	2008	This requires profilin"s G-actin binding activity and its direct interaction with Htt, which are both inhibited by the ROCK1-mediated phosphorylation of profilin at Ser-137.	Serine	165-168	huntingtin	Homo sapiens	82-85
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.	cytosine-adenine-guanine	33-57	huntingtin	Homo sapiens	144-154
18556210-6	2008	3Beta-(4-Methylphenyl)-2beta-[3"-(4-fluorobenzyl)isoxazol-5-yl]tropane (3b) with IC(50) of 5.9nM at the DAT and K(i)s of 454 and 113nM at the NET and 5-HTT, respectively, was the most potent and DAT-selective analog.	3beta-(4-methylphenyl)-2beta-[3"-(4-fluorobenzyl)isoxazol-5-yl]tropane	0-70	huntingtin	Homo sapiens	152-155
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.	cytosine-adenine-guanine	33-57	huntingtin	Homo sapiens	156-159
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	59-62	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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	59-62	huntingtin	Homo sapiens	156-159
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
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
18488016-3	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
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.	trinucleotide	91-104	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.	trinucleotide	91-104	huntingtin	Homo sapiens	156-159
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
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
18267960-3	2008	We show that in primary striatal cultures, dopamine increases the toxicity of an N-terminal fragment of mutated huntingtin (Htt-171-82Q).	Dopamine	43-51	huntingtin	Homo sapiens	124-127
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
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	100-103	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.	trinucleotide	104-117	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
18588526-1	2008	Huntington"s disease (HD) is caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene, which leads to neuronal loss in the striatum and cortex and to the appearance of neuronal intranuclear inclusions of mutant huntingtin.	cytosine-adenine-guanine	55-79	huntingtin	Homo sapiens	101-111
18588526-1	2008	Huntington"s disease (HD) is caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene, which leads to neuronal loss in the striatum and cortex and to the appearance of neuronal intranuclear inclusions of mutant huntingtin.	cytosine-adenine-guanine	55-79	huntingtin	Homo sapiens	242-252
18588526-1	2008	Huntington"s disease (HD) is caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene, which leads to neuronal loss in the striatum and cortex and to the appearance of neuronal intranuclear inclusions of mutant huntingtin.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	81-84	huntingtin	Homo sapiens	101-111
18588526-1	2008	Huntington"s disease (HD) is caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene, which leads to neuronal loss in the striatum and cortex and to the appearance of neuronal intranuclear inclusions of mutant huntingtin.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	81-84	huntingtin	Homo sapiens	242-252
18267960-0	2008	Dopamine determines the vulnerability of striatal neurons to the N-terminal fragment of mutant huntingtin through the regulation of mitochondrial complex II.	Dopamine	0-8	huntingtin	Homo sapiens	95-105
18267960-3	2008	We show that in primary striatal cultures, dopamine increases the toxicity of an N-terminal fragment of mutated huntingtin (Htt-171-82Q).	Dopamine	43-51	huntingtin	Homo sapiens	112-122
18403567-1	2008	BACKGROUND: Huntington disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an unstable expansion of the CAG trinucleotide repeat in exon 1 of the HTT (huntingtin) gene and typically has an adult onset.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	132-135	huntingtin	Homo sapiens	174-177
18403567-1	2008	BACKGROUND: Huntington disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an unstable expansion of the CAG trinucleotide repeat in exon 1 of the HTT (huntingtin) gene and typically has an adult onset.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	132-135	huntingtin	Homo sapiens	179-189
18403567-1	2008	BACKGROUND: Huntington disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an unstable expansion of the CAG trinucleotide repeat in exon 1 of the HTT (huntingtin) gene and typically has an adult onset.	trinucleotide	136-149	huntingtin	Homo sapiens	174-177
18403567-1	2008	BACKGROUND: Huntington disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an unstable expansion of the CAG trinucleotide repeat in exon 1 of the HTT (huntingtin) gene and typically has an adult onset.	trinucleotide	136-149	huntingtin	Homo sapiens	179-189
18081711-11	2008	Concomitant increases in cortisol were not observed, but dexamethasone treatment stimulated 5-HTT expression regardless of genotype/rearing group, and 5-HTT expression in the post-stressor sample was correlated with plasma cortisol levels at all time points.	Dexamethasone	57-70	huntingtin	Homo sapiens	94-97
18403126-4	2008	Although the basis of this specific vulnerability remains unclear, a great deal of evidence has documented the ability of the dopamine system to modulate the toxicity of expanded htt.	Dopamine	126-134	huntingtin	Homo sapiens	179-182
18403126-7	2008	Remarkably, low doses of a selective D1 receptors agonist or forskolin, an activator of adenylate cyclase, accelerated the formation of mutant htt nuclear aggregates, whereas the number of cytoplasmic aggregates was decreased.	Colforsin	61-70	huntingtin	Homo sapiens	143-146
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
18418060-3	2008	Recently it was proposed that rapamycin and its derivatives enhance the clearance (and/or reduce the accumulation) of mutant intracellular proteins causing proteinopathies such as tau, alpha-synuclein, ataxin-3, and full-length or fragments of huntingtin containing a polyglutamine (polyQ) expansion, by upregulating macroautophagy.	Sirolimus	30-39	huntingtin	Homo sapiens	244-254
18418060-5	2008	We found that rapamycin inhibits the aggregation of a fragment of huntingtin (exon 1) containing 97 polyQs similarly in macroautophagy-proficient (Atg5(+/+)) and macroautophagy-deficient (Atg5(-/-)) cells.	Sirolimus	14-23	huntingtin	Homo sapiens	66-76
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
18622081-2	2008	In particular, the neurotransmitter serotonin (5-hydroxytryptamine [5-HT]) has been hypothesized to play a role in skeletal metabolism via its transporter (5-HTT).	Serotonin	36-45	huntingtin	Homo sapiens	158-161
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
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
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
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
18379433-6	2008	Carbachol-stimulated release of intracellular calcium is significantly higher in cells expressing N-terminal mutant huntingtin and TG2 compared with vector-transfected cells; expression of either CaM-center or CaM-overlap in these cells returned the levels of carbachol-stimulated intracellular calcium release to control values.	Carbachol	0-9	huntingtin	Homo sapiens	116-126
18379433-6	2008	Carbachol-stimulated release of intracellular calcium is significantly higher in cells expressing N-terminal mutant huntingtin and TG2 compared with vector-transfected cells; expression of either CaM-center or CaM-overlap in these cells returned the levels of carbachol-stimulated intracellular calcium release to control values.	Calcium	46-53	huntingtin	Homo sapiens	116-126
18622081-2	2008	In particular, the neurotransmitter serotonin (5-hydroxytryptamine [5-HT]) has been hypothesized to play a role in skeletal metabolism via its transporter (5-HTT).	Serotonin	47-66	huntingtin	Homo sapiens	158-161
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	80-90
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
18065495-6	2008	Furthermore, we observed SDS-soluble wild-type htt (wthtt)-wthtt, wthtt-muhtt and muhtt-muhtt interactions, which were enhanced by the presence of Pak1.	Sodium Dodecyl Sulfate	25-28	huntingtin	Homo sapiens	47-50
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
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
18241680-8	2008	Phophorlyated Hsp27 also decreased the inclusion body formation by the huntingtin polyglutamines.	polyglutamine	82-96	huntingtin	Homo sapiens	71-81
18094623-6	2008	We show that the proline-rich region is essential for the Bag3-mediated stimulation of mutated huntingtin clearance.	Proline	17-24	huntingtin	Homo sapiens	95-105
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
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
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
18036835-3	2008	Of the biomarkers in the serotonin system, serotonin(1A) (5-HT(1A)) receptor is implicated in depression, and anxiety and serotonin transporter (5-HTT) is a target for selective serotonin reuptake inhibitors, psychotropic drugs used in the treatment of these disorders.	Serotonin	25-34	huntingtin	Homo sapiens	147-150
18036835-9	2008	Sex differences in 5-HT(1A) receptor and 5-HTT BP(ND) may reflect biological distinctions in the serotonin system contributing to sex differences in the prevalence of psychiatric disorders such as depression and anxiety.	Serotonin	97-106	huntingtin	Homo sapiens	43-46
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
17986868-7	2008	We compare these recent findings to the well characterized mammalian target of rapamycin, mTor, a protein described over a decade ago as related to huntingtin structurally by leucine-rich, repetitive HEAT sequences.	Leucine	175-182	huntingtin	Homo sapiens	148-158
18341412-1	2008	Huntington disease (HD), caused by polyglutamate expansions in the huntingtin protein, is a progressive neurodegenerative disease resulting in cognitive and motor impairments and death.	Polyglutamic Acid	35-48	huntingtin	Homo sapiens	67-77
18182772-6	2008	The association between the -1438AA vs. AG/GG genotypes and heroin dependence was enhanced in the presence of 12-repeat 5-HTT VNTR and short 5-HTTLPR alleles [24.8% in heroin-dependent patients vs. 12.6% in controls; corrected p = 0.045, OR = 2.28 (95% CI = 1.36-3.82)].	Heroin	60-66	huntingtin	Homo sapiens	122-125
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
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
17944533-5	2007	Applying this screening paradigm, we determined that a bioactive green tea extract contains an assemblage of catechins that were individually characterized for their respective protective effects against huntingtin and alpha-synuclein toxicity.	Catechin	109-118	huntingtin	Homo sapiens	204-214
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
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
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.	polyproline	90-101	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.	polyproline	90-101	huntingtin	Homo sapiens	163-166
17940007-3	2007	We introduced cholesterol-conjugated small interfering RNA duplexes (cc-siRNA) targeting human Htt mRNA (siRNA-Htt) into mouse striata that also received adeno-associated virus containing either expanded (100 CAG) or wild-type (18 CAG) Htt cDNA encoding huntingtin (Htt) 1-400.	Cholesterol	14-25	huntingtin	Homo sapiens	95-98
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
17940007-3	2007	We introduced cholesterol-conjugated small interfering RNA duplexes (cc-siRNA) targeting human Htt mRNA (siRNA-Htt) into mouse striata that also received adeno-associated virus containing either expanded (100 CAG) or wild-type (18 CAG) Htt cDNA encoding huntingtin (Htt) 1-400.	Cholesterol	14-25	huntingtin	Homo sapiens	111-114
17940007-3	2007	We introduced cholesterol-conjugated small interfering RNA duplexes (cc-siRNA) targeting human Htt mRNA (siRNA-Htt) into mouse striata that also received adeno-associated virus containing either expanded (100 CAG) or wild-type (18 CAG) Htt cDNA encoding huntingtin (Htt) 1-400.	Cholesterol	14-25	huntingtin	Homo sapiens	111-114
17940007-3	2007	We introduced cholesterol-conjugated small interfering RNA duplexes (cc-siRNA) targeting human Htt mRNA (siRNA-Htt) into mouse striata that also received adeno-associated virus containing either expanded (100 CAG) or wild-type (18 CAG) Htt cDNA encoding huntingtin (Htt) 1-400.	Cholesterol	14-25	huntingtin	Homo sapiens	254-264
17940007-3	2007	We introduced cholesterol-conjugated small interfering RNA duplexes (cc-siRNA) targeting human Htt mRNA (siRNA-Htt) into mouse striata that also received adeno-associated virus containing either expanded (100 CAG) or wild-type (18 CAG) Htt cDNA encoding huntingtin (Htt) 1-400.	Cholesterol	14-25	huntingtin	Homo sapiens	111-114
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
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
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
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
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
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
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
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
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
17611284-4	2007	We show here that huntingtin is phosphorylated by the cyclin-dependent kinase 5 (Cdk5) at serines 1181 and 1201.	Serine	90-97	huntingtin	Homo sapiens	18-28
17611284-7	2007	Absence of phosphorylation of huntingtin at serines 1181 and 1201 confers toxic properties to wild-type huntingtin in a p53-dependent manner in striatal neurons and accelerates neuronal death induced by DNA damage.	Serine	44-51	huntingtin	Homo sapiens	30-40
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
17455294-9	2007	Finally, treatment with 3-nitropropionic acid, a succinate dehydrogenase inhibitor, had opposite effects on the ubiquitin-proteasome system with activation in wild-type and decreased activity in mutant huntingtin expressing cells.	3-nitropropionic acid	24-45	huntingtin	Homo sapiens	202-212
17373643-0	2007	Mapping of the epitope of monoclonal antibody 2B4 to the proline-rich region of human Huntingtin, a region critical for aggregation and toxicity.	Proline	57-64	huntingtin	Homo sapiens	86-96
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
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
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
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
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
17287080-0	2007	Response of risperidone treatment may be associated with polymorphisms of HTT gene in Chinese schizophrenia patients.	Risperidone	12-23	huntingtin	Homo sapiens	74-77
17287080-7	2007	Our study has, for the first time, produced evidence that the potential for therapy in patients with schizophrenia is related to the HTTRLP polymorphism in the HTT gene and haplotype L-12 may help to predict risperidone treatment efficiency.	Risperidone	208-219	huntingtin	Homo sapiens	133-136
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	97-100	huntingtin	Homo sapiens	210-220
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.	trinucleotide	101-114	huntingtin	Homo sapiens	210-220
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
17687393-5	2007	CONCLUSION: The results definitely confirm the diagnosis of HD and indicate the CAG trinucleotide repeat expansion of IT15 gene in this HD family.	trinucleotide	84-97	huntingtin	Homo sapiens	118-122
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
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
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
17327906-6	2007	PA28gamma also improved cell viability in mutant huntingtin-expressing striatal neurons exposed to pathological stressors, such as the excitotoxin quinolinic acid and the reversible proteasome inhibitor MG132.	Quinolinic Acid	147-162	huntingtin	Homo sapiens	49-59
17327906-6	2007	PA28gamma also improved cell viability in mutant huntingtin-expressing striatal neurons exposed to pathological stressors, such as the excitotoxin quinolinic acid and the reversible proteasome inhibitor MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	203-208	huntingtin	Homo sapiens	49-59
17182613-0	2007	Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein.	Trehalose	0-9	huntingtin	Homo sapiens	92-102
17182613-4	2007	Trehalose-induced autophagy enhanced the clearance of autophagy substrates like mutant huntingtin and the A30P and A53T mutants of alpha-synuclein, associated with Huntington disease (HD) and Parkinson disease (PD), respectively.	Trehalose	0-9	huntingtin	Homo sapiens	87-97
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
17213954-6	2007	Htt fragments were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and detected with anti-Htt antibodies.	Sodium Dodecyl Sulfate	32-53	huntingtin	Homo sapiens	0-3
17213954-6	2007	Htt fragments were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and detected with anti-Htt antibodies.	polyacrylamide	54-68	huntingtin	Homo sapiens	0-3
17213954-6	2007	Htt fragments were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and detected with anti-Htt antibodies.	Sodium Dodecyl Sulfate	90-93	huntingtin	Homo sapiens	0-3
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
17596719-7	2007	Quantitative RT-PCR and SDS-PAGE experiments revealed that 17-DMAG induces expression of the molecular chaperones Hsp40, Hsp70, and Hsp105 in mammalian cells and inhibits the formation of mutant huntingtin aggregates with higher efficiency than 17-AAG or geldanamycin itself.	17-(dimethylaminoethylamino)-17-demethoxygeldanamycin	59-66	huntingtin	Homo sapiens	195-205
19172113-1	2007	Huntingtin containing an expanded polyglutamine causes neuronal death and Huntington disease.	polyglutamine	34-47	huntingtin	Homo sapiens	0-10
17116244-0	2006	Huntingtin inclusion bodies are iron-dependent centers of oxidative events.	Iron	32-36	huntingtin	Homo sapiens	0-10
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
17115386-1	2007	Huntington"s disease (HD) is a neurodegenerative disorder associated with expansion of CAG trinucleotide repeats in the huntingtin gene.	trinucleotide	91-104	huntingtin	Homo sapiens	120-130
17596719-0	2007	Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation.	polyglutamine	54-59	huntingtin	Homo sapiens	69-79
17184144-4	2007	Neurochemical changes are specifically oriented to deplete GABAergic and cholinergic systems, while molecular alterations include an increased expression of CAG trinucleotide at exon 1 from the huntingtin (htt) gene, as well as aggregation of mutant htt.	trinucleotide	161-174	huntingtin	Homo sapiens	194-204
17184144-4	2007	Neurochemical changes are specifically oriented to deplete GABAergic and cholinergic systems, while molecular alterations include an increased expression of CAG trinucleotide at exon 1 from the huntingtin (htt) gene, as well as aggregation of mutant htt.	trinucleotide	161-174	huntingtin	Homo sapiens	206-209
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
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
17151278-6	2006	Strikingly, mutant huntingtin diminished post-Golgi trafficking of Val-BDNF, whereas Met-BDNF was not modified.	Valine	67-70	huntingtin	Homo sapiens	19-29
17151278-8	2006	Moreover, mutant huntingtin severely affected the KCl-evoked release of Val-BDNF, although it had little effect on Met-BDNF regulated release.	Potassium Chloride	50-53	huntingtin	Homo sapiens	17-27
17151278-11	2006	We conclude that mutant huntingtin differently affects intracellular transport and release of Val-BDNF and Met-BDNF.	Valine	94-97	huntingtin	Homo sapiens	24-34
20396523-4	2006	Mutant huntingtin with abnormally long glutamine stretch aggregates and forms intranuclear inclusions.	Glutamine	39-48	huntingtin	Homo sapiens	7-17
17161366-0	2006	Structural insights into the specific binding of huntingtin proline-rich region with the SH3 and WW domains.	Proline	60-67	huntingtin	Homo sapiens	49-59
17161366-2	2006	We report the specific interactions of Htt proline-rich region (PRR) with the SH3GL3-SH3 domain and HYPA-WW1-2 domain pair by NMR.	Proline	43-50	huntingtin	Homo sapiens	39-42
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
16801344-9	2006	This may be relevant to the pathogenesis of human Huntington"s disease, as we have previously shown that both polyserine and polyalanine-containing proteins are modifiers of mutant huntingtin toxicity, with low expression levels of polyalanine-containing proteins having a protective effect.	polyserine	110-120	huntingtin	Homo sapiens	181-191
17034350-5	2006	Mutant htt-mediated toxicity in the brain disrupts a number of vital cellular processes in the course of disease progression, including energy metabolism, gene transcription, clathrin-dependent endocytosis, intraneuronal trafficking, and postsynaptic signaling, but the crucial initiation mechanism induced by mhtt is still unclear.	mhtt	310-314	huntingtin	Homo sapiens	7-10
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.	trinucleotide	36-49	huntingtin	Homo sapiens	149-159
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
16801344-9	2006	This may be relevant to the pathogenesis of human Huntington"s disease, as we have previously shown that both polyserine and polyalanine-containing proteins are modifiers of mutant huntingtin toxicity, with low expression levels of polyalanine-containing proteins having a protective effect.	polyalanine	125-136	huntingtin	Homo sapiens	181-191
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
17007735-1	2006	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, which is caused by an abnormal expansion of Cytosine Adenine Guanine (CAG) trinucleotide repeat in the gene making huntingtin (Htt).	cytosine adenine guanine	123-147	huntingtin	Homo sapiens	194-204
17007735-1	2006	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, which is caused by an abnormal expansion of Cytosine Adenine Guanine (CAG) trinucleotide repeat in the gene making huntingtin (Htt).	cytosine adenine guanine	123-147	huntingtin	Homo sapiens	206-209
17007735-1	2006	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, which is caused by an abnormal expansion of Cytosine Adenine Guanine (CAG) trinucleotide repeat in the gene making huntingtin (Htt).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	149-152	huntingtin	Homo sapiens	194-204
17007735-1	2006	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, which is caused by an abnormal expansion of Cytosine Adenine Guanine (CAG) trinucleotide repeat in the gene making huntingtin (Htt).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	149-152	huntingtin	Homo sapiens	206-209
17007735-1	2006	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, which is caused by an abnormal expansion of Cytosine Adenine Guanine (CAG) trinucleotide repeat in the gene making huntingtin (Htt).	trinucleotide	154-167	huntingtin	Homo sapiens	194-204
17007735-1	2006	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder, which is caused by an abnormal expansion of Cytosine Adenine Guanine (CAG) trinucleotide repeat in the gene making huntingtin (Htt).	trinucleotide	154-167	huntingtin	Homo sapiens	206-209
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
16414028-8	2006	High concentrations of 5-HTT-positive fibers in the central nucleus indicate that tight regulation of serotonin is critical in modulating fear responses mediated by this nucleus.	Serotonin	102-111	huntingtin	Homo sapiens	25-28
16856124-2	2006	The serotonin transporter (HTT) regulates the availability of serotonin by reuptake of the neurotransmitter from the synaptic cleft.	Serotonin	4-13	huntingtin	Homo sapiens	27-30
16966188-3	2006	The separate and combined analyses of the gene-linked polymorphic region (5-HTTLPR) and the Intron 2 VNTR suggest that these two HTT polymorphisms may contribute to acute subjective responses to d-amphetamine with a small effect.	Dextroamphetamine	195-208	huntingtin	Homo sapiens	76-79
16893904-0	2006	Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington"s disease models.	epigallocatechin gallate	10-38	huntingtin	Homo sapiens	65-75
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
16893904-3	2006	Here, we demonstrate that the green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG) potently inhibits the aggregation of mutant htt exon 1 protein in a dose-dependent manner.	Polyphenols	40-50	huntingtin	Homo sapiens	133-136
16893904-3	2006	Here, we demonstrate that the green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG) potently inhibits the aggregation of mutant htt exon 1 protein in a dose-dependent manner.	epigallocatechin gallate	51-81	huntingtin	Homo sapiens	133-136
16893904-3	2006	Here, we demonstrate that the green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG) potently inhibits the aggregation of mutant htt exon 1 protein in a dose-dependent manner.	epigallocatechin gallate	83-87	huntingtin	Homo sapiens	133-136
16893904-4	2006	Dot-blot assays and atomic force microscopy studies revealed that EGCG modulates misfolding and oligomerization of mutant htt exon 1 protein in vitro, indicating that it interferes with very early events in the aggregation process.	epigallocatechin gallate	66-70	huntingtin	Homo sapiens	122-125
16893904-5	2006	Also, EGCG significantly reduced polyQ-mediated htt protein aggregation and cytotoxicity in an yeast model of HD.	epigallocatechin gallate	6-10	huntingtin	Homo sapiens	48-51
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
16893904-6	2006	When EGCG was fed to transgenic HD flies overexpressing a pathogenic htt exon 1 protein, photoreceptor degeneration and motor function improved.	epigallocatechin gallate	5-9	huntingtin	Homo sapiens	69-72
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.	epigallocatechin gallate	89-93	huntingtin	Homo sapiens	42-45
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
16414028-9	2006	High concentrations of 5-HTT-labeled fibers in the intercalated islands and parvicellular basal nucleus/paralaminar nucleus, which contain immature -appearing neurons, suggest a potential trophic role for serotonin in these subregions.	Serotonin	205-214	huntingtin	Homo sapiens	25-28
16829072-1	2006	Thirteen years ago, the culmination of genetic rather than biochemical strategies resulted in the identification of the root cause of Huntington"s disease: an expanded CAG trinucleotide repeat that leads to an elongated polyglutamine tract in the huntingtin protein.	trinucleotide	172-185	huntingtin	Homo sapiens	247-257
16829072-2	2006	Since then, biochemical and cell biological attempts to elucidate pathogenesis have largely focused on N-terminal polyglutamine-containing huntingtin fragments.	n-terminal polyglutamine	103-127	huntingtin	Homo sapiens	139-149
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
16854064-2	2006	The results show that binding to the dopamine and serotonin transporters (DAT and 5-HTT) is highly dependent on the specific linker used.	Dopamine	37-45	huntingtin	Homo sapiens	84-87
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
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
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
16854064-4	2006	Cyclo-3beta-(4-aminophenyl)-2beta-tropanemethanol sebacic acid ester/amide (5e) had a Ki of 1.9 nM at the 5-HTT and was 68- and 737-fold selective for the 5-HTT relative to the DAT and NET.	cyclo-3beta-(4-aminophenyl)-2beta-tropanemethanol sebacic acid ester	0-68	huntingtin	Homo sapiens	108-111
16854064-4	2006	Cyclo-3beta-(4-aminophenyl)-2beta-tropanemethanol sebacic acid ester/amide (5e) had a Ki of 1.9 nM at the 5-HTT and was 68- and 737-fold selective for the 5-HTT relative to the DAT and NET.	cyclo-3beta-(4-aminophenyl)-2beta-tropanemethanol sebacic acid ester	0-68	huntingtin	Homo sapiens	157-160
16854064-4	2006	Cyclo-3beta-(4-aminophenyl)-2beta-tropanemethanol sebacic acid ester/amide (5e) had a Ki of 1.9 nM at the 5-HTT and was 68- and 737-fold selective for the 5-HTT relative to the DAT and NET.	Amides	69-74	huntingtin	Homo sapiens	108-111
16854064-4	2006	Cyclo-3beta-(4-aminophenyl)-2beta-tropanemethanol sebacic acid ester/amide (5e) had a Ki of 1.9 nM at the 5-HTT and was 68- and 737-fold selective for the 5-HTT relative to the DAT and NET.	Amides	69-74	huntingtin	Homo sapiens	157-160
16616982-2	2006	The serotonin transporter (5-HTT) may play an important role in the termination of serotonergic neurotransmission by serotonin (5-HT) uptaking into presynaptic neurons and representing as an initial action site for selective 5-HTT reuptake inhibitors (SSRI).	Serotonin	4-13	huntingtin	Homo sapiens	29-32
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
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
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.	Reactive Oxygen Species	190-213	huntingtin	Homo sapiens	108-118
16570300-1	2006	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder that results from an expanded trinucleotide (CAG) repeat on the huntingtin gene.	trinucleotide	120-133	huntingtin	Homo sapiens	154-164
16570300-1	2006	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder that results from an expanded trinucleotide (CAG) repeat on the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	135-138	huntingtin	Homo sapiens	154-164
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
16616982-2	2006	The serotonin transporter (5-HTT) may play an important role in the termination of serotonergic neurotransmission by serotonin (5-HT) uptaking into presynaptic neurons and representing as an initial action site for selective 5-HTT reuptake inhibitors (SSRI).	Serotonin	4-13	huntingtin	Homo sapiens	227-230
16616982-7	2006	The higher level of mRNA expressions of IFNgamma and 5-HTT diminished after fluoxetine treatment.	Fluoxetine	76-86	huntingtin	Homo sapiens	55-58
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).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	89-92	huntingtin	Homo sapiens	196-206
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).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	89-92	huntingtin	Homo sapiens	208-211
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).	trinucleotide	93-106	huntingtin	Homo sapiens	196-206
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).	trinucleotide	93-106	huntingtin	Homo sapiens	208-211
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
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
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
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
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
16504973-13	2006	The extent of lateralization was strongly related to age at onset and to the number of cytosine-adenine-guanine (CAG) triplet repeats on gene IT15.	cytosine-adenine-guanine	87-111	huntingtin	Homo sapiens	142-146
16504973-13	2006	The extent of lateralization was strongly related to age at onset and to the number of cytosine-adenine-guanine (CAG) triplet repeats on gene IT15.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	113-116	huntingtin	Homo sapiens	142-146
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
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
16874097-3	2006	Induction of autophagy by lithium led to enhanced clearance of autophagy substrates, like mutant huntingtin fragments and mutant alpha-synucleins, associated with Huntington"s disease (HD) and some autosomal dominant forms of Parkinson"s disease (PD), respectively.	Lithium	26-33	huntingtin	Homo sapiens	97-107
16633150-0	2006	Time course of in vivo 5-HTT transporter occupancy by fluvoxamine.	Fluvoxamine	54-65	huntingtin	Homo sapiens	25-28
16633150-2	2006	In this study, we measured the time course of the selective serotonin reuptake inhibitor fluvoxamine in the human brain based on serotonin transporter (5-HTT) occupancy by positron emission tomography.	Fluvoxamine	89-100	huntingtin	Homo sapiens	154-157
16633150-6	2006	The relationship between the plasma concentration of fluvoxamine and 5-HTT occupancy at these different time points was fitted to the law of mass action.	Fluvoxamine	53-64	huntingtin	Homo sapiens	71-74
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
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
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
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
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
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
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
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	93-100	huntingtin	Homo sapiens	119-129
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
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
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.	oligoproline	121-133	huntingtin	Homo sapiens	53-63
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
16279803-5	2005	However, the 2beta,3beta-diaryltropanes tended to be more potent at the DAT and more selective for the DAT relative to the NET and 5-HTT.	3beta-diaryltropanes	19-39	huntingtin	Homo sapiens	133-136
16279803-6	2005	One of the most interesting compounds was 3beta-(4-methylphenyl)-2beta-(4-methylphenyl)tropane (3d), which showed an IC50 of 1.23 nM at the DAT with 289- and 185-fold selectivity for the DAT relative to the NET and 5-HTT.	3beta-(4-methylphenyl)-2beta-(4-methylphenyl)tropane	42-94	huntingtin	Homo sapiens	217-220
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
16138320-1	2005	The aim of this study was to explore the potential of a new selective serotonin transporter (5-HTT) inhibitor, N,N-dimethyl-2-(2-amino-4-methylphenylthio)benzylamine (MADAM, K(i)=1.65 nM), as a PET radioligand for examination of 5-HTT in the nonhuman primate brain.	N,N-dimethyl-2-(2-amino-4-methylphenylthio)benzylamine	111-165	huntingtin	Homo sapiens	95-98
16138320-1	2005	The aim of this study was to explore the potential of a new selective serotonin transporter (5-HTT) inhibitor, N,N-dimethyl-2-(2-amino-4-methylphenylthio)benzylamine (MADAM, K(i)=1.65 nM), as a PET radioligand for examination of 5-HTT in the nonhuman primate brain.	N,N-dimethyl-2-(2-amino-4-methylphenylthio)benzylamine	111-165	huntingtin	Homo sapiens	231-234
16162412-1	2005	We have identified a novel interaction between huntingtin (htt) and N-type calcium channels, a channel key in coupling calcium influx with synaptic vesicle exocytosis.	Calcium	75-82	huntingtin	Homo sapiens	47-57
16162412-1	2005	We have identified a novel interaction between huntingtin (htt) and N-type calcium channels, a channel key in coupling calcium influx with synaptic vesicle exocytosis.	Calcium	75-82	huntingtin	Homo sapiens	59-62
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
16162412-6	2005	Our data indicate that htt(exon1) enhances calcium influx by blocking syntaxin 1A inhibition of N-type calcium channels and attributes a key role for htt N-terminal fragments in the fine tuning of neurotransmission.	Calcium	43-50	huntingtin	Homo sapiens	23-26
16055197-2	2005	HD is caused by an expanded trinucleotide CAG repeat in the gene coding for the protein huntingtin.	trinucleotide	28-41	huntingtin	Homo sapiens	88-98
16085648-0	2005	Huntingtin associates with acidic phospholipids at the plasma membrane.	Phospholipids	34-47	huntingtin	Homo sapiens	0-10
16085648-4	2005	In cells, N-terminal huntingtin fragments targeted to regions of plasma membrane enriched in phosphatidylinositol 4,5-bisphosphate, receptor bound-transferrin, and endogenous huntingtin.	Phosphatidylinositol 4,5-Diphosphate	93-130	huntingtin	Homo sapiens	21-31
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
16085648-6	2005	Our data support a new model in which huntingtin directly binds membranes through electrostatic interactions with acidic phospholipids.	Phospholipids	121-134	huntingtin	Homo sapiens	38-48
16115812-8	2005	Thus, the polyglutamine tract in huntingtin appears to regulate mitochondrial ADP-phosphorylation in a Ca2+-dependent process that fulfills the genetic criteria for the HD trigger of pathogenesis, and it thereby determines a fundamental biological parameter--cellular energy status, which may contribute to the exquisite vulnerability of striatal neurons in HD.	Adenosine Diphosphate	78-81	huntingtin	Homo sapiens	33-43
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
16186256-4	2005	We show that lithium induces autophagy, and thereby, enhances the clearance of autophagy substrates, like mutant huntingtin and alpha-synucleins.	Lithium	13-20	huntingtin	Homo sapiens	113-123
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
16181417-4	2005	When incubated in concentrated formic acid, purified inclusions release a polymer, an oligomer and a broad range of N-terminal fragments of expanded huntingtin.	formic acid	31-42	huntingtin	Homo sapiens	149-159
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
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
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	133-143
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
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
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
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
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
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.	Asparagine	216-226	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
15809304-3	2005	This neuroprotective effect involves the phosphorylation of huntingtin at Ser(421) by the prosurvival kinase Akt (Humbert, S., Bryson, E. A., Cordelieres, F. P., Connors, N. C., Datta, S. R., Finkbeiner, S., Greenberg, M. E., and Saudou, F. (2002) Dev.	Serine	74-77	huntingtin	Homo sapiens	60-70
15916486-1	2005	Huntington"s disease (HD) is an inherited autosomal dominant, neurodegenerative disease that is caused by a gain of function mutation characterized by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (htt) gene.	trinucleotide	174-187	huntingtin	Homo sapiens	212-222
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
15832309-2	2005	The disease is caused by the abnormal expansion of a CAG trinucleotide repeat in the first exon of the huntingtin gene in chromosome 4p16.3.	trinucleotide	57-70	huntingtin	Homo sapiens	103-113
15916486-1	2005	Huntington"s disease (HD) is an inherited autosomal dominant, neurodegenerative disease that is caused by a gain of function mutation characterized by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (htt) gene.	trinucleotide	174-187	huntingtin	Homo sapiens	224-227
15777787-2	2005	Here, we report uptake of silica (SiO(2)) nanoparticles to the cell nucleus where they induce aberrant clusters of topoisomerase I (topo I) in the nucleoplasm that additionally contain signature proteins of nuclear domains, and protein aggregation such as ubiquitin, proteasomes, cellular glutamine repeat (polyQ) proteins, and huntingtin.	Silicon Dioxide	26-32	huntingtin	Homo sapiens	328-338
15777787-2	2005	Here, we report uptake of silica (SiO(2)) nanoparticles to the cell nucleus where they induce aberrant clusters of topoisomerase I (topo I) in the nucleoplasm that additionally contain signature proteins of nuclear domains, and protein aggregation such as ubiquitin, proteasomes, cellular glutamine repeat (polyQ) proteins, and huntingtin.	Silicon Dioxide	34-40	huntingtin	Homo sapiens	328-338
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
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
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
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.	trinucleotide	165-178	huntingtin	Homo sapiens	10-13
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	30-43	huntingtin	Homo sapiens	70-73
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
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
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
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.	trinucleotide	36-49	huntingtin	Homo sapiens	163-173
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
15715085-2	2005	Our laboratory previously demonstrated that huntingtin protein colocalizes with transglutaminase 2 and its product, the epsilon-(gamma-glutamyl)lysine bond in intranuclear inclusions in HD frontal cortex.	Lysine	144-150	huntingtin	Homo sapiens	44-54
15715085-7	2005	Treatment of cells with cystamine, a chemical inhibitor of transglutaminase, decreased aggregated and cross-linked huntingtin and increased viability of cells that were transfected with transglutaminase 2 and htt-N63-148Q-myc.	Cystamine	24-33	huntingtin	Homo sapiens	115-125
15715085-7	2005	Treatment of cells with cystamine, a chemical inhibitor of transglutaminase, decreased aggregated and cross-linked huntingtin and increased viability of cells that were transfected with transglutaminase 2 and htt-N63-148Q-myc.	Cystamine	24-33	huntingtin	Homo sapiens	209-212
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
16471265-7	2005	This anti-apopototic effect is mediated via the phosphorylation of serine 421 of huntingtin.	Serine	67-73	huntingtin	Homo sapiens	81-91
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
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
15583118-4	2004	Carbon 11-labeled 3-amino-4-(2-dimethylaminomethyl-phenylsulfanyl)-benzonitrile (DASB) positron emission tomography (PET) is the first brain imaging technique that can measure the 5-HTT BP in cortical and subcortical brain regions in vivo.	Carbon-11	0-9	huntingtin	Homo sapiens	182-185
15583118-4	2004	Carbon 11-labeled 3-amino-4-(2-dimethylaminomethyl-phenylsulfanyl)-benzonitrile (DASB) positron emission tomography (PET) is the first brain imaging technique that can measure the 5-HTT BP in cortical and subcortical brain regions in vivo.	3-amino-4-(2-dimethylaminomethylphenylsulfanyl)benzonitrile	18-79	huntingtin	Homo sapiens	182-185
15583118-4	2004	Carbon 11-labeled 3-amino-4-(2-dimethylaminomethyl-phenylsulfanyl)-benzonitrile (DASB) positron emission tomography (PET) is the first brain imaging technique that can measure the 5-HTT BP in cortical and subcortical brain regions in vivo.	3-amino-4-(2-dimethylaminomethylphenylsulfanyl)benzonitrile	81-85	huntingtin	Homo sapiens	182-185
15583118-13	2004	The magnitude of regional 5-HTT BP can provide a vulnerability to low levels of extracellular serotonin and symptoms of extremely negativistic dysfunctional attitudes.	Serotonin	94-103	huntingtin	Homo sapiens	28-31
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
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
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	117-121
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
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.	Adenosine	120-129	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.	Adenosine	304-313	huntingtin	Homo sapiens	99-109
15474886-4	2004	Transgenic R6/1 mice that incorporate a human genomic fragment containing promoter elements exon 1 and a portion of intron 2 of the huntingtin gene responsible for Huntington"s disease develop late-onset neurologic deficits in a manner similar to the motor abnormalities of Huntington"s disease and show increased survival rates and decreased neurologic deficits when supplemented with essential fatty acids throughout life.	Fatty Acids, Essential	386-407	huntingtin	Homo sapiens	132-142
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
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
15340079-6	2004	Consistent with a progressive loss of function, wild-type htt, trafficking motors, and mitochondrial components were selectively sequestered by mhtt in human Huntington"s disease-affected brain.	mhtt	144-148	huntingtin	Homo sapiens	58-61
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
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
15140195-0	2004	Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity.	polyglutamine	39-52	huntingtin	Homo sapiens	11-21
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
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
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
14985437-7	2004	Transfection with transglutaminase 2 and htt-N63-148Q-myc followed by treatment of cells with N-(6-aminohexyl)-1-naphthalenesulfonamide, a calmodulin inhibitor, resulted in a decrease in cross-linked huntingtin.	N-(6-aminohexyl)-1-naphthalenesulfonamide	94-135	huntingtin	Homo sapiens	200-210
14969746-3	2004	We show that malonate stress increases the number of dead or dying cells when organotypic slice cultures are transduced to express pathological-length huntingtin fragments.	malonic acid	13-21	huntingtin	Homo sapiens	151-161
14715959-0	2004	Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction.	polyproline	61-72	huntingtin	Homo sapiens	0-10
14978683-2	2004	Because the protein Huntingtin interacts with the homocysteine metabolism modulating enzyme cystathionine beta-synthase, we hypothesize that homocysteine promotes neurodegeneration in HD.	Homocysteine	50-62	huntingtin	Homo sapiens	20-30
14978683-2	2004	Because the protein Huntingtin interacts with the homocysteine metabolism modulating enzyme cystathionine beta-synthase, we hypothesize that homocysteine promotes neurodegeneration in HD.	Homocysteine	141-153	huntingtin	Homo sapiens	20-30
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.	Proline	23-31	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.	Proline	23-31	huntingtin	Homo sapiens	114-117
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
12810713-6	2003	Expression of the mutated huntingtin also induced tyrosine phosphorylation of NR2B (NMDA receptor 2B) subunits, and co-expression of PSD-95 enhanced the phosphorylation.	Tyrosine	50-58	huntingtin	Homo sapiens	26-36
14725621-0	2004	The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin.	Serine	112-118	huntingtin	Homo sapiens	65-75
14725621-0	2004	The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin.	Serine	112-118	huntingtin	Homo sapiens	126-136
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
14725621-3	2004	Indeed, upon IGF-1 activation, Akt phosphorylates polyQ-huntingtin at serine 421 and abrogates its toxicity.	Serine	70-76	huntingtin	Homo sapiens	56-66
14725621-6	2004	We show that SGK phosphorylates huntingtin at serine 421 and that phosphorylation can protect striatal neurons against polyQ-huntingtin-induced toxicity.	Serine	46-52	huntingtin	Homo sapiens	32-42
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
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
15218539-2	2004	HD is caused by a trinucleotide (CAG) repeat mutation, encoding an expanded polyglutamine tract in the huntingtin protein.	trinucleotide	18-31	huntingtin	Homo sapiens	103-113
15218539-2	2004	HD is caused by a trinucleotide (CAG) repeat mutation, encoding an expanded polyglutamine tract in the huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	103-113
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
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
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
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
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.	Glutamine	117-127	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.	Sodium Dodecyl Sulfate	134-137	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
12888569-4	2003	We found that mutant htt promotes the aggregation of wild-type htt, causing the formation of SDS-resistant co-aggregates with a fibrillar morphology.	Sodium Dodecyl Sulfate	93-96	huntingtin	Homo sapiens	21-24
12888569-4	2003	We found that mutant htt promotes the aggregation of wild-type htt, causing the formation of SDS-resistant co-aggregates with a fibrillar morphology.	Sodium Dodecyl Sulfate	93-96	huntingtin	Homo sapiens	63-66
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
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
13679594-2	2003	HD is caused by the expansion of a CAG trinucleotide repeat stretch in the coding sequence of the HD gene that gives rise to a long polyglutamine tract in the huntingtin protein.	trinucleotide	39-52	huntingtin	Homo sapiens	159-169
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
12810713-0	2003	Expression of polyglutamine-expanded huntingtin induces tyrosine phosphorylation of N-methyl-D-aspartate receptors.	Tyrosine	56-64	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
12810713-7	2003	Treatment of SU6656 (a specific Src inhibitor) or co-expression of a mutated NR2B subunit with mutations of all three major tyrosine phosphorylation sites significantly attenuated neuronal toxicity induced by the mutated huntingtin.	SU 6656	13-19	huntingtin	Homo sapiens	221-231
12810713-7	2003	Treatment of SU6656 (a specific Src inhibitor) or co-expression of a mutated NR2B subunit with mutations of all three major tyrosine phosphorylation sites significantly attenuated neuronal toxicity induced by the mutated huntingtin.	Tyrosine	124-132	huntingtin	Homo sapiens	221-231
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
12810713-9	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.	Tyrosine	82-90	huntingtin	Homo sapiens	61-71
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.	Tyrosine	82-90	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.	Tyrosine	159-167	huntingtin	Homo sapiens	61-71
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.	Tyrosine	159-167	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
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	101-104	huntingtin	Homo sapiens	169-179
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
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
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).	Calcium	151-158	huntingtin	Homo sapiens	0-10
12873381-0	2003	Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1.	Calcium	66-73	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
12873381-6	2003	Transfection of full-length Httexp or caspase-resistant Httexp, but not normal Htt, into medium spiny striatal neurons faciliates Ca2+ release in response to threshold concentrations of the selective mGluR1/5 agonist 3,5-DHPG.	3,5-dihydroxyphenylglycine	217-225	huntingtin	Homo sapiens	28-31
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
12783847-2	2003	CAG DNA expansion results in a polyglutamine tract expansion in mutant huntingtin protein.	polyglutamine	31-44	huntingtin	Homo sapiens	71-81
12783847-7	2003	Leptomycin B treatment of clonal striatal cells enhanced the nuclear localization of huntingtin, and a mutant NES huntingtin displayed increased nuclear localization, indicating that huntingtin can shuttle to and from the nucleus.	leptomycin B	0-12	huntingtin	Homo sapiens	85-95
12783847-7	2003	Leptomycin B treatment of clonal striatal cells enhanced the nuclear localization of huntingtin, and a mutant NES huntingtin displayed increased nuclear localization, indicating that huntingtin can shuttle to and from the nucleus.	leptomycin B	0-12	huntingtin	Homo sapiens	114-124
12783847-7	2003	Leptomycin B treatment of clonal striatal cells enhanced the nuclear localization of huntingtin, and a mutant NES huntingtin displayed increased nuclear localization, indicating that huntingtin can shuttle to and from the nucleus.	leptomycin B	0-12	huntingtin	Homo sapiens	114-124
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	107-112	huntingtin	Homo sapiens	153-156
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
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
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	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
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
12824708-4	2003	The genetic defect is a CAG trinucleotide repeat expansion at the 5" end of the IT-15 gene on chromosome 4.	trinucleotide	28-41	huntingtin	Homo sapiens	80-85
12528814-4	2003	Using immunofluorescence and confocal microscopy we demonstrate 99% colocalization of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine covalent cross-links with nuclear aggregates of huntingtin protein in the frontal cortex of postmortem HD brain tissue.	epsilon-(gamma-glutamyl)-lysine	113-144	huntingtin	Homo sapiens	193-203
12528814-6	2003	Transient transfection of N-terminally truncated huntingtin with an expanded glutamine domain (htt-N63-148Q-myc) with and without and transglutaminase 2 into HEK 293T cells resulted in an increase in cross-linked huntingtin in the insoluble formic acid-treated pellet in comparison to transfection of N-terminally truncated huntingtin with normal length glutamine domain (htt-N63-18Q-myc).	formic acid	241-252	huntingtin	Homo sapiens	49-59
12528814-6	2003	Transient transfection of N-terminally truncated huntingtin with an expanded glutamine domain (htt-N63-148Q-myc) with and without and transglutaminase 2 into HEK 293T cells resulted in an increase in cross-linked huntingtin in the insoluble formic acid-treated pellet in comparison to transfection of N-terminally truncated huntingtin with normal length glutamine domain (htt-N63-18Q-myc).	formic acid	241-252	huntingtin	Homo sapiens	95-98
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
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
12200414-0	2002	Calcium-dependent cleavage of endogenous wild-type huntingtin in primary cortical neurons.	Calcium	0-7	huntingtin	Homo sapiens	51-61
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
12486229-0	2002	Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans neurons from huntingtin polyglutamine neurotoxicity.	Proline	10-17	huntingtin	Homo sapiens	82-92
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
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
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
12200548-4	2002	Using this method, a total of 25 benzothiazole derivatives that inhibit huntingtin fibrillogenesis in a dose-dependent manner were discovered from a library of approximately 184,000 small molecules.	benzothiazole	33-46	huntingtin	Homo sapiens	72-82
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
12171927-0	2002	Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization.	polyglutamine	55-68	huntingtin	Homo sapiens	0-10
12171927-4	2002	Furthermore, Congo Red, a dye that stains amyloid fibrils, prevented the assembly of mutant htt into mature fibrils, but not the formation of protofibrils.	Congo Red	13-22	huntingtin	Homo sapiens	92-95
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
12200414-5	2002	Exposure of primary neurons to glutamate or 3-nitropropionic acid increases intracellular calcium concentration, leading to loss of intact full-length wild-type huntingtin.	Glutamic Acid	31-40	huntingtin	Homo sapiens	161-171
12200414-5	2002	Exposure of primary neurons to glutamate or 3-nitropropionic acid increases intracellular calcium concentration, leading to loss of intact full-length wild-type huntingtin.	3-nitropropionic acid	44-65	huntingtin	Homo sapiens	161-171
12200414-5	2002	Exposure of primary neurons to glutamate or 3-nitropropionic acid increases intracellular calcium concentration, leading to loss of intact full-length wild-type huntingtin.	Calcium	90-97	huntingtin	Homo sapiens	161-171
12200414-7	2002	Degradation of wild-type huntingtin by calcium-dependent proteases thus occurs in HD neurons, leading to loss of wild-type huntingtin neuroprotective activity.	Calcium	39-46	huntingtin	Homo sapiens	25-35
12200414-7	2002	Degradation of wild-type huntingtin by calcium-dependent proteases thus occurs in HD neurons, leading to loss of wild-type huntingtin neuroprotective activity.	Calcium	39-46	huntingtin	Homo sapiens	123-133
12460551-0	2002	Polyglutamine repeat length-dependent proteolysis of huntingtin.	polyglutamine	0-13	huntingtin	Homo sapiens	53-63
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
12460551-1	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
12523115-0	2002	[Clinical picture of patients with Huntington"s disease in relation to the number of trinucleotide CAG repeats in IT-15 gene].	trinucleotide	85-98	huntingtin	Homo sapiens	114-119
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	66-76
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
12523115-6	2002	The number of CAG repeats in examination of the IT-15 gene was determined by polymerase chain reaction (PCR) and separation of radioisotope labelled PCR product against DNA size marker in polyacrylamide gel.	polyacrylamide	188-202	huntingtin	Homo sapiens	48-53
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
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
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
11983185-5	2002	Positron emission tomography scans were performed using a selective ligand for 5-HTT, [11C](+)McN5652.	Carbon-11	87-90	huntingtin	Homo sapiens	81-84
12077181-8	2002	The rate of cleavage of Htt by calpain was polyglutamine-length-dependent.	polyglutamine	43-56	huntingtin	Homo sapiens	24-27
12062094-1	2002	In the search for neuroprotective factors in Huntington"s disease, we found that insulin growth factor 1 via activation of the serine/threonine kinase Akt/PKB is able to inhibit neuronal death specifically induced by mutant huntingtin containing an expanded polyglutamine stretch.	Serine	127-133	huntingtin	Homo sapiens	224-234
11978772-8	2002	However, we observed that mutant huntingtin caused increased levels of ROS in neuronal and non-neuronal cells.	Reactive Oxygen Species	71-74	huntingtin	Homo sapiens	33-43
11978772-10	2002	HSP27 decreased ROS in cells expressing mutant huntingtin, suggesting that this chaperone protects cells against oxidative stress.	Reactive Oxygen Species	16-19	huntingtin	Homo sapiens	47-57
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
11978772-0	2002	Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin.	Reactive Oxygen Species	94-117	huntingtin	Homo sapiens	128-138
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
11739372-4	2002	Huntingtin-positive nuclear bodies redistributed after treatment with sodium butyrate.	Butyric Acid	70-85	huntingtin	Homo sapiens	0-10
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
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
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
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.	polyproline	96-101	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
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
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
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
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
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
11789098-4	2001	The toxicity of mutant huntingtin, or the loss of its normal function, causes disruption of cellular functions such as protein and calcium metabolism, transmitter release, mitochondria and gene transcription.	Calcium	131-138	huntingtin	Homo sapiens	23-33
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
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
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
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
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
11571498-6	2001	These results are consistent with the conclusion that Huntington"s disease may be associated with an abnormality of neuronal membrane fatty acid metabolism, possibly as a consequence of an as yet unidentified action of huntingtin.	Fatty Acids	134-144	huntingtin	Homo sapiens	219-229
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
11319238-4	2001	However, how polyglutamine expansion in huntingtin promotes glutamate-mediated excitotoxicity remains a mystery.	Glutamic Acid	60-69	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.	N-Methylaspartate	80-100	huntingtin	Homo sapiens	50-60
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.	N-Methylaspartate	80-100	huntingtin	Homo sapiens	222-232
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.	N-Methylaspartate	80-100	huntingtin	Homo sapiens	222-232
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.	N-Methylaspartate	102-106	huntingtin	Homo sapiens	50-60
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.	N-Methylaspartate	102-106	huntingtin	Homo sapiens	222-232
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.	N-Methylaspartate	102-106	huntingtin	Homo sapiens	222-232
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
11319238-6	2001	The expression of polyglutamine-expanded huntingtin causes sensitization of NMDA receptors and promotes neuronal apoptosis induced by glutamate.	Glutamic Acid	134-143	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
11319238-9	2001	Our results demonstrate that polyglutamine expansion impairs the ability of huntingtin to bind PSD-95 and inhibits glutamate-mediated excitotoxicity.	Glutamic Acid	115-124	huntingtin	Homo sapiens	76-86
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
11399172-2	2001	Both head-to-head (HTH) and head-to-tail (HTT) rotamer forms are found in the crystal structure of cis-[PtCl(2)(quinoline)(2)].	cis-[ptcl(2)	99-111	huntingtin	Homo sapiens	42-45
11443529-1	2001	The promoter polymorphism of the serotonin transporter gene (HTT, locus SLC6A4) is of special interest in autism given the well-replicated platelet hyperserotonemia of autism, treatment effects of serotonin reuptake inhibitors, and the role of serotonin in limbic functioning and neurodevelopment.	Serotonin	33-42	huntingtin	Homo sapiens	61-64
11443529-1	2001	The promoter polymorphism of the serotonin transporter gene (HTT, locus SLC6A4) is of special interest in autism given the well-replicated platelet hyperserotonemia of autism, treatment effects of serotonin reuptake inhibitors, and the role of serotonin in limbic functioning and neurodevelopment.	Serotonin	197-206	huntingtin	Homo sapiens	61-64
11399172-2	2001	Both head-to-head (HTH) and head-to-tail (HTT) rotamer forms are found in the crystal structure of cis-[PtCl(2)(quinoline)(2)].	quinoline	112-121	huntingtin	Homo sapiens	42-45
11406606-7	2001	The results suggest that the combination of mutant huntingtin and a source of oxyradical stress (provided in this case by dopamine) induces autophagy and may underlie the selective cell death characteristic of HD.	Dopamine	122-130	huntingtin	Homo sapiens	51-61
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
11406612-0	2001	Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington"s disease.	geldanamycin	0-12	huntingtin	Homo sapiens	58-68
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
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
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
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
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
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.	tetramethylenedisulfotetramine	236-239	huntingtin	Homo sapiens	4-14
11359930-4	2001	Inhibition of proteasome activity resulted in a twofold increase in the amount of ubiquitinated, SDS-resistant aggregates, indicating that inclusion bodies accumulate when the capacity of the ubiquitin-proteasome system to degrade aggregation-prone huntingtin protein is exhausted.	Sodium Dodecyl Sulfate	97-100	huntingtin	Homo sapiens	249-259
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
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
11285271-6	2001	In the cells expressing the mutant truncated huntingtin construct, numerous SDS-resistant aggregates were present in the cytoplasm and nucleus.	Sodium Dodecyl Sulfate	76-79	huntingtin	Homo sapiens	45-55
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
11035034-1	2001	Huntington"s disease is caused by an expanded CAG trinucleotide repeat coding for a polyglutamine stretch within the huntingtin protein.	trinucleotide	50-63	huntingtin	Homo sapiens	117-127
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
11172033-0	2001	The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington"s disease pathogenesis.	glutaminylalanine	4-11	huntingtin	Homo sapiens	66-76
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
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
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
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
11092755-0	2000	Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles.	Iron	15-19	huntingtin	Homo sapiens	0-10
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
11092755-4	2000	Moreover, upmodulation by deferoxamine mesylate implicates huntingtin as an iron-response protein.	Deferoxamine	26-47	huntingtin	Homo sapiens	59-69
11092755-3	2000	Although the majority did not differ, dramatic changes in six classes revealed that huntingtin"s function is essential for the normal nuclear (nucleoli, transcription factor-speckles) and perinuclear membrane (mitochondria, endoplasmic reticulum, Golgi and recycling endosomes) organelles and for proper regulation of the iron pathway.	Iron	322-326	huntingtin	Homo sapiens	84-94
11092755-4	2000	Moreover, upmodulation by deferoxamine mesylate implicates huntingtin as an iron-response protein.	Iron	76-80	huntingtin	Homo sapiens	59-69
10801775-0	2000	Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin.	polyglutamine	50-63	huntingtin	Homo sapiens	73-83
11092755-6	2000	Thus, organelles that require huntingtin to function suggest roles for the protein in RNA biogenesis, trafficking and iron homeostasis to be explored in HD pathogenesis.	Iron	118-122	huntingtin	Homo sapiens	30-40
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
10958656-5	2000	Glutathione S:-transferase partner "pull-down" assays reveal soluble, aberrantly migrating, forms of full-length mutant huntingtin specific to HD target tissue.	Glutathione	0-11	huntingtin	Homo sapiens	120-130
10970063-1	2000	Huntington"s disease is a progressive and fatal neurological disorder caused by the expansion of a CAG trinucleotide repeat in exon 1 of the gene coding for a protein of unknown function that has been named huntingtin.	trinucleotide	103-116	huntingtin	Homo sapiens	207-217
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
11013077-1	2000	Huntington"s disease (HD) is associated with a significant expansion of a CAG trinucleotide repeat, which results in a lengthened polyglutamine tract in the single gene product, huntingtin, on human 4p16.3.	trinucleotide	78-91	huntingtin	Homo sapiens	178-188
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
10991985-2	2000	A series of AS oligodeoxynucleotides (ODNs) complementary to the huntingtin transcript [i.e., nucleotide (nt) -25 to 35] were designed and synthesized, and the AS efficacy was investigated by using a combination of in vitro transcription and translation to mimic in vivo conditions.	Oligodeoxyribonucleotides	15-36	huntingtin	Homo sapiens	65-75
10991985-2	2000	A series of AS oligodeoxynucleotides (ODNs) complementary to the huntingtin transcript [i.e., nucleotide (nt) -25 to 35] were designed and synthesized, and the AS efficacy was investigated by using a combination of in vitro transcription and translation to mimic in vivo conditions.	Oligodeoxyribonucleotides	38-42	huntingtin	Homo sapiens	65-75
10991985-2	2000	A series of AS oligodeoxynucleotides (ODNs) complementary to the huntingtin transcript [i.e., nucleotide (nt) -25 to 35] were designed and synthesized, and the AS efficacy was investigated by using a combination of in vitro transcription and translation to mimic in vivo conditions.	Nucleotides	52-54	huntingtin	Homo sapiens	65-75
10991985-3	2000	An oligomer directed to nt -1 to 15 (ODN III) markedly reduced the incorporation of [(3)H]leucine into the huntingtin gene product in a dose-dependent manner (ED(50) of approximately 11.5 microM).	Leucine	90-97	huntingtin	Homo sapiens	107-117
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
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.	chrysamine G	209-221	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.	Direct Fast Yellow	227-245	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
11043541-0	2000	12-O-tetradecanoyl-phorbol-13-acetate down-regulates the Huntingtin promoter at Sp1 sites.	Tetradecanoylphorbol Acetate	0-37	huntingtin	Homo sapiens	57-67
10961047-7	2000	The mutation of huntingtin produces an expanded stretch of glutamine (Gln) residues.	Glutamine	59-68	huntingtin	Homo sapiens	16-26
10961047-7	2000	The mutation of huntingtin produces an expanded stretch of glutamine (Gln) residues.	Glutamine	70-73	huntingtin	Homo sapiens	16-26
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.	Oligonucleotides	124-139	huntingtin	Homo sapiens	96-106
10859666-3	2000	We have looked at the nucleotide sequence coding for huntingtin and find that another possibility may exist for the correlation between the occurrence of HD and poly-CAG length.	poly-cag	161-169	huntingtin	Homo sapiens	53-63
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
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
10717003-7	2000	Treatment with heat shock and lactacystin, a proteasome inhibitor, increased the proportion of mutant huntingtin exon 1-expressing cells with inclusions.	lactacystin	30-41	huntingtin	Homo sapiens	102-112
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
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
11285147-1	1999	Biogenic amine transporters, namely the dopamine (DA), norepinephrine (NE) and 5-hydroxytryptamine (serotonin, 5-HT) transporters (DAT, NET and 5-HTT, respectively) appear to be the key elements in regulating biogenic amine neurotransmission.	Amines	9-14	huntingtin	Homo sapiens	146-149
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
10516137-2	1999	Cellular taurine accumulation occurs by an osmotically induced, protein kinase C (PKC)-regulated Na(+)-taurine cotransporter (hTT).	Taurine	9-16	huntingtin	Homo sapiens	126-129
10516137-4	1999	In low AR-expressing cells, 20 mM glucose decreased taurine content, hTT transporter activity, and mRNA levels, and these effects were unaffected by AR inhibition (ARI).	Glucose	34-41	huntingtin	Homo sapiens	69-72
10516137-8	1999	In these cells exposed to 5 mM glucose, hTT mRNA abundance was decreased and declined further in 20 mM glucose but was corrected by ARI.	Glucose	31-38	huntingtin	Homo sapiens	40-43
10516137-5	1999	In these cells, the inhibitory effects of high glucose on hTT appeared to be posttranscriptionally mediated, because 20 mM glucose decreased hTT mRNA stability without affecting hTT transcriptional rate.	Glucose	47-54	huntingtin	Homo sapiens	58-61
10516137-8	1999	In these cells exposed to 5 mM glucose, hTT mRNA abundance was decreased and declined further in 20 mM glucose but was corrected by ARI.	Glucose	103-110	huntingtin	Homo sapiens	40-43
10516137-9	1999	In 5 mM glucose, hTT transcriptional rate was markedly decreased in high AR-expressing cells, did not decline further in 20 mM glucose, but was increased by ARI to levels above those observed in low AR-expressing cells.	Glucose	8-15	huntingtin	Homo sapiens	17-20
10516137-5	1999	In these cells, the inhibitory effects of high glucose on hTT appeared to be posttranscriptionally mediated, because 20 mM glucose decreased hTT mRNA stability without affecting hTT transcriptional rate.	Glucose	47-54	huntingtin	Homo sapiens	141-144
10516137-9	1999	In 5 mM glucose, hTT transcriptional rate was markedly decreased in high AR-expressing cells, did not decline further in 20 mM glucose, but was increased by ARI to levels above those observed in low AR-expressing cells.	Glucose	127-134	huntingtin	Homo sapiens	17-20
10516137-5	1999	In these cells, the inhibitory effects of high glucose on hTT appeared to be posttranscriptionally mediated, because 20 mM glucose decreased hTT mRNA stability without affecting hTT transcriptional rate.	Glucose	47-54	huntingtin	Homo sapiens	141-144
10516137-10	1999	Therefore, glucose rapidly and specifically decreases taurine content, hTT activity, and mRNA abundance by AR-unrelated and AR-related posttranscriptional and transcriptional mechanisms.	Glucose	11-18	huntingtin	Homo sapiens	71-74
10516137-5	1999	In these cells, the inhibitory effects of high glucose on hTT appeared to be posttranscriptionally mediated, because 20 mM glucose decreased hTT mRNA stability without affecting hTT transcriptional rate.	Glucose	123-130	huntingtin	Homo sapiens	58-61
10516137-5	1999	In these cells, the inhibitory effects of high glucose on hTT appeared to be posttranscriptionally mediated, because 20 mM glucose decreased hTT mRNA stability without affecting hTT transcriptional rate.	Glucose	123-130	huntingtin	Homo sapiens	141-144
10516137-5	1999	In these cells, the inhibitory effects of high glucose on hTT appeared to be posttranscriptionally mediated, because 20 mM glucose decreased hTT mRNA stability without affecting hTT transcriptional rate.	Glucose	123-130	huntingtin	Homo sapiens	141-144
10516137-6	1999	Inhibition of PKC overcame the decrease in hTT activity in high glucose-exposed cells.	Glucose	64-71	huntingtin	Homo sapiens	43-46
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
10502848-6	1999	We evaluated a polymerase chain reaction (PCR) technique for the detection of CAG trinucleotide repeats in the Huntington IT15 gene on chromosome 4 for the diagnosis of HD.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	78-81	huntingtin	Homo sapiens	122-126
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
10471702-3	1999	Sla1C and several other Sup35N-interacting proteins also exhibit two-hybrid interactions with the poly-Gln-expanded N-proximal fragment of human huntingtin, which promotes Huntington disease-associated aggregation.	poly-gln	98-106	huntingtin	Homo sapiens	145-155
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
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
10502848-6	1999	We evaluated a polymerase chain reaction (PCR) technique for the detection of CAG trinucleotide repeats in the Huntington IT15 gene on chromosome 4 for the diagnosis of HD.	trinucleotide	82-95	huntingtin	Homo sapiens	122-126
10502848-11	1999	RESULTS: We successfully identified four subjects with expansion of CAG trinucleotide repeats in Huntington gene IT15 on chromosome 4.	trinucleotide	72-85	huntingtin	Homo sapiens	113-117
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
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
10381332-1	1999	In a study of a group of elderly athletes we observed an unexpected association between serum cholesterol levels and the HTTLPR insertion/deletion polymorphism of the promoter region of the serotonin transporter gene (HTT, SLC6A4).	Cholesterol	94-105	huntingtin	Homo sapiens	121-124
10381332-9	1999	While these studies are preliminary and exploratory, they are consistent with a relationship of the HTT gene in cholesterol levels and a risk for heart disease.	Cholesterol	112-123	huntingtin	Homo sapiens	100-103
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
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
10023115-2	1999	The genetic defect is a CAG trinucleotide repeat expansion at the 5" end of the IT 15 gene on chromosome 4.	trinucleotide	28-41	huntingtin	Homo sapiens	80-85
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
10377424-4	1999	More TGase-catalyzed aggregates formed when the polyglutamine domain of htt exceeded the pathologic threshold of polyQ36.	polyq36	113-120	huntingtin	Homo sapiens	72-75
10350633-5	1999	Subcellular fractionation and sucrose density centrifugation of rabbit brain extract showed that most of the huntingtin exists as a high molecular weight complex in the cytoplasm.	Sucrose	30-37	huntingtin	Homo sapiens	109-119
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.	trinucleotides	171-185	huntingtin	Homo sapiens	10-14
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
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
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
9932964-2	1999	The expanded IT-15 allele was only detected with the use of modified PCR and Southern transfer techniques, which showed a CAG trinucleotide repeat expansion of approximately 250 repeats-the largest CAG expansion reported within the huntingtin gene.	trinucleotide	126-139	huntingtin	Homo sapiens	232-242
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).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	66-69	huntingtin	Homo sapiens	94-104
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	80-83	huntingtin	Homo sapiens	47-57
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
10222786-2	1999	An unstable CAG trinucleotide repeat expansion within the first exon of the responsible gene "IT15", encoding huntingtin, was identified.	trinucleotide	16-29	huntingtin	Homo sapiens	110-120
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
10090478-1	1999	Huntington disease (HD) is an autosomal dominant neurodegenerative disorder associated with expansions of an unstable CAG trinucleotide repeat in exon 1 of the IT15 gene.	trinucleotide	122-135	huntingtin	Homo sapiens	160-164
10362304-0	1999	Forskolin and dopamine D1 receptor activation increase huntingtin"s association with endosomes in immortalized neuronal cells of striatal origin.	Colforsin	0-9	huntingtin	Homo sapiens	55-65
10362304-5	1999	When these neurons were differentiated by treatment with forskolin, huntingtin redistributed to perinuclear regions, discrete puncta along plasma membranes, and branch points and terminal growth cones in neurites.	Colforsin	57-66	huntingtin	Homo sapiens	68-78
10362304-8	1999	Dopamine treatment altered the subcellular localization of huntingtin and increased its expression in clathrin-enriched membrane fractions.	Dopamine	0-8	huntingtin	Homo sapiens	59-69
10362304-10	1999	Results suggest that the transport of huntingtin and its co-expression in clathrin and huntingtin-interacting protein 1-enriched membranes is influenced by activation of adenylyl cyclase and stimulation of dopamine D1 receptors.	Dopamine	206-214	huntingtin	Homo sapiens	38-48
9768849-0	1998	Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons.	polyglutamine	0-13	huntingtin	Homo sapiens	29-39
9792871-2	1998	The disease is associated with a CAG trinucleotide-repeat expansion in the Huntington gene (IT15) on chromosome 4p16.3.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	92-96
9792871-2	1998	The disease is associated with a CAG trinucleotide-repeat expansion in the Huntington gene (IT15) on chromosome 4p16.3.	trinucleotide	37-50	huntingtin	Homo sapiens	92-96
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
9700202-6	1998	This interaction is mediated by huntingtin"s proline-rich region and is enhanced by lengthening the adjacent glutamine tract.	Proline	45-52	huntingtin	Homo sapiens	32-42
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
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.	trinucleotide	26-39	huntingtin	Homo sapiens	155-165
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
9768849-5	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
9768849-6	1998	As in human neurons, polyglutamine-expanded huntingtin induced neuronal degeneration.	polyglutamine	21-34	huntingtin	Homo sapiens	44-54
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
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
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
9647305-1	1998	OBJECTIVES: To evaluate possible influences of CCG and delta2642 glutamic acid polymorphisms adjacent to the (CAG)n trinucleotide repeat in Huntington"s disease gene IT15 on some clinical features (age and symptoms) at onset.	n trinucleotide	114-129	huntingtin	Homo sapiens	166-170
29508777-1	1998	It has been identified that the expansion of normally polymorphic CTG repeats in myotonin protein kinase (DM-PK) gene in myotonic dystrophy (DM) and CAG repeats in huntingtin gene in Huntington"s disease (HD) acts as the causative mutation.	ctg	66-69	huntingtin	Homo sapiens	164-174
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.	trinucleotide	55-68	huntingtin	Homo sapiens	146-156
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
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
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
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
9466992-2	1998	We detected an interaction with cystathionine beta-synthase (CBS) [L-serine hydrolyase (adding homocysteine), EC 4.2.1.22], which was confirmed in vitro using His-tagged CBS expressed in Escherichia coli , which was able to specifically bind both rat and human full-length huntingtin.	Serine	69-75	huntingtin	Homo sapiens	273-283
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
9536081-1	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
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
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
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
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
9466992-2	1998	We detected an interaction with cystathionine beta-synthase (CBS) [L-serine hydrolyase (adding homocysteine), EC 4.2.1.22], which was confirmed in vitro using His-tagged CBS expressed in Escherichia coli , which was able to specifically bind both rat and human full-length huntingtin.	Homocysteine	95-107	huntingtin	Homo sapiens	273-283
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
9660943-4	1998	As a result, huntingtin with expanded polyglutamine is preferentially incorporated into polymers.	Polymers	88-96	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
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
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
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
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.	trinucleotide	75-88	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.	trinucleotide	75-88	huntingtin	Homo sapiens	190-200
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
9299885-1	1997	The defect causing Huntington"s disease (HD) has recently been discovered as an expanded CAG trinucleotide repeat located at the 5" end of the IT15 gene.	trinucleotide	93-106	huntingtin	Homo sapiens	143-147
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
9322235-3	1997	SRIs block the reuptake of serotonin (5-HT) into the presynaptic neuron, a process mediated by the serotonin transporter (5-HTT).	Serotonin	27-36	huntingtin	Homo sapiens	124-127
9303588-4	1997	Gene IT15 analysis revealed an abnormal expansion of (CAG) trinucleotide repeats in 18 subjects, being normal in the remaining 18.	trinucleotide	59-72	huntingtin	Homo sapiens	5-9
9211185-2	1997	The mutation is an expansion of a CAG trinucleotide repeat, which translates to give a polyglutamine tract at the N-terminus of a large protein, huntingtin.	trinucleotide	38-51	huntingtin	Homo sapiens	145-155
11669756-2	1997	The reaction of cis-[MCl(2)(dppm)] (M = Pt(II) and Pd(II); dppm = bis(diphenylphosphino)methane) with H(2)TT and NaOH (H(2)TT = 8-thiotheophylline) yields neutral mononuclear [M(HTT-S(8))(2)(dppm)] complexes.	phospholyl(diphenylphosphino)methane	28-32	huntingtin	Homo sapiens	178-181
11669756-5	1997	Heterodinuclear [(dppm)Pt(&mgr;-TT)(2)Pd(L-L)] complexes are obtained by reaction of [Pt(HTT)(2)(dppm)] with [PdCl(2)(L-L)] in basic medium (L-L = dppm and 2,2"-bipyridine).	phospholyl(diphenylphosphino)methane	18-22	huntingtin	Homo sapiens	93-96
9143014-1	1997	We correlated trinucleotide CAG repeat numbers in the huntingtin gene with the regional brain atrophy and clinical phenotype in 23 adult autopsy cases of Huntington"s disease (HD).	trinucleotide	14-27	huntingtin	Homo sapiens	54-64
9079622-1	1997	Based on the presence of multiple proline-rich motifs in the huntingtin sequence, we tested its possible association with epidermal growth factor (EGF) receptor signaling complexes through SH3 domain-containing modules.	Proline	34-41	huntingtin	Homo sapiens	61-71
9079622-2	1997	We found that huntingtin is associated with Grb2, RasGAP, and tyrosine-phosphorylated EGF receptor.	Tyrosine	62-70	huntingtin	Homo sapiens	14-24
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
9126163-2	1997	We have attempted to reduce the expression in vivo of the Huntington"s disease gene protein, Huntingtin, using an 18-mer fluorescein-labeled phosphorothiorated antisense oligodeoxynucleotide (ODN) targeted against the start site of the first exon of the IT15 gene.	Fluorescein	121-132	huntingtin	Homo sapiens	93-103
9126163-2	1997	We have attempted to reduce the expression in vivo of the Huntington"s disease gene protein, Huntingtin, using an 18-mer fluorescein-labeled phosphorothiorated antisense oligodeoxynucleotide (ODN) targeted against the start site of the first exon of the IT15 gene.	Fluorescein	121-132	huntingtin	Homo sapiens	254-258
9126163-2	1997	We have attempted to reduce the expression in vivo of the Huntington"s disease gene protein, Huntingtin, using an 18-mer fluorescein-labeled phosphorothiorated antisense oligodeoxynucleotide (ODN) targeted against the start site of the first exon of the IT15 gene.	Oligodeoxyribonucleotides	170-190	huntingtin	Homo sapiens	93-103
9126163-2	1997	We have attempted to reduce the expression in vivo of the Huntington"s disease gene protein, Huntingtin, using an 18-mer fluorescein-labeled phosphorothiorated antisense oligodeoxynucleotide (ODN) targeted against the start site of the first exon of the IT15 gene.	Oligodeoxyribonucleotides	192-195	huntingtin	Homo sapiens	93-103
9126163-2	1997	We have attempted to reduce the expression in vivo of the Huntington"s disease gene protein, Huntingtin, using an 18-mer fluorescein-labeled phosphorothiorated antisense oligodeoxynucleotide (ODN) targeted against the start site of the first exon of the IT15 gene.	Oligodeoxyribonucleotides	192-195	huntingtin	Homo sapiens	254-258
8855141-1	1996	Huntington disease (HD) is a neurodegenerative disorder caused by an expanded trinucleotide repeat (CAG)n located at the 5" end of the novel IT15 gene.	trinucleotide	78-91	huntingtin	Homo sapiens	141-145
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
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
8755937-0	1996	Errors in Huntington disease diagnostic test caused by trinucleotide deletion in the IT15 gene.	trinucleotide	55-68	huntingtin	Homo sapiens	85-89
8858182-4	1996	The confirmation of the complex II inhibitor 3-nitropropionic acid as a toxin model for Huntington"s disease, together with the demonstration of reduced mitochondrial function in Huntington"s disease caudate, supports the proposition that mutant huntingtin may exert its effect through an abnormality of energy metabolism.	3-nitropropionic acid	45-66	huntingtin	Homo sapiens	246-256
8643525-0	1996	Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin.	polyglutamine	13-26	huntingtin	Homo sapiens	37-47
8643525-6	1996	Huntingtin from brain extracts is retained on calmodulin(CAM)-Sepharose in a calcium-dependent fashion.	Sepharose	62-71	huntingtin	Homo sapiens	0-10
8643525-6	1996	Huntingtin from brain extracts is retained on calmodulin(CAM)-Sepharose in a calcium-dependent fashion.	Calcium	77-84	huntingtin	Homo sapiens	0-10
8643525-10	1996	Furthermore, an increased amount of mutant huntingtin from HD patient brains is retained on CAM-Sepharose compared to normal huntingtin from control patient brains, and the mutant allele is preferentially retained on CAM-Sepharose in the absence of calcium.	Sepharose	96-105	huntingtin	Homo sapiens	43-53
8643525-10	1996	Furthermore, an increased amount of mutant huntingtin from HD patient brains is retained on CAM-Sepharose compared to normal huntingtin from control patient brains, and the mutant allele is preferentially retained on CAM-Sepharose in the absence of calcium.	Sepharose	221-230	huntingtin	Homo sapiens	43-53
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
8614526-1	1996	We examined the relationship between length of the trinucleotide (CAG) repeat at IT-15 and clinical progression of Huntington"s disease in 46 mildly to moderately affected patients over a 2-year interval.	trinucleotide	51-64	huntingtin	Homo sapiens	81-86
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
8614526-1	1996	We examined the relationship between length of the trinucleotide (CAG) repeat at IT-15 and clinical progression of Huntington"s disease in 46 mildly to moderately affected patients over a 2-year interval.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	66-69	huntingtin	Homo sapiens	81-86
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
8954302-2	1996	We examined the expanded trinucleotide (CAG) repeat sequence in the IT15 gene of 27 "sporadic" cases, classified as having clinically probable or clinically doubtful HD.	trinucleotide	25-38	huntingtin	Homo sapiens	68-72
8954302-2	1996	We examined the expanded trinucleotide (CAG) repeat sequence in the IT15 gene of 27 "sporadic" cases, classified as having clinically probable or clinically doubtful HD.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	40-43	huntingtin	Homo sapiens	68-72
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
8720339-0	1995	[Chorea with prominent spasticity associated with an expansion of the CAG trinucleotide repeat in the IT15 gene: a case report].	trinucleotide	74-87	huntingtin	Homo sapiens	102-106
7576661-1	1995	A trinucleotide repeat (CAG) expansion in the huntingtin gene causes Huntington"s disease (HD).	trinucleotide	2-15	huntingtin	Homo sapiens	46-56
8697093-2	1995	We describe the molecular diagnosis for 8 HD patients and 39 risky family members in two large HD pedigrees by using G8 RFLP linkage analysis as well as direct detection of the expanded (CAG) repeat in IT15 gene with the nested PCR denaturing polyacrylamide gel electrophoretic autoradiography and direct DNA sequencing.	polyacrylamide	243-257	huntingtin	Homo sapiens	202-206
7662891-2	1995	In this study, we examined IT15 mRNA levels during the quinolinic acid (QA) excitotoxic cascade to determine whether neuronal and/or glial expression is regulated by neurodegeneration.	Quinolinic Acid	72-74	huntingtin	Homo sapiens	27-31
8774958-1	1995	Positional cloning has shown that the Huntington disease (HD) mutation is an expanded trinucleotide repeat in the IT15 gene.	trinucleotide	86-99	huntingtin	Homo sapiens	114-118
7568002-1	1995	The Huntington disease (HD) phenotype is associated with expansion of a trinucleotide repeat in the IT15 gene, which is predicted to encode a 348-kDa protein named huntington.	trinucleotide	72-85	huntingtin	Homo sapiens	100-104
7668287-1	1995	Huntington disease (HD) is an autosomal dominant degenerative disorder caused by an expanded and unstable trinucleotide repeat (CAG)n in a gene (IT-15) on chromosome 4.	trinucleotide	106-119	huntingtin	Homo sapiens	145-150
7484060-6	1995	INTRODUCTION--The discovery of an expansion of a trinucleotide (CAG) repeat region in the IT15 gene on the short arm of chromosome 4 has identified the mutational mechanism causing Huntington"s disease (HD) and enables the direct diagnosis of affected subjects based on DNA analysis alone.	trinucleotide	49-62	huntingtin	Homo sapiens	90-94
7484060-6	1995	INTRODUCTION--The discovery of an expansion of a trinucleotide (CAG) repeat region in the IT15 gene on the short arm of chromosome 4 has identified the mutational mechanism causing Huntington"s disease (HD) and enables the direct diagnosis of affected subjects based on DNA analysis alone.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	64-67	huntingtin	Homo sapiens	90-94
7484060-9	1995	MATERIAL AND METHODS--A labelled polymerase chain reaction (PCR) test has been used to amplify the repeat region of the IT15 gene and DNA fragments were analyzed by Polyacrylamide gel electrophoresis.	polyacrylamide	165-179	huntingtin	Homo sapiens	120-124
7639626-1	1995	OBJECTIVE: To investigate possible correlations between the length of the (CAG)n trinucleotide repeat in Hungtington"s disease gene IT15 and clinical features (age at onset, symptoms at onset, and mode of progression) in Huntington"s disease.	n trinucleotide	79-94	huntingtin	Homo sapiens	132-136
7639626-8	1995	CONCLUSION: Factors that determine the nature of symptoms at onset and the mode of progression of Huntington"s disease seem to be operating independently of the (CAG)n trinucleotide repeat in gene IT15.	n trinucleotide	166-181	huntingtin	Homo sapiens	197-201
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
7581375-6	1995	In order to determine expression of the two alleles of the IT15 protein we used Western blots of 4% polyacrylamide gels.	polyacrylamide	100-114	huntingtin	Homo sapiens	59-63
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
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
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
7853373-1	1994	The genetic defect causing Huntington"s disease (HD) has been identified as an unstable expansion of a trinucleotide (CAG) repeat sequence within the coding region of the IT15 gene on chromosome 4.	trinucleotide	103-116	huntingtin	Homo sapiens	171-175
7847863-3	1995	An expansion of a trinucleotide repeat on chromosome 4p16.3 within the coding region of a gene termed IT15 has been identified as the mutation causing HD.	trinucleotide	18-31	huntingtin	Homo sapiens	102-106
7750074-6	1995	The gene for HD has recently been discovered and characterized as an unstable CAG trinucleotide repeat sequence on the short arm of chromosome 4 (now known as IT15).	trinucleotide	82-95	huntingtin	Homo sapiens	159-163
7711729-1	1995	Huntington"s disease (HD) is an inherited neurodegenerative disorder expressed when a trinucleotide repeat in the gene IT-15 is expanded.	trinucleotide	86-99	huntingtin	Homo sapiens	119-124
7853373-1	1994	The genetic defect causing Huntington"s disease (HD) has been identified as an unstable expansion of a trinucleotide (CAG) repeat sequence within the coding region of the IT15 gene on chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	118-121	huntingtin	Homo sapiens	171-175
8208412-1	1994	The specific mutation in Huntington"s disease (HD) is an expansion of the unstable CAG trinucleotide repeat in the IT15 gene in chromosome 4p.	trinucleotide	87-100	huntingtin	Homo sapiens	115-119
7909529-0	1994	A Sau3A polymorphism in the 5" end of the IT15 gene that nonrandomly segregates with the Huntington disease trinucleotide expansion.	trinucleotide	108-121	huntingtin	Homo sapiens	42-46
8044653-2	1994	Recently the IT15 gene on chromosome 4p has been identified containing an unstable and expanded trinucleotide repeat in patients with HD.	trinucleotide	96-109	huntingtin	Homo sapiens	13-17
8458085-4	1993	A new gene, IT15, isolated using cloned trapped exons from the target area contains a polymorphic trinucleotide repeat that is expanded and unstable on HD chromosomes.	trinucleotide	98-111	huntingtin	Homo sapiens	12-16
7888133-0	1994	Trinucleotide repeat elongation in the huntingtin gene in Huntington"s disease patients from 85 French families.	trinucleotide	0-13	huntingtin	Homo sapiens	39-49
8162020-0	1994	A single allele from the polymorphic CCG rich sequence immediately 3" to the unstable CAG trinucleotide in the IT15 cDNA shows almost complete disequilibrium with Huntington"s disease chromosomes in the Scottish population.	trinucleotide	90-103	huntingtin	Homo sapiens	111-115
8268907-0	1993	Correlation between the onset age of Huntington"s disease and length of the trinucleotide repeat in IT-15.	trinucleotide	76-89	huntingtin	Homo sapiens	100-105
8268927-0	1993	Analysis of the huntingtin gene reveals a trinucleotide-length polymorphism in the region of the gene that contains two CCG-rich stretches and a correlation between decreased age of onset of Huntington"s disease and CAG repeat number.	trinucleotide	42-55	huntingtin	Homo sapiens	16-26
8242074-0	1993	Trinucleotide repeat elongation in the Huntingtin gene in Huntington disease patients from 71 Danish families.	trinucleotide	0-13	huntingtin	Homo sapiens	39-49
8411732-6	1993	IT 15 contains a polymorphic trinucleotide repeat that is expanded and unstable on HD chromosomes.	trinucleotide	29-42	huntingtin	Homo sapiens	0-5
8366869-1	1993	The Huntington"s Disease (HD) Collaborative Research Group has recently published the sequence of a new cDNA, IT15, containing a polymorphic trinucleotide (CAG)n repeat that is expanded and unstable on HD chromosomes.	trinucleotide	141-154	huntingtin	Homo sapiens	110-114
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
33809220-0	2021	The Novel Alpha-2 Adrenoceptor Inhibitor Beditin Reduces Cytotoxicity and Huntingtin Aggregates in Cell Models of Huntington"s Disease.	beditin	41-48	huntingtin	Homo sapiens	74-84
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
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
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
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.	trinucleotide	40-53	huntingtin	Homo sapiens	80-90
32796930-7	2020	Therapeutically, the first human trial of an HTT-lowering antisense oligonucleotide successfully, and safely, reduced the CSF concentration of mHTT in individuals with HD.	Oligonucleotides	68-83	huntingtin	Homo sapiens	45-48
32796930-7	2020	Therapeutically, the first human trial of an HTT-lowering antisense oligonucleotide successfully, and safely, reduced the CSF concentration of mHTT in individuals with HD.	mhtt	143-147	huntingtin	Homo sapiens	45-48
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.	trinucleotide	40-53	huntingtin	Homo sapiens	161-171
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
25558393-1	2014	We have shown that the expression of full-length mutated huntingtin in human neuroblastoma cells (SK-N-SH) leads to an abnormal increase in calcium entry through store-operated channels.	Calcium	140-147	huntingtin	Homo sapiens	57-67
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
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
19515365-10	2009	Three pairs of primers were used for the amplification of the IT15 gene at the: 1) trinucleotide expansion site; 2) trinucleotide expansion site plus the polymorphic site situated on its 3"-end; and 3) polymorphic marker located downstream of the trinucleotide repeats.	trinucleotide	83-96	huntingtin	Homo sapiens	62-66
19515365-10	2009	Three pairs of primers were used for the amplification of the IT15 gene at the: 1) trinucleotide expansion site; 2) trinucleotide expansion site plus the polymorphic site situated on its 3"-end; and 3) polymorphic marker located downstream of the trinucleotide repeats.	trinucleotide	116-129	huntingtin	Homo sapiens	62-66
19515365-10	2009	Three pairs of primers were used for the amplification of the IT15 gene at the: 1) trinucleotide expansion site; 2) trinucleotide expansion site plus the polymorphic site situated on its 3"-end; and 3) polymorphic marker located downstream of the trinucleotide repeats.	trinucleotide	116-129	huntingtin	Homo sapiens	62-66
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
34741261-0	2022	Inhibition of HIPK3 by AST487 Ameliorates Mutant HTT-Induced Neurotoxicity and Apoptosis via Enhanced Autophagy.	AST 487	23-29	huntingtin	Homo sapiens	49-52
34942093-1	2022	It is well known that the length of the CAG trinucleotide expansion of the huntingtin gene is associated with many aspects of Huntington disease progression.	trinucleotide	44-57	huntingtin	Homo sapiens	75-85
34918046-2	2021	Since mutant huntingtin (mHTT) protein is the root cause of Huntington"s disease, oligonucleotide-based therapeutic approaches using small interfering RNAs (siRNAs) and antisense oligonucleotides designed to specifically silence mHTT may be novel therapeutic strategies for Huntington"s disease.	Oligonucleotides	82-97	huntingtin	Homo sapiens	13-23
34918046-2	2021	Since mutant huntingtin (mHTT) protein is the root cause of Huntington"s disease, oligonucleotide-based therapeutic approaches using small interfering RNAs (siRNAs) and antisense oligonucleotides designed to specifically silence mHTT may be novel therapeutic strategies for Huntington"s disease.	Oligonucleotides	179-195	huntingtin	Homo sapiens	13-23
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
34911927-1	2021	Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the huntingtin (HTT) gene.	cytosine-adenine-guanine	92-116	huntingtin	Homo sapiens	152-162
34911927-1	2021	Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the huntingtin (HTT) gene.	cytosine-adenine-guanine	92-116	huntingtin	Homo sapiens	164-167
34911927-1	2021	Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	118-121	huntingtin	Homo sapiens	152-162
34911927-1	2021	Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	118-121	huntingtin	Homo sapiens	164-167
34911927-1	2021	Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the huntingtin (HTT) gene.	trinucleotide	123-136	huntingtin	Homo sapiens	152-162
34911927-1	2021	Huntington"s disease (HD) is a hereditary neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats in the huntingtin (HTT) gene.	trinucleotide	123-136	huntingtin	Homo sapiens	164-167
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
34958078-4	2021	Submilligram production of FL HTT in mammalian cells was achieved using doxycycline-inducible stable cell line expression.	Doxycycline	72-83	huntingtin	Homo sapiens	30-33
34958078-6	2021	This paper presents a robust method for low-milligram quantity production of FL HTT and its variants from codon-optimized plasmids by transient transfection using polyethylenimine (PEI).	Polyethyleneimine	163-179	huntingtin	Homo sapiens	80-83
34958078-6	2021	This paper presents a robust method for low-milligram quantity production of FL HTT and its variants from codon-optimized plasmids by transient transfection using polyethylenimine (PEI).	Polyethyleneimine	181-184	huntingtin	Homo sapiens	80-83
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
34888656-7	2022	Using a combination of in vitro methylation and cell-based experiments we identified PRMT4 (CARM1) and PRMT6 as major enzymes methylating HTT at specific arginines.	Arginine	154-163	huntingtin	Homo sapiens	138-141
34888656-11	2022	Thus, arginine methylation pathways that involve specific HTT-modifying PRMT enzymes and modulate HTT biochemical and toxic properties could provide targets for HD-modifying therapies.	Arginine	6-14	huntingtin	Homo sapiens	58-61
34888656-11	2022	Thus, arginine methylation pathways that involve specific HTT-modifying PRMT enzymes and modulate HTT biochemical and toxic properties could provide targets for HD-modifying therapies.	Arginine	6-14	huntingtin	Homo sapiens	98-101
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
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
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
34959389-0	2021	Posiphen Reduces the Levels of Huntingtin Protein through Translation Suppression.	phenserine	0-8	huntingtin	Homo sapiens	31-41
34924935-0	2021	Synthesis and Evaluation of a Fluorine-18 Radioligand for Imaging Huntingtin Aggregates by Positron Emission Tomographic Imaging.	Fluorine	30-38	huntingtin	Homo sapiens	66-76
34959389-11	2021	Unchanged mRNA levels of HTT and a comparable decay rate of HTT proteins after Posiphen treatment supported the coclusion that Posiphen reduced HTT via downregulation of the translation of HTT mRNA.	phenserine	127-135	huntingtin	Homo sapiens	144-147
34959389-11	2021	Unchanged mRNA levels of HTT and a comparable decay rate of HTT proteins after Posiphen treatment supported the coclusion that Posiphen reduced HTT via downregulation of the translation of HTT mRNA.	phenserine	127-135	huntingtin	Homo sapiens	189-192
34959389-13	2021	The mRNAs encoding HTT, APP and alphaSYN contain an atypical iron response element (IRE) in their 5"-untranslated regions (5"-UTRs) that bind iron regulatory protein 1 (IRP1), and Posiphen specifically bound this complex.	Iron	61-65	huntingtin	Homo sapiens	19-22
34959389-15	2021	Taken together, Posiphen shows high affinity binding to the IRE/IRP1 complex of mRNAs with an atypical IRE stem loop, inducing their translation suppression, including the mRNAs of neurotoxic proteins APP, alphaSYN and HTT.	phenserine	16-24	huntingtin	Homo sapiens	219-222
34786953-6	2021	Genetic testing revealed a 47 CAG trinucleotide repeats in the Huntingtin gene; family history is negative.	trinucleotide	34-47	huntingtin	Homo sapiens	63-73
34793942-0	2021	Modified cyclodextrin-based nanoparticles mediated delivery of siRNA for Huntingtin gene silencing across an in vitro BBB model.	Cyclodextrins	9-21	huntingtin	Homo sapiens	73-83
34793942-6	2021	Here, we described a novel delivery system based on modified cyclodextrin nanoparticles (CDs) loaded with small interfering RNAs (siRNAs) targeting HTT andcomplexed with the rabies virus glycoprotein(RVG), a BBB-shuttle peptide.	Cyclodextrins	61-73	huntingtin	Homo sapiens	148-151
34793942-6	2021	Here, we described a novel delivery system based on modified cyclodextrin nanoparticles (CDs) loaded with small interfering RNAs (siRNAs) targeting HTT andcomplexed with the rabies virus glycoprotein(RVG), a BBB-shuttle peptide.	cds	89-92	huntingtin	Homo sapiens	148-151
34732320-0	2021	N-alpha-acetylation of Huntingtin protein increases its propensity to aggregate.	n-alpha	0-7	huntingtin	Homo sapiens	23-33
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
34732320-7	2021	These studies represent the first link between N-terminal acetylation and the promotion of a neurodegenerative disease, and implicates NatA-mediated Htt acetylation as a new potential therapeutic target in HD.	N-acetyltryptophanamide	135-139	huntingtin	Homo sapiens	149-152
34899193-4	2021	Huntingtin lowering strategies mostly focus on nucleic acid approaches, such as small interfering RNAs (siRNAs) and antisense oligonucleotides (ASOs).	Oligonucleotides	126-142	huntingtin	Homo sapiens	0-10
34520257-0	2021	Oligonucleotides Targeting DNA Repeats Downregulate Huntingtin Gene Expression in Huntington"s Patient-Derived Neural Model System.	Oligonucleotides	0-16	huntingtin	Homo sapiens	52-62
34520257-3	2021	HD is caused by a CAG CTG trinucleotide-repeat expansion in exon 1 of the huntingtin (HTT) gene leading to the formation of mutant HTT (mtHTT) protein aggregates.	ctg	22-25	huntingtin	Homo sapiens	74-84
34520257-3	2021	HD is caused by a CAG CTG trinucleotide-repeat expansion in exon 1 of the huntingtin (HTT) gene leading to the formation of mutant HTT (mtHTT) protein aggregates.	ctg	22-25	huntingtin	Homo sapiens	86-89
34520257-3	2021	HD is caused by a CAG CTG trinucleotide-repeat expansion in exon 1 of the huntingtin (HTT) gene leading to the formation of mutant HTT (mtHTT) protein aggregates.	ctg	22-25	huntingtin	Homo sapiens	131-134
34520257-3	2021	HD is caused by a CAG CTG trinucleotide-repeat expansion in exon 1 of the huntingtin (HTT) gene leading to the formation of mutant HTT (mtHTT) protein aggregates.	trinucleotide	26-39	huntingtin	Homo sapiens	74-84
34520257-3	2021	HD is caused by a CAG CTG trinucleotide-repeat expansion in exon 1 of the huntingtin (HTT) gene leading to the formation of mutant HTT (mtHTT) protein aggregates.	trinucleotide	26-39	huntingtin	Homo sapiens	86-89
34520257-3	2021	HD is caused by a CAG CTG trinucleotide-repeat expansion in exon 1 of the huntingtin (HTT) gene leading to the formation of mutant HTT (mtHTT) protein aggregates.	trinucleotide	26-39	huntingtin	Homo sapiens	131-134
34520257-6	2021	Previously, we designed a novel anti-gene oligonucleotide (AGO)-based strategy directly targeting the HTT trinucleotide-repeats in DNA and reported downregulation of mRNA and protein in HD patient fibroblasts.	Oligonucleotides	42-57	huntingtin	Homo sapiens	102-105
34520257-6	2021	Previously, we designed a novel anti-gene oligonucleotide (AGO)-based strategy directly targeting the HTT trinucleotide-repeats in DNA and reported downregulation of mRNA and protein in HD patient fibroblasts.	trinucleotide	106-119	huntingtin	Homo sapiens	102-105
34884576-1	2021	Visual deficit is one of the complications of Huntington disease (HD), a fatal neurological disorder caused by CAG trinucleotide expansions in the Huntingtin gene, leading to the production of mutant Huntingtin (mHTT) protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	111-114	huntingtin	Homo sapiens	147-157
34884576-1	2021	Visual deficit is one of the complications of Huntington disease (HD), a fatal neurological disorder caused by CAG trinucleotide expansions in the Huntingtin gene, leading to the production of mutant Huntingtin (mHTT) protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	111-114	huntingtin	Homo sapiens	200-210
34888656-0	2022	Interaction of huntingtin (HTT) with PRMTs and its subsequent arginine methylation affects HTT solubility, phase transition behavior and neuronal toxicity.	Arginine	62-70	huntingtin	Homo sapiens	15-25
34884576-1	2021	Visual deficit is one of the complications of Huntington disease (HD), a fatal neurological disorder caused by CAG trinucleotide expansions in the Huntingtin gene, leading to the production of mutant Huntingtin (mHTT) protein.	trinucleotide	115-128	huntingtin	Homo sapiens	147-157
34888656-0	2022	Interaction of huntingtin (HTT) with PRMTs and its subsequent arginine methylation affects HTT solubility, phase transition behavior and neuronal toxicity.	Arginine	62-70	huntingtin	Homo sapiens	27-30
34888656-0	2022	Interaction of huntingtin (HTT) with PRMTs and its subsequent arginine methylation affects HTT solubility, phase transition behavior and neuronal toxicity.	Arginine	62-70	huntingtin	Homo sapiens	91-94
34884576-1	2021	Visual deficit is one of the complications of Huntington disease (HD), a fatal neurological disorder caused by CAG trinucleotide expansions in the Huntingtin gene, leading to the production of mutant Huntingtin (mHTT) protein.	trinucleotide	115-128	huntingtin	Homo sapiens	200-210
34888656-3	2022	Arginine methylation/dimethylation is an important modification with an emerging role in neurodegeneration, however arginine methylation of HTT remains largely unexplored.	Arginine	116-124	huntingtin	Homo sapiens	140-143
34888656-4	2022	Here we report nearly two dozen novel arginine methylation/dimethylation sites on the endogenous HTT from human and mouse brain and human cells suggested by mass spectrometry with data-dependent acquisition (DDA).	Arginine	38-46	huntingtin	Homo sapiens	97-100
34830381-1	2021	Huntington"s disease (HD) is a rare neurodegenerative disorder caused by an expansion of CAG trinucleotide repeat located in the exon 1 of Huntingtin (HTT) gene in human chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	89-92	huntingtin	Homo sapiens	139-149
34830381-1	2021	Huntington"s disease (HD) is a rare neurodegenerative disorder caused by an expansion of CAG trinucleotide repeat located in the exon 1 of Huntingtin (HTT) gene in human chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	89-92	huntingtin	Homo sapiens	151-154
34830381-1	2021	Huntington"s disease (HD) is a rare neurodegenerative disorder caused by an expansion of CAG trinucleotide repeat located in the exon 1 of Huntingtin (HTT) gene in human chromosome 4.	trinucleotide	93-106	huntingtin	Homo sapiens	139-149
34830381-1	2021	Huntington"s disease (HD) is a rare neurodegenerative disorder caused by an expansion of CAG trinucleotide repeat located in the exon 1 of Huntingtin (HTT) gene in human chromosome 4.	trinucleotide	93-106	huntingtin	Homo sapiens	151-154
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
34600937-8	2021	Treatment with YM-1 reduced N-terminal huntingtin clustering and nuclear aggregation.	N-(3-pyridylmethyl)adriamycin	15-19	huntingtin	Homo sapiens	39-49
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
34087615-11	2021	The Pearson coefficient (95% confidence interval) was 0.10 (-0.53-0.66) between cTT and hTT (n = 11) and 0.93 (0.74-0.98) between uTT and hTT.	UTT	130-133	huntingtin	Homo sapiens	138-141
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
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
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
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
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
34831058-2	2021	One of these diseases is Huntington"s, which is caused by increased glutamine-encoding trinucleotide repeats within the Huntingtin gene.	trinucleotide	87-100	huntingtin	Homo sapiens	120-130
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
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
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
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
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
34089719-5	2021	Mitochondrial lipids, cardiolipin (CL) in particular, are essential in mitochondria function and have the potential to directly interact with htt, altering its aggregation.	Cardiolipins	22-33	huntingtin	Homo sapiens	142-145
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
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
34246856-11	2021	In contrast, the addition of crowders enhanced deposition of htt aggregates onto supported total brain lipid extract (TBLE) bilayers.	lipid extract	103-116	huntingtin	Homo sapiens	61-64
34246856-11	2021	In contrast, the addition of crowders enhanced deposition of htt aggregates onto supported total brain lipid extract (TBLE) bilayers.	tble	118-122	huntingtin	Homo sapiens	61-64
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
34658796-7	2021	Lowering total HTT using HTT-targeted anti-sense oligonucleotides partially restored gene expression, as well as subtly reducing mislocalization of proteins involved in nucleocytoplasmic transport.	Oligonucleotides	49-65	huntingtin	Homo sapiens	15-18
34658796-7	2021	Lowering total HTT using HTT-targeted anti-sense oligonucleotides partially restored gene expression, as well as subtly reducing mislocalization of proteins involved in nucleocytoplasmic transport.	Oligonucleotides	49-65	huntingtin	Homo sapiens	25-28
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
34594185-7	2021	There is evidence for EGCG"s ability to inhibit the aggregation of alpha-synuclein, amyloid-beta, and huntingtin proteins, respectively associated with PD, AD, and HD.	epigallocatechin gallate	22-26	huntingtin	Homo sapiens	102-112
34504195-1	2021	Huntington"s disease (HD) is caused by a CAG trinucleotide repeat expansion in the first exon of the huntingtin (HTT) gene coding for the huntingtin (HTT) protein.	trinucleotide	45-58	huntingtin	Homo sapiens	101-111
34504195-1	2021	Huntington"s disease (HD) is caused by a CAG trinucleotide repeat expansion in the first exon of the huntingtin (HTT) gene coding for the huntingtin (HTT) protein.	trinucleotide	45-58	huntingtin	Homo sapiens	113-116
34504195-1	2021	Huntington"s disease (HD) is caused by a CAG trinucleotide repeat expansion in the first exon of the huntingtin (HTT) gene coding for the huntingtin (HTT) protein.	trinucleotide	45-58	huntingtin	Homo sapiens	138-148
34504195-1	2021	Huntington"s disease (HD) is caused by a CAG trinucleotide repeat expansion in the first exon of the huntingtin (HTT) gene coding for the huntingtin (HTT) protein.	trinucleotide	45-58	huntingtin	Homo sapiens	150-153
34098113-1	2021	Huntington"s disease (HD) is an autosomal neurodegenerative disorder caused by extended trinucleotide CAG repetition in the HTT gene.	trinucleotide	88-101	huntingtin	Homo sapiens	124-127
34445734-4	2021	The huntingtin models consist of a wild-type structure, one mutant with 45 glutamine residues and the second mutant with nine additional key-point mutations from glutamine residues into proline residues (9P(EM) model).	Proline	186-193	huntingtin	Homo sapiens	4-14
34319089-2	2021	Herein, we unexpectedly found that hepta-histidine (7H), an inhibitor of the interaction between Ku70 and Huntingtin proteins, suppresses aggregation of Tau-R3 peptides in vitro.	hepta-histidine	35-50	huntingtin	Homo sapiens	106-116
34319089-2	2021	Herein, we unexpectedly found that hepta-histidine (7H), an inhibitor of the interaction between Ku70 and Huntingtin proteins, suppresses aggregation of Tau-R3 peptides in vitro.	7,8-diacetoxy-3-(4-nitrophenyl)coumarin	52-54	huntingtin	Homo sapiens	106-116
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
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
34445734-1	2021	Mutant huntingtin (m-HTT) proteins and calmodulin (CaM) co-localize in the cerebral cortex with significant effects on the intracellular calcium levels by altering the specific calcium-mediated signals.	Calcium	137-144	huntingtin	Homo sapiens	7-17
34445734-1	2021	Mutant huntingtin (m-HTT) proteins and calmodulin (CaM) co-localize in the cerebral cortex with significant effects on the intracellular calcium levels by altering the specific calcium-mediated signals.	Calcium	137-144	huntingtin	Homo sapiens	21-24
34445734-1	2021	Mutant huntingtin (m-HTT) proteins and calmodulin (CaM) co-localize in the cerebral cortex with significant effects on the intracellular calcium levels by altering the specific calcium-mediated signals.	Calcium	177-184	huntingtin	Homo sapiens	7-17
34445734-1	2021	Mutant huntingtin (m-HTT) proteins and calmodulin (CaM) co-localize in the cerebral cortex with significant effects on the intracellular calcium levels by altering the specific calcium-mediated signals.	Calcium	177-184	huntingtin	Homo sapiens	21-24
34423068-1	2021	Huntington disease (HD) is caused by a pathologic cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the HTT gene.	cytosine-adenine-guanine (cag	50-79	huntingtin	Homo sapiens	119-122
34423068-1	2021	Huntington disease (HD) is caused by a pathologic cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the HTT gene.	trinucleotide	81-94	huntingtin	Homo sapiens	119-122
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	162-165
34200421-0	2021	The Effect of CAG Repeats within the Non-Pathological Range in the HTT Gene on Cognitive Functions in Patients with Subjective Cognitive Decline and Mild Cognitive Impairment.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	14-17	huntingtin	Homo sapiens	67-70
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
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
34206228-2	2021	HD results from an autosomal dominant mutation that causes a trinucleotide CAG repeat expansion and the production of mutant Huntingtin protein (mHTT).	trinucleotide	61-74	huntingtin	Homo sapiens	125-135
34211373-2	2021	HD is caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which results in the production of a pathogenic mutant HTT protein (mHTT).	trinucleotide	22-35	huntingtin	Homo sapiens	60-70
34211373-2	2021	HD is caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which results in the production of a pathogenic mutant HTT protein (mHTT).	trinucleotide	22-35	huntingtin	Homo sapiens	72-75
34211373-2	2021	HD is caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which results in the production of a pathogenic mutant HTT protein (mHTT).	trinucleotide	22-35	huntingtin	Homo sapiens	138-141
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
34207177-3	2021	HTT may also directly or indirectly affect purine metabolism and signaling.	purine	43-49	huntingtin	Homo sapiens	0-3
34266596-6	2021	However, translation of these findings from bench-to-bedside is hampered by differences in murine HD models and HD patients, including mutant huntingtin trinucleotide repeat length, which is highly heterogeneous across the various models.	trinucleotide	153-166	huntingtin	Homo sapiens	142-152
34180418-1	2021	BACKGROUND: Huntington"s disease (HD) is caused by an expanded (>35) CAG trinucleotide repeat in huntingtin (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	69-72	huntingtin	Homo sapiens	97-107
34180418-1	2021	BACKGROUND: Huntington"s disease (HD) is caused by an expanded (>35) CAG trinucleotide repeat in huntingtin (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	69-72	huntingtin	Homo sapiens	109-112
34180418-1	2021	BACKGROUND: Huntington"s disease (HD) is caused by an expanded (>35) CAG trinucleotide repeat in huntingtin (HTT).	trinucleotide	73-86	huntingtin	Homo sapiens	97-107
34180418-1	2021	BACKGROUND: Huntington"s disease (HD) is caused by an expanded (>35) CAG trinucleotide repeat in huntingtin (HTT).	trinucleotide	73-86	huntingtin	Homo sapiens	109-112
35608753-1	2022	Huntington"s disease (HD) is an autosomal dominantly-inherited neurodegenerative disease, which is caused by CAG trinucleotide expansion in exon 1 of the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	109-112	huntingtin	Homo sapiens	154-164
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.	Cysteine	36-44	huntingtin	Homo sapiens	183-193
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.	Deuterium	49-52	huntingtin	Homo sapiens	183-193
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
35608753-1	2022	Huntington"s disease (HD) is an autosomal dominantly-inherited neurodegenerative disease, which is caused by CAG trinucleotide expansion in exon 1 of the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	109-112	huntingtin	Homo sapiens	166-169
35608753-1	2022	Huntington"s disease (HD) is an autosomal dominantly-inherited neurodegenerative disease, which is caused by CAG trinucleotide expansion in exon 1 of the Huntingtin (HTT) gene.	trinucleotide	113-126	huntingtin	Homo sapiens	154-164
35608753-1	2022	Huntington"s disease (HD) is an autosomal dominantly-inherited neurodegenerative disease, which is caused by CAG trinucleotide expansion in exon 1 of the Huntingtin (HTT) gene.	trinucleotide	113-126	huntingtin	Homo sapiens	166-169
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
35615642-1	2022	Huntington"s disease (HD) is an autosomal neurodegenerative disease that is characterized by an excessive number of CAG trinucleotide repeats within the huntingtin gene (HTT).	trinucleotide	120-133	huntingtin	Homo sapiens	153-163
35615642-1	2022	Huntington"s disease (HD) is an autosomal neurodegenerative disease that is characterized by an excessive number of CAG trinucleotide repeats within the huntingtin gene (HTT).	trinucleotide	120-133	huntingtin	Homo sapiens	170-173
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
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
35631226-3	2022	HTT interacts with phospholipids in vitro; however, its interactions are changed when the protein is mutated in HD.	Phospholipids	19-32	huntingtin	Homo sapiens	0-3
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
35275350-1	2022	Huntington"s disease (HD) is a genetic neurodegenerative progressive and fatal disease characterized by motor disorder, cognitive impairment, and behavioral problems, caused by expanded repeats of CAG trinucleotides in the HTT gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	197-200	huntingtin	Homo sapiens	223-226
35275350-1	2022	Huntington"s disease (HD) is a genetic neurodegenerative progressive and fatal disease characterized by motor disorder, cognitive impairment, and behavioral problems, caused by expanded repeats of CAG trinucleotides in the HTT gene.	trinucleotides	201-215	huntingtin	Homo sapiens	223-226
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
35439000-4	2022	Here, the impact of unsaturation in phospholipid tails on htt-lipid interaction and htt aggregation was determined.	Phospholipids	36-48	huntingtin	Homo sapiens	58-61
35439000-4	2022	Here, the impact of unsaturation in phospholipid tails on htt-lipid interaction and htt aggregation was determined.	Phospholipids	36-48	huntingtin	Homo sapiens	84-87
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.	Guanine	9-16	huntingtin	Homo sapiens	76-86
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
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
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
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.	trinucleotide	63-76	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.	trinucleotide	63-76	huntingtin	Homo sapiens	153-163
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
35241644-1	2022	Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by CAG trinucleotide repeat expansions in exon 1 of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	80-83	huntingtin	Homo sapiens	133-143
35241644-1	2022	Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by CAG trinucleotide repeat expansions in exon 1 of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	80-83	huntingtin	Homo sapiens	145-148
35241644-1	2022	Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by CAG trinucleotide repeat expansions in exon 1 of the huntingtin (HTT) gene.	trinucleotide	84-97	huntingtin	Homo sapiens	133-143
35241644-1	2022	Huntington"s Disease (HD) is a progressive neurodegenerative disorder caused by CAG trinucleotide repeat expansions in exon 1 of the huntingtin (HTT) gene.	trinucleotide	84-97	huntingtin	Homo sapiens	145-148
35254632-3	2022	Antisense oligonucleotides (ASOs) lower HTT by targeting transcripts and are well suited for treating neurodegenerative disorders as they distribute broadly throughout the central nervous system (CNS) and are freely taken up by neurons, glia, and ependymal cells.	Oligonucleotides	10-26	huntingtin	Homo sapiens	40-43
35254632-3	2022	Antisense oligonucleotides (ASOs) lower HTT by targeting transcripts and are well suited for treating neurodegenerative disorders as they distribute broadly throughout the central nervous system (CNS) and are freely taken up by neurons, glia, and ependymal cells.	Oligonucleotides, Antisense	28-32	huntingtin	Homo sapiens	40-43
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
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.	trinucleotide	95-108	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.	trinucleotide	95-108	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.	trinucleotide	95-108	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	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
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
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
35363437-3	2022	Here we utilize mu-X-ray fluorescence imaging in combination with rapid freezing to resolve the elemental distribution of phosphorus, sulfur, potassium, and zinc in huntingtin exon-1-mYFP expressing HeLa cells.	Phosphorus	122-132	huntingtin	Homo sapiens	165-175
35363437-3	2022	Here we utilize mu-X-ray fluorescence imaging in combination with rapid freezing to resolve the elemental distribution of phosphorus, sulfur, potassium, and zinc in huntingtin exon-1-mYFP expressing HeLa cells.	Sulfur	134-140	huntingtin	Homo sapiens	165-175
35363437-3	2022	Here we utilize mu-X-ray fluorescence imaging in combination with rapid freezing to resolve the elemental distribution of phosphorus, sulfur, potassium, and zinc in huntingtin exon-1-mYFP expressing HeLa cells.	Potassium	142-151	huntingtin	Homo sapiens	165-175
35238684-0	2022	Suppression of toxicity of the mutant huntingtin protein by its interacting compound, desonide.	Desonide	86-94	huntingtin	Homo sapiens	38-48
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
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
35046408-3	2022	HTT lowering strategies, including antisense oligonucleotides (ASO) showed promising results very recently.	Oligonucleotides	45-61	huntingtin	Homo sapiens	0-3
35046408-3	2022	HTT lowering strategies, including antisense oligonucleotides (ASO) showed promising results very recently.	Oligonucleotides, Antisense	63-66	huntingtin	Homo sapiens	0-3
35069097-0	2021	Cysteine String Protein Controls Two Routes of Export for Misfolded Huntingtin.	Cysteine	0-8	huntingtin	Homo sapiens	68-78
34985962-0	2022	Calcineurin and huntingtin form a calcium-sensing machinery that directs neurotrophic signals to the nucleus.	Calcium	34-41	huntingtin	Homo sapiens	16-26
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
34038804-1	2021	Huntington"s disease (HD) is a devastating and fatal monogenic neurodegenerative disorder characterized by progressive loss of selective neurons in the brain and is caused by an abnormal expansion of CAG trinucleotide repeats in a coding exon of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	200-203	huntingtin	Homo sapiens	250-260
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
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.	Phospholipids	107-120	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.	Phospholipids	107-120	huntingtin	Homo sapiens	257-267
33892278-11	2021	Larger series with more comprehensive diagnostic workout and neuropathological studies are needed to confirm or rule out whether IAs in the HTT gene may cause HD.	4-Iodoacetamidosalicylic acid	129-132	huntingtin	Homo sapiens	140-143
33576024-2	2021	It is caused by a CAG trinucleotide repeat expansion in exon 1 of the huntingtin (HTT) gene located on chromosome 4 1 .	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	18-21	huntingtin	Homo sapiens	70-80
33979693-1	2021	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that is caused by expansion of cytosine/adenosine/guanine repeats in the huntingtin (HTT) gene, which leads to a toxic, aggregation-prone, mutant HTT-polyQ protein.	Cytosine	106-114	huntingtin	Homo sapiens	148-158
33979693-1	2021	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that is caused by expansion of cytosine/adenosine/guanine repeats in the huntingtin (HTT) gene, which leads to a toxic, aggregation-prone, mutant HTT-polyQ protein.	Cytosine	106-114	huntingtin	Homo sapiens	160-163
33979693-1	2021	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that is caused by expansion of cytosine/adenosine/guanine repeats in the huntingtin (HTT) gene, which leads to a toxic, aggregation-prone, mutant HTT-polyQ protein.	Adenosine	115-124	huntingtin	Homo sapiens	148-158
33979693-1	2021	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that is caused by expansion of cytosine/adenosine/guanine repeats in the huntingtin (HTT) gene, which leads to a toxic, aggregation-prone, mutant HTT-polyQ protein.	Adenosine	115-124	huntingtin	Homo sapiens	160-163
33979693-1	2021	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that is caused by expansion of cytosine/adenosine/guanine repeats in the huntingtin (HTT) gene, which leads to a toxic, aggregation-prone, mutant HTT-polyQ protein.	Guanine	125-132	huntingtin	Homo sapiens	148-158
33979693-1	2021	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that is caused by expansion of cytosine/adenosine/guanine repeats in the huntingtin (HTT) gene, which leads to a toxic, aggregation-prone, mutant HTT-polyQ protein.	Guanine	125-132	huntingtin	Homo sapiens	160-163
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
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	83-86	huntingtin	Homo sapiens	158-168
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
33871049-0	2021	Pridopidine reduces mutant huntingtin-induced endoplasmic reticulum stress by modulation of the Sigma-1 receptor.	pridopidine	0-11	huntingtin	Homo sapiens	27-37
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
33576024-2	2021	It is caused by a CAG trinucleotide repeat expansion in exon 1 of the huntingtin (HTT) gene located on chromosome 4 1 .	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	18-21	huntingtin	Homo sapiens	82-85
33576024-2	2021	It is caused by a CAG trinucleotide repeat expansion in exon 1 of the huntingtin (HTT) gene located on chromosome 4 1 .	trinucleotide	22-35	huntingtin	Homo sapiens	70-80
33576024-2	2021	It is caused by a CAG trinucleotide repeat expansion in exon 1 of the huntingtin (HTT) gene located on chromosome 4 1 .	trinucleotide	22-35	huntingtin	Homo sapiens	82-85
33980291-7	2021	In thalamus, we observed a 5-HT1A-by-5-HTT and group-by-5-HTT interaction in GABA concentrations, with the 5-HTT high expressing genotype differing between groups and 5-HT1A genotypes.	gamma-Aminobutyric Acid	77-81	huntingtin	Homo sapiens	58-61
33980291-7	2021	In thalamus, we observed a 5-HT1A-by-5-HTT and group-by-5-HTT interaction in GABA concentrations, with the 5-HTT high expressing genotype differing between groups and 5-HT1A genotypes.	gamma-Aminobutyric Acid	77-81	huntingtin	Homo sapiens	58-61
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
34038804-1	2021	Huntington"s disease (HD) is a devastating and fatal monogenic neurodegenerative disorder characterized by progressive loss of selective neurons in the brain and is caused by an abnormal expansion of CAG trinucleotide repeats in a coding exon of the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	200-203	huntingtin	Homo sapiens	262-265
33852844-0	2021	Huntingtin-mediated axonal transport requires arginine methylation by PRMT6.	Arginine	46-54	huntingtin	Homo sapiens	0-10
33852844-2	2021	To better understand how HTT mediates axonal transport and why this function is disrupted in Huntington"s disease (HD), we study vesicle-associated HTT and find that it is dimethylated at a highly conserved arginine residue (R118) by the protein arginine methyltransferase 6 (PRMT6).	Arginine	207-215	huntingtin	Homo sapiens	148-151
33852844-6	2021	Arginine methylation thus regulates HTT-mediated vesicular transport along the axon, and increasing HTT methylation could be of therapeutic interest for HD.	Arginine	0-8	huntingtin	Homo sapiens	36-39
34038804-1	2021	Huntington"s disease (HD) is a devastating and fatal monogenic neurodegenerative disorder characterized by progressive loss of selective neurons in the brain and is caused by an abnormal expansion of CAG trinucleotide repeats in a coding exon of the huntingtin (HTT) gene.	trinucleotide	204-217	huntingtin	Homo sapiens	250-260
34038804-1	2021	Huntington"s disease (HD) is a devastating and fatal monogenic neurodegenerative disorder characterized by progressive loss of selective neurons in the brain and is caused by an abnormal expansion of CAG trinucleotide repeats in a coding exon of the huntingtin (HTT) gene.	trinucleotide	204-217	huntingtin	Homo sapiens	262-265
33889127-6	2021	In HD, monthly intrathecal delivery of an antisense oligonucleotide (ASO) targeting the huntingtin protein (HTT) mRNA proved to be safe and tolerable, and demonstrated a dose-dependent reduction of the cerebrospinal fluid levels of mutated HTT, while a small phase-I study testing implantable capsules of cells engineered to synthesize ciliary neurotrophic factor failed to show consistent drug delivery.	Oligonucleotides	52-67	huntingtin	Homo sapiens	88-98
33889127-6	2021	In HD, monthly intrathecal delivery of an antisense oligonucleotide (ASO) targeting the huntingtin protein (HTT) mRNA proved to be safe and tolerable, and demonstrated a dose-dependent reduction of the cerebrospinal fluid levels of mutated HTT, while a small phase-I study testing implantable capsules of cells engineered to synthesize ciliary neurotrophic factor failed to show consistent drug delivery.	Oligonucleotides	52-67	huntingtin	Homo sapiens	108-111
33889127-6	2021	In HD, monthly intrathecal delivery of an antisense oligonucleotide (ASO) targeting the huntingtin protein (HTT) mRNA proved to be safe and tolerable, and demonstrated a dose-dependent reduction of the cerebrospinal fluid levels of mutated HTT, while a small phase-I study testing implantable capsules of cells engineered to synthesize ciliary neurotrophic factor failed to show consistent drug delivery.	Oligonucleotides	52-67	huntingtin	Homo sapiens	240-243
33889127-6	2021	In HD, monthly intrathecal delivery of an antisense oligonucleotide (ASO) targeting the huntingtin protein (HTT) mRNA proved to be safe and tolerable, and demonstrated a dose-dependent reduction of the cerebrospinal fluid levels of mutated HTT, while a small phase-I study testing implantable capsules of cells engineered to synthesize ciliary neurotrophic factor failed to show consistent drug delivery.	Oligonucleotides, Antisense	69-72	huntingtin	Homo sapiens	88-98
33889127-6	2021	In HD, monthly intrathecal delivery of an antisense oligonucleotide (ASO) targeting the huntingtin protein (HTT) mRNA proved to be safe and tolerable, and demonstrated a dose-dependent reduction of the cerebrospinal fluid levels of mutated HTT, while a small phase-I study testing implantable capsules of cells engineered to synthesize ciliary neurotrophic factor failed to show consistent drug delivery.	Oligonucleotides, Antisense	69-72	huntingtin	Homo sapiens	108-111
33889127-6	2021	In HD, monthly intrathecal delivery of an antisense oligonucleotide (ASO) targeting the huntingtin protein (HTT) mRNA proved to be safe and tolerable, and demonstrated a dose-dependent reduction of the cerebrospinal fluid levels of mutated HTT, while a small phase-I study testing implantable capsules of cells engineered to synthesize ciliary neurotrophic factor failed to show consistent drug delivery.	Oligonucleotides, Antisense	69-72	huntingtin	Homo sapiens	240-243
32941796-5	2021	We ectopically expressed full-length (FL) and exon1 fragment of human HTT with phosphomimetic and resistant mutations at serines 13 and 16 in different neuronal populations.	Serine	121-128	huntingtin	Homo sapiens	70-73
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
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
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.	gamma-Aminobutyric Acid	173-196	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.	gamma-Aminobutyric Acid	173-196	huntingtin	Homo sapiens	130-133
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.	gamma-Aminobutyric Acid	198-202	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.	gamma-Aminobutyric Acid	198-202	huntingtin	Homo sapiens	130-133
33797036-4	2021	Pridopidine effects on mitochondrial dynamics were assessed in primary neurons from YAC128 HD mice expressing the mutant human HTT gene.	pridopidine	0-11	huntingtin	Homo sapiens	127-130
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
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
33731741-3	2021	As an alternative to siRNA or oligonucleotide methods, we hypothesized that suppression of HTT expression might be accomplished by small molecules that either (1) directly decrease HTT expression by suppressing HTT promoter activity or (2) indirectly decrease HTT expression by increasing the promoter activity of HTT-AS, the gene antisense to HTT that appears to inhibit expression of HTT.	Oligonucleotides	30-45	huntingtin	Homo sapiens	91-94
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
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
32498555-5	2021	Mutant huntingtin (mHTT) can directly interact with mitochondrial proteins, as translocase of the inner membrane 23 (TIM23), disrupting mitochondrial proteostasis and favoring ROS production and HD progression.	Reactive Oxygen Species	176-179	huntingtin	Homo sapiens	7-17
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
33517535-10	2021	Our findings further support emerging evidence that pathogenic trinucleotide repeat expansions of the HTT gene may impact neurodevelopment.	trinucleotide	63-76	huntingtin	Homo sapiens	102-105
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
33567536-0	2021	A Novel Triplet-Primed PCR Assay to Detect the Full Range of Trinucleotide CAG Repeats in the Huntingtin Gene (HTT).	trinucleotide	61-74	huntingtin	Homo sapiens	94-104
33567536-0	2021	A Novel Triplet-Primed PCR Assay to Detect the Full Range of Trinucleotide CAG Repeats in the Huntingtin Gene (HTT).	trinucleotide	61-74	huntingtin	Homo sapiens	111-114
33606279-1	2021	Huntington"s disease (HD) is a fatal disorder associated with germline trinucleotide repeat expansions in the HTT gene and characterised by striatal neurodegeneration.	trinucleotide	71-84	huntingtin	Homo sapiens	110-113
33586075-3	2021	The etiology of Huntington"s disease (HD) is well-known as an abnormally expanded trinucleotide repeat within the huntingtin gene.	trinucleotide	82-95	huntingtin	Homo sapiens	114-124
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
33604336-7	2021	Moreover, a previously described potential anti-HD drug EVP4593 has been found to attenuate high levels of both huntingtin and STIM2 that may contribute to its neuroprotective effect.	EVP 4593	56-63	huntingtin	Homo sapiens	112-122
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
33509017-6	2021	Selective autophagy was inhibited as illustrated by the accumulation of large protein aggregates in BPLF1-positive cells co-transfected with an aggregate-prone HTT (huntingtin)-Q109 construct, and by a slower autophagy-dependent clearance of protein aggregates upon transfection of BPLF1 in cells expressing a tetracycline-regulated HTT-Q103.	Tetracycline	310-322	huntingtin	Homo sapiens	165-175
33495516-0	2021	Gossypol, a novel modulator of VCP, induces autophagic degradation of mutant huntingtin by promoting the formation of VCP/p97-LC3-mHTT complex.	Gossypol	0-8	huntingtin	Homo sapiens	77-87
33310753-11	2021	Recently, it was demonstrated that intrathecal administration of a HTT lowering agent leads to dose-dependent reduction of CSF mHTT in HD patients.	mhtt	127-131	huntingtin	Homo sapiens	67-70
33310753-13	2021	Our findings that HTT enters CSF by both passive release and active secretion followed by glymphatic clearance may have significant implications for interpretation of treatment-induced changes of CSF mHTT in clinical trials for HD.	mhtt	200-204	huntingtin	Homo sapiens	18-21
32805086-1	2021	Posttranslational modifications (PTMs) within the first 17 amino acids (Nt17) of exon1 of the Huntingtin protein (Httex1) play important roles in modulating its cellular properties and functions in health and disease.	17 amino acids	56-70	huntingtin	Homo sapiens	94-104
32861946-5	2021	On the rise of the HTT, the carbonaceous structures of biopolymer compositions were reorganized and converted to graphitic structures in biochar accompanied by the large decomposition or carbonization of CEL and HEM, leading to the reduced carbon content, surface functional groups, aromaticity and molecular weight of DBCs, as well as the decrease of protein-like and relative increase of fulvic-like fluorescent substances in most DBCs.	Carbon	28-34	huntingtin	Homo sapiens	19-22
32805086-2	2021	In particular, phosphorylation of threonine and serine residues (T3, S13, and/or S16) has been shown to inhibit Htt aggregation in vitro and inclusion formation in cellular and animal models of Huntington"s disease (HD).	Threonine	34-43	huntingtin	Homo sapiens	112-115
32805086-2	2021	In particular, phosphorylation of threonine and serine residues (T3, S13, and/or S16) has been shown to inhibit Htt aggregation in vitro and inclusion formation in cellular and animal models of Huntington"s disease (HD).	Serine	48-54	huntingtin	Homo sapiens	112-115
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.	cytosine-adenine-guanine	167-191	huntingtin	Homo sapiens	108-118
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
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
33130095-8	2021	With zwitterionic head groups, large lipid to peptide ratios were required to have a statistically significant impact on htt aggregation.	Peptides	46-53	huntingtin	Homo sapiens	121-124
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	193-196	huntingtin	Homo sapiens	108-118
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
32686867-1	2020	BACKGROUND: Huntington"s disease (HD) develops in individuals with extended cytosine-adenine-guanine (CAG) repeats within the huntingtin (HTT) gene, causing neurodegeneration and progressive motor and cognitive symptoms.	cytosine-adenine-guanine	76-100	huntingtin	Homo sapiens	126-136
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
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.	Calcium	201-208	huntingtin	Homo sapiens	49-59
33425919-5	2020	The dysregulation of Ca2+ homeostasis is postulated to be a cause of HD progression because the SOCE pathway is indirectly and abnormally activated by mutant huntingtin (HTT) in gamma-aminobutyric acid (GABA)ergic medium spiny neurons (MSNs) from the striatum in HD models before the first symptoms of the disease appear.	gamma-Aminobutyric Acid	178-201	huntingtin	Homo sapiens	158-168
33425919-5	2020	The dysregulation of Ca2+ homeostasis is postulated to be a cause of HD progression because the SOCE pathway is indirectly and abnormally activated by mutant huntingtin (HTT) in gamma-aminobutyric acid (GABA)ergic medium spiny neurons (MSNs) from the striatum in HD models before the first symptoms of the disease appear.	gamma-Aminobutyric Acid	178-201	huntingtin	Homo sapiens	170-173
33425919-5	2020	The dysregulation of Ca2+ homeostasis is postulated to be a cause of HD progression because the SOCE pathway is indirectly and abnormally activated by mutant huntingtin (HTT) in gamma-aminobutyric acid (GABA)ergic medium spiny neurons (MSNs) from the striatum in HD models before the first symptoms of the disease appear.	gamma-Aminobutyric Acid	203-207	huntingtin	Homo sapiens	158-168
33425919-5	2020	The dysregulation of Ca2+ homeostasis is postulated to be a cause of HD progression because the SOCE pathway is indirectly and abnormally activated by mutant huntingtin (HTT) in gamma-aminobutyric acid (GABA)ergic medium spiny neurons (MSNs) from the striatum in HD models before the first symptoms of the disease appear.	gamma-Aminobutyric Acid	203-207	huntingtin	Homo sapiens	170-173
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
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.	n-terminal amino acids	45-67	huntingtin	Homo sapiens	78-81
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
32878904-1	2020	BACKGROUND: Huntington"s disease (HD)(MIM:143100) is an severe autosomal dominant neurodegenerative disease caused by the dynamic expansion of CAG trinucleotides (> 35) in the HTT gene [Genomic Coordinates- (GRCh38):4:3,074,680-3,243,959].	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	143-146	huntingtin	Homo sapiens	176-179
32878904-1	2020	BACKGROUND: Huntington"s disease (HD)(MIM:143100) is an severe autosomal dominant neurodegenerative disease caused by the dynamic expansion of CAG trinucleotides (> 35) in the HTT gene [Genomic Coordinates- (GRCh38):4:3,074,680-3,243,959].	trinucleotides	147-161	huntingtin	Homo sapiens	176-179
32686867-1	2020	BACKGROUND: Huntington"s disease (HD) develops in individuals with extended cytosine-adenine-guanine (CAG) repeats within the huntingtin (HTT) gene, causing neurodegeneration and progressive motor and cognitive symptoms.	cytosine-adenine-guanine	76-100	huntingtin	Homo sapiens	138-141
32686867-1	2020	BACKGROUND: Huntington"s disease (HD) develops in individuals with extended cytosine-adenine-guanine (CAG) repeats within the huntingtin (HTT) gene, causing neurodegeneration and progressive motor and cognitive symptoms.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	102-105	huntingtin	Homo sapiens	126-136
32686867-1	2020	BACKGROUND: Huntington"s disease (HD) develops in individuals with extended cytosine-adenine-guanine (CAG) repeats within the huntingtin (HTT) gene, causing neurodegeneration and progressive motor and cognitive symptoms.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	102-105	huntingtin	Homo sapiens	138-141
32979507-1	2020	Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in exon 1 of the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	70-73	huntingtin	Homo sapiens	122-132
32979507-1	2020	Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in exon 1 of the huntingtin gene.	trinucleotide	74-87	huntingtin	Homo sapiens	122-132
33329316-1	2020	Huntington"s disease (HD) is an autosomal dominantly inherited neurodegenerative disorder caused by a trinucleotide repeat expansion in the Huntingtin gene.	trinucleotide	102-115	huntingtin	Homo sapiens	140-150
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
33096080-0	2020	Structural Model of the Proline-rich Domain of Huntingtin exon-1 fibrils.	Proline	24-31	huntingtin	Homo sapiens	47-57
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
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
33094816-6	2020	A</protein-id> 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
33167595-1	2020	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by pathogenic expansions of the triplet cytosine-adenosine-guanosine (CAG) within the Huntingtin gene.	Adenosine	134-143	huntingtin	Homo sapiens	171-181
33167595-1	2020	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by pathogenic expansions of the triplet cytosine-adenosine-guanosine (CAG) within the Huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	155-158	huntingtin	Homo sapiens	171-181
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
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
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
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.	thioflavin T	186-198	huntingtin	Homo sapiens	44-47
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.	thioflavin T	200-203	huntingtin	Homo sapiens	44-47
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
33209959-1	2020	Novel treatments for Huntington"s disease (HD), a progressive neurodegenerative disorder, include selective targeting of the mutant allele of the huntingtin gene (mHTT) carrying the abnormally expanded disease-causing cytosine-adenine-guanine (CAG) repeat.	cytosine-adenine-guanine	218-242	huntingtin	Homo sapiens	146-156
33209959-1	2020	Novel treatments for Huntington"s disease (HD), a progressive neurodegenerative disorder, include selective targeting of the mutant allele of the huntingtin gene (mHTT) carrying the abnormally expanded disease-causing cytosine-adenine-guanine (CAG) repeat.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	244-247	huntingtin	Homo sapiens	146-156
33049985-1	2020	Huntington"s disease is a rare neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) trinucleotide expansion in the Huntingtin (HTT) gene.	cytosine-adenine-guanine	69-93	huntingtin	Homo sapiens	131-141
33049985-1	2020	Huntington"s disease is a rare neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) trinucleotide expansion in the Huntingtin (HTT) gene.	cytosine-adenine-guanine	69-93	huntingtin	Homo sapiens	143-146
33049985-1	2020	Huntington"s disease is a rare neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) trinucleotide expansion in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	95-98	huntingtin	Homo sapiens	131-141
33049985-1	2020	Huntington"s disease is a rare neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) trinucleotide expansion in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	95-98	huntingtin	Homo sapiens	143-146
33049985-1	2020	Huntington"s disease is a rare neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) trinucleotide expansion in the Huntingtin (HTT) gene.	trinucleotide	100-113	huntingtin	Homo sapiens	131-141
33049985-1	2020	Huntington"s disease is a rare neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) trinucleotide expansion in the Huntingtin (HTT) gene.	trinucleotide	100-113	huntingtin	Homo sapiens	143-146
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
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
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
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
33214751-0	2020	Molecular docking studies of a-mangostin with oral cancer targets ARRB1, FLNA, CALM3 and HTT.	mangostin	29-40	huntingtin	Homo sapiens	89-92
33214751-5	2020	Results shows HTT having good inhibition features with the Alpha Mangostin followed by the CALM3, FLNA and finally ARRB1 in the decreasing order.	mangostin	59-74	huntingtin	Homo sapiens	14-17
33214751-7	2020	CALM3 and HTT were promising targets for anticancer treatment using alpha mangostin.	mangostin	68-83	huntingtin	Homo sapiens	10-13
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
32662649-1	2020	Mutant huntingtin (mHTT) protein carrying the elongated N-terminal polyglutamine (polyQ) tract misfolds and forms protein aggregates characteristic of HD pathology.	n-terminal polyglutamine	56-80	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
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
32649191-3	2020	Here we report hyperbranched polyglycerol dendrimer terminated with anti-amyloidogenic small molecules such as gallate, tyrosine and trehalose and their potential in inhibiting lysozyme/huntingtin protein aggregation under intra/extracellular space.	polyglycerol	29-41	huntingtin	Homo sapiens	186-196
32649191-3	2020	Here we report hyperbranched polyglycerol dendrimer terminated with anti-amyloidogenic small molecules such as gallate, tyrosine and trehalose and their potential in inhibiting lysozyme/huntingtin protein aggregation under intra/extracellular space.	Gallic acid	111-118	huntingtin	Homo sapiens	186-196
32649191-3	2020	Here we report hyperbranched polyglycerol dendrimer terminated with anti-amyloidogenic small molecules such as gallate, tyrosine and trehalose and their potential in inhibiting lysozyme/huntingtin protein aggregation under intra/extracellular space.	Tyrosine	120-128	huntingtin	Homo sapiens	186-196
32649191-3	2020	Here we report hyperbranched polyglycerol dendrimer terminated with anti-amyloidogenic small molecules such as gallate, tyrosine and trehalose and their potential in inhibiting lysozyme/huntingtin protein aggregation under intra/extracellular space.	Trehalose	133-142	huntingtin	Homo sapiens	186-196
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
32784364-1	2020	Huntington"s disease (HD) is a fatal neurodegenerative disease caused by the expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene.	cytosine-adenine-guanine	90-114	huntingtin	Homo sapiens	136-146
32784364-1	2020	Huntington"s disease (HD) is a fatal neurodegenerative disease caused by the expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	116-119	huntingtin	Homo sapiens	136-146
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
32657893-1	2020	PURPOSE OF REVIEW: Huntington"s disease is a fatal autosomal dominant neurodegenerative disorder caused by a trinucleotide expansion in the HTT gene, and current therapies focus on symptomatic treatment.	trinucleotide	109-122	huntingtin	Homo sapiens	140-143
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
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
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
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
32560122-3	2020	The mutant huntingtin protein (HTT) exhibits an expansion of a polyglutamine repeat.	polyglutamine	63-76	huntingtin	Homo sapiens	11-21
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
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
32402249-0	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
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
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.	Proline	170-177	huntingtin	Homo sapiens	96-106
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
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
33642842-0	2020	Discovery of sultam-containing small-molecule disruptors of the huntingtin-calmodulin protein-protein interaction.	naphthosultone	13-19	huntingtin	Homo sapiens	64-74
32410324-2	2020	Alterations in cholesterol metabolism and distribution have been reported in Huntington"s disease, including abnormal interactions between mutant huntingtin and sterol regulatory element-binding proteins, decreased levels of apolipoprotein E/cholesterol/low-density lipoprotein receptor complexes, and alterations in the synthesis of ATP-binding cassette transporter A1.	Cholesterol	15-26	huntingtin	Homo sapiens	146-156
32410324-4	2020	The interaction of mutant huntingtin with sterol regulatory element-binding proteins is of particular interest given that sterol regulatory element-binding proteins play a dual role: They take part in lipid and cholesterol metabolism, but also in the inflammatory response that induces immune cell migration as well as toxic effects, particularly in astrocytes.	Sterols	42-48	huntingtin	Homo sapiens	26-36
32410324-4	2020	The interaction of mutant huntingtin with sterol regulatory element-binding proteins is of particular interest given that sterol regulatory element-binding proteins play a dual role: They take part in lipid and cholesterol metabolism, but also in the inflammatory response that induces immune cell migration as well as toxic effects, particularly in astrocytes.	Cholesterol	211-222	huntingtin	Homo sapiens	26-36
32407769-1	2020	Huntington"s disease (HD) is caused by a highly polymorphic CAG trinucleotide expansion in the gene encoding for the huntingtin protein (HTT).	trinucleotide	64-77	huntingtin	Homo sapiens	117-127
32407769-1	2020	Huntington"s disease (HD) is caused by a highly polymorphic CAG trinucleotide expansion in the gene encoding for the huntingtin protein (HTT).	trinucleotide	64-77	huntingtin	Homo sapiens	137-140
32439599-6	2020	Despite the small degree of spreading, the presence of mHTT generated changes in endogenous huntingtin (HTT) levels in both models.	mhtt	55-59	huntingtin	Homo sapiens	92-102
32555394-1	2020	Trinucleotide (CAG) repeat expansions longer than 39 in the huntingtin (HTT) gene cause Huntington"s disease (HD).	trinucleotide	0-13	huntingtin	Homo sapiens	60-70
32555394-1	2020	Trinucleotide (CAG) repeat expansions longer than 39 in the huntingtin (HTT) gene cause Huntington"s disease (HD).	trinucleotide	0-13	huntingtin	Homo sapiens	72-75
32555394-1	2020	Trinucleotide (CAG) repeat expansions longer than 39 in the huntingtin (HTT) gene cause Huntington"s disease (HD).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	15-18	huntingtin	Homo sapiens	60-70
32555394-1	2020	Trinucleotide (CAG) repeat expansions longer than 39 in the huntingtin (HTT) gene cause Huntington"s disease (HD).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	15-18	huntingtin	Homo sapiens	72-75
32555394-3	2020	The Swedish Huntingtin Alleles and Phenotype (SHAPE) study aims to assess the frequency of trinucleotide repeat expansions in the HTT gene in north Sweden.	trinucleotide	91-104	huntingtin	Homo sapiens	12-22
32555394-3	2020	The Swedish Huntingtin Alleles and Phenotype (SHAPE) study aims to assess the frequency of trinucleotide repeat expansions in the HTT gene in north Sweden.	trinucleotide	91-104	huntingtin	Homo sapiens	130-133
20301482-2	1993	DIAGNOSIS/TESTING: The diagnosis of HD rests on positive family history, characteristic clinical findings, and the detection of an expansion of 36 or more CAG trinucleotide repeats in HTT.	trinucleotide	159-172	huntingtin	Homo sapiens	184-187
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
32498290-2	2020	The present study emphasizes the protective effects of (-)-loliolide (HTT) isolated from Sargassum horneri against FD-induced oxidative stress in human HaCaT keratinocytes.	loliolide	59-68	huntingtin	Homo sapiens	70-73
32498290-4	2020	HTT did not show any cytotoxicity, and it further illustrated the potential to increase cell viability by reducing the reactive oxygen species (ROS) production in FD-stimulated keratinocytes.	Reactive Oxygen Species	119-142	huntingtin	Homo sapiens	0-3
32498290-4	2020	HTT did not show any cytotoxicity, and it further illustrated the potential to increase cell viability by reducing the reactive oxygen species (ROS) production in FD-stimulated keratinocytes.	Reactive Oxygen Species	144-147	huntingtin	Homo sapiens	0-3
32202594-1	2020	Huntington disease (HD) is caused by a cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin gene, HTT, that results in expression of variant (mutant) huntingtin protein (HTT).	cytosine-adenine-guanine trinucleotide	39-77	huntingtin	Homo sapiens	102-112
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
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
32202594-1	2020	Huntington disease (HD) is caused by a cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin gene, HTT, that results in expression of variant (mutant) huntingtin protein (HTT).	cytosine-adenine-guanine trinucleotide	39-77	huntingtin	Homo sapiens	119-122
32202594-1	2020	Huntington disease (HD) is caused by a cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin gene, HTT, that results in expression of variant (mutant) huntingtin protein (HTT).	cytosine-adenine-guanine trinucleotide	39-77	huntingtin	Homo sapiens	171-181
32202594-1	2020	Huntington disease (HD) is caused by a cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin gene, HTT, that results in expression of variant (mutant) huntingtin protein (HTT).	cytosine-adenine-guanine trinucleotide	39-77	huntingtin	Homo sapiens	191-194
32202594-10	2020	In a recently completed phase 1/2a study of RG6042 in 46 adults with early manifest HD, antisense oligonucleotide-mediated partial reduction of HTT was reported to be generally safe and well tolerated over the course of 4-monthly RG6042 doses.	rg6042	44-50	huntingtin	Homo sapiens	144-147
32202594-10	2020	In a recently completed phase 1/2a study of RG6042 in 46 adults with early manifest HD, antisense oligonucleotide-mediated partial reduction of HTT was reported to be generally safe and well tolerated over the course of 4-monthly RG6042 doses.	Oligonucleotides	98-113	huntingtin	Homo sapiens	144-147
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
32548276-1	2020	Background: The huntingtin gene (HTT) pathogenic cytosine-adenine-guanine (CAG) repeat expansion responsible for Huntington disease (HD) is phased with single nucleotide polymorphisms (SNPs), providing targets for allele-selective treatments.	cytosine-adenine-guanine	49-73	huntingtin	Homo sapiens	16-26
32548276-1	2020	Background: The huntingtin gene (HTT) pathogenic cytosine-adenine-guanine (CAG) repeat expansion responsible for Huntington disease (HD) is phased with single nucleotide polymorphisms (SNPs), providing targets for allele-selective treatments.	cytosine-adenine-guanine	49-73	huntingtin	Homo sapiens	33-36
32279715-1	2020	Huntington disease, a neurodegenerative disease characterized by progressive motor, behavioral, and cognitive decline, is caused by a CAG trinucleotide repeat expansion in the huntingtin gene on chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	134-137	huntingtin	Homo sapiens	176-186
32279715-1	2020	Huntington disease, a neurodegenerative disease characterized by progressive motor, behavioral, and cognitive decline, is caused by a CAG trinucleotide repeat expansion in the huntingtin gene on chromosome 4.	trinucleotide	138-151	huntingtin	Homo sapiens	176-186
32391325-0	2020	Length-Dependent Structural Transformations of Huntingtin PolyQ Domain Upon Binding to 2D-Nanomaterials.	polyglutamine	58-63	huntingtin	Homo sapiens	47-57
32004439-6	2020	Top mutant huntingtin toxicity modifier genes included several Nme genes and several genes involved in methylation-dependent chromatin silencing and dopamine signaling, results that reveal new HD therapeutic target pathways.	Dopamine	149-157	huntingtin	Homo sapiens	11-21
32067426-1	2020	BACKGROUND: Huntington disease (HD) (MIM: 143100) is a severe autosomal dominant neurodegenerative disease caused by the expansion of CAG trinucleotides (>35) in the HTT.	trinucleotides	138-152	huntingtin	Homo sapiens	166-169
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
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
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.	trinucleotide	118-131	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.	trinucleotide	118-131	huntingtin	Homo sapiens	157-160
32235053-6	2021	Overall, our FLIM study combined with confocal fluorescence imaging visualizes the absorption of the mutant Htt protein aggregates which results in a distinct NADH fluorescence lifetime between control cells and acceptor cells.	NAD	159-163	huntingtin	Homo sapiens	108-111
32245050-1	2020	Trials using antisense oligonucleotide technology to lower Huntingtin levels in Huntington"s disease (HD) are currently ongoing.	Oligonucleotides	23-38	huntingtin	Homo sapiens	59-69
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
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
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
31899071-1	2020	Despite being an autosomal dominant disorder caused by a known coding mutation in the gene HTT, Huntington"s disease (HD) patients with similar trinucleotide repeat mutations can have an age of onset that varies by decades.	trinucleotide	144-157	huntingtin	Homo sapiens	91-94
32463584-4	2020	For antidepressants, the clinical threshold of serotonin transporter (5-HTT) occupancy is reported to be 70%-80% although the relation between the side effect and 5-HTT occupancy has not yet been established.	Serotonin	47-56	huntingtin	Homo sapiens	72-75
32266815-3	2020	Here, we apply site-specific isotopic labeling to obtain high-resolution NMR data on the cis/trans equilibrium of prolines within the poly-P repeats of huntingtin exon 1, the causative agent of Huntington"s disease.	Proline	114-122	huntingtin	Homo sapiens	152-162
32266815-3	2020	Here, we apply site-specific isotopic labeling to obtain high-resolution NMR data on the cis/trans equilibrium of prolines within the poly-P repeats of huntingtin exon 1, the causative agent of Huntington"s disease.	polyproline	134-140	huntingtin	Homo sapiens	152-162
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.	deuterated	33-43	huntingtin	Homo sapiens	86-96
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
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
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.	Carbon	225-231	huntingtin	Homo sapiens	86-96
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.	Deuterium	232-241	huntingtin	Homo sapiens	86-96
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
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
31715317-7	2020	Considering its adult-onset nature, a potential relationship between dysregulation in the synthesis of sex steroid hormones and the pathogenesis of the mutant HTT gene appears to be an important clinical issue in HD.	Steroids	107-114	huntingtin	Homo sapiens	159-162
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
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
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
31880908-6	2020	Three lysine residues (K6, K9, and K15) within Nt17 can be SUMOylated, which modifies htt"s accumulation and toxicity within cells in a variety of HD models.	tyrosyl-lysine	6-12	huntingtin	Homo sapiens	86-89
31940909-2	2020	The cause of disease pathology is an expansion of cytosine-adenine-guanine (CAG) repeats within the huntingtin gene (HTT) on chromosome 4 (4p16.3), which codes the huntingtin protein (mHTT).	cytidylyl-3'-5'-guanosine	50-74	huntingtin	Homo sapiens	100-110
31814404-0	2020	Nucleation Inhibition of Huntingtin Protein (htt) by Polyproline PPII Helices: A Potential Interaction with the N-Terminal alpha-Helical Region of Htt.	polyproline	53-64	huntingtin	Homo sapiens	25-43
31814404-0	2020	Nucleation Inhibition of Huntingtin Protein (htt) by Polyproline PPII Helices: A Potential Interaction with the N-Terminal alpha-Helical Region of Htt.	polyproline	53-64	huntingtin	Homo sapiens	45-48
31814404-3	2020	Because tertiary interactions with a downstream (C-terminal) polyproline (polyP) region of htt may disrupt the formation of oligomers, which are precursors to fibrillar species, the effect of co-incubation of a region of htt with a 10-residue polyP peptide on oligomerization and fibrillization has been examined by atomic force microscopy.	polyproline	61-72	huntingtin	Homo sapiens	91-94
31757420-2	2020	Here, we used the N&amp;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&amp;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&amp;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&amp;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
31875875-0	2020	Mutant huntingtin interacts with the sterol regulatory element-binding proteins and impairs their nuclear import.	Sterols	37-43	huntingtin	Homo sapiens	7-17
31875875-1	2020	Brain cholesterol homeostasis is altered in Huntington"s disease (HD), a neurodegenerative disorder caused by the expansion of a CAG nucleotide repeat in the HTT gene.	Cholesterol	6-17	huntingtin	Homo sapiens	158-161
31875875-2	2020	Genes involved in the synthesis of cholesterol and fatty acids were shown to be downregulated shortly after the expression of mutant huntingtin (mHTT) in inducible HD cells.	Cholesterol	35-46	huntingtin	Homo sapiens	133-143
31875875-2	2020	Genes involved in the synthesis of cholesterol and fatty acids were shown to be downregulated shortly after the expression of mutant huntingtin (mHTT) in inducible HD cells.	Fatty Acids	51-62	huntingtin	Homo sapiens	133-143
31940909-2	2020	The cause of disease pathology is an expansion of cytosine-adenine-guanine (CAG) repeats within the huntingtin gene (HTT) on chromosome 4 (4p16.3), which codes the huntingtin protein (mHTT).	cytidylyl-3'-5'-guanosine	50-74	huntingtin	Homo sapiens	117-120
31940909-2	2020	The cause of disease pathology is an expansion of cytosine-adenine-guanine (CAG) repeats within the huntingtin gene (HTT) on chromosome 4 (4p16.3), which codes the huntingtin protein (mHTT).	cytidylyl-3'-5'-guanosine	50-74	huntingtin	Homo sapiens	164-174
31940909-2	2020	The cause of disease pathology is an expansion of cytosine-adenine-guanine (CAG) repeats within the huntingtin gene (HTT) on chromosome 4 (4p16.3), which codes the huntingtin protein (mHTT).	cytidylyl-3'-5'-guanosine	76-79	huntingtin	Homo sapiens	100-110
31940909-2	2020	The cause of disease pathology is an expansion of cytosine-adenine-guanine (CAG) repeats within the huntingtin gene (HTT) on chromosome 4 (4p16.3), which codes the huntingtin protein (mHTT).	cytidylyl-3'-5'-guanosine	76-79	huntingtin	Homo sapiens	117-120
31940909-2	2020	The cause of disease pathology is an expansion of cytosine-adenine-guanine (CAG) repeats within the huntingtin gene (HTT) on chromosome 4 (4p16.3), which codes the huntingtin protein (mHTT).	cytidylyl-3'-5'-guanosine	76-79	huntingtin	Homo sapiens	164-174
32566927-5	2020	The length of the disease-causing trinucleotide repeat expansion in the huntingtin gene predicted the change in the precentral gyrus (P = 0.03) and the intensity of the exercise intervention predicted hippocampal perfusion change in Huntington"s disease participants (P < 0.001).	trinucleotide	34-47	huntingtin	Homo sapiens	72-82
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
31645369-6	2019	We were able to demonstrate not only an accumulation of different forms of mutant huntingtin (mHTT) in TgHD brain, but also pathological changes associated with cellular damage caused by mHTT.	mhtt	94-98	huntingtin	Homo sapiens	82-92
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
30523767-3	2020	This HD variation is because of the development of a polyglutamine (CAG) repeats in the exon 1 of the Huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	68-71	huntingtin	Homo sapiens	102-112
32623404-0	2020	Cysteamine Protects Neurons from Mutant Huntingtin Toxicity.	Cysteamine	0-10	huntingtin	Homo sapiens	40-50
31223078-3	2020	Huntington"s disease is a genetic neurological disorder caused by a repeated expansion of the CAG trinucleotide, causing instability in the N-terminal of the gene coding for the Huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	94-97	huntingtin	Homo sapiens	178-188
31223078-3	2020	Huntington"s disease is a genetic neurological disorder caused by a repeated expansion of the CAG trinucleotide, causing instability in the N-terminal of the gene coding for the Huntingtin protein.	trinucleotide	98-111	huntingtin	Homo sapiens	178-188
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 tract	70-89	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 tract	70-89	huntingtin	Homo sapiens	185-195
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	103-106	huntingtin	Homo sapiens	153-163
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
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	103-106	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	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
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
31304621-2	2019	HD is driven by elongated cytosine-adenine-guanine (CAG) repeat (36 repeats or more) on the short arm of chromosome 4p16.3 in the Huntingtin gene (HTTg) which encode the huntingtin protein (HTT).	cytosine-adenine-guanine	26-50	huntingtin	Homo sapiens	130-140
31304621-2	2019	HD is driven by elongated cytosine-adenine-guanine (CAG) repeat (36 repeats or more) on the short arm of chromosome 4p16.3 in the Huntingtin gene (HTTg) which encode the huntingtin protein (HTT).	cytosine-adenine-guanine	26-50	huntingtin	Homo sapiens	170-180
31304621-2	2019	HD is driven by elongated cytosine-adenine-guanine (CAG) repeat (36 repeats or more) on the short arm of chromosome 4p16.3 in the Huntingtin gene (HTTg) which encode the huntingtin protein (HTT).	cytosine-adenine-guanine	26-50	huntingtin	Homo sapiens	147-150
31304621-2	2019	HD is driven by elongated cytosine-adenine-guanine (CAG) repeat (36 repeats or more) on the short arm of chromosome 4p16.3 in the Huntingtin gene (HTTg) which encode the huntingtin protein (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	52-55	huntingtin	Homo sapiens	130-140
31304621-2	2019	HD is driven by elongated cytosine-adenine-guanine (CAG) repeat (36 repeats or more) on the short arm of chromosome 4p16.3 in the Huntingtin gene (HTTg) which encode the huntingtin protein (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	52-55	huntingtin	Homo sapiens	170-180
31304621-2	2019	HD is driven by elongated cytosine-adenine-guanine (CAG) repeat (36 repeats or more) on the short arm of chromosome 4p16.3 in the Huntingtin gene (HTTg) which encode the huntingtin protein (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	52-55	huntingtin	Homo sapiens	147-150
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
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	53-63
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
31608620-10	2019	Here, we investigated if the presence of lipid vesicles altered the ability of EGCG or curcumin to modulate htt aggregation and influence the interaction of htt with lipid membranes.	Curcumin	87-95	huntingtin	Homo sapiens	108-111
31608620-11	2019	The presence of POPC or total brain lipid extract vesicles prevented the curcumin from inhibiting htt fibril formation.	1-palmitoyl-2-oleoylphosphatidylcholine	16-20	huntingtin	Homo sapiens	98-101
31608620-11	2019	The presence of POPC or total brain lipid extract vesicles prevented the curcumin from inhibiting htt fibril formation.	Curcumin	73-81	huntingtin	Homo sapiens	98-101
31608620-12	2019	In contrast, EGCG"s inhibition of htt fibril formation persisted in the presence of lipids.	epigallocatechin gallate	13-17	huntingtin	Homo sapiens	34-37
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
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
31431260-9	2019	Notably, intracellular Huntington"s disease-specific aggregates of elongated huntingtin, a well-established autophagy substrate, were significantly decreased by memantine.	Memantine	161-170	huntingtin	Homo sapiens	77-87
31632982-0	2019	The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus.	Nitrogen	83-84	huntingtin	Homo sapiens	72-82
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
31296921-1	2019	Huntington"s disease (HD) is caused by an expanded CAG trinucleotide repeat in the first exon of the huntingtin gene (HTT).	trinucleotide	55-68	huntingtin	Homo sapiens	101-111
31296921-1	2019	Huntington"s disease (HD) is caused by an expanded CAG trinucleotide repeat in the first exon of the huntingtin gene (HTT).	trinucleotide	55-68	huntingtin	Homo sapiens	118-121
31184975-0	2019	Lowering Mutant Huntingtin Using Tricyclo-DNA Antisense Oligonucleotides As a Therapeutic Approach for Huntington"s Disease.	Oligonucleotides	56-72	huntingtin	Homo sapiens	16-26
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
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
31184975-4	2019	However, reducing the expression of the huntingtin protein (HTT) using antisense oligonucleotides (ASOs) has been shown as a promising therapeutic strategy.	Oligonucleotides	81-97	huntingtin	Homo sapiens	40-50
31184975-4	2019	However, reducing the expression of the huntingtin protein (HTT) using antisense oligonucleotides (ASOs) has been shown as a promising therapeutic strategy.	Oligonucleotides	81-97	huntingtin	Homo sapiens	60-63
31184975-4	2019	However, reducing the expression of the huntingtin protein (HTT) using antisense oligonucleotides (ASOs) has been shown as a promising therapeutic strategy.	Oligonucleotides, Antisense	99-103	huntingtin	Homo sapiens	40-50
31184975-4	2019	However, reducing the expression of the huntingtin protein (HTT) using antisense oligonucleotides (ASOs) has been shown as a promising therapeutic strategy.	Oligonucleotides, Antisense	99-103	huntingtin	Homo sapiens	60-63
31184975-5	2019	In this study, we explore the therapeutic potential of ASO made of tricyclo-DNA (tcDNA), a conformationally constrained DNA analog, to silence HTT.	Oligonucleotides, Antisense	55-58	huntingtin	Homo sapiens	143-146
31184975-0	2019	Lowering Mutant Huntingtin Using Tricyclo-DNA Antisense Oligonucleotides As a Therapeutic Approach for Huntington"s Disease.	tricyclo-dna	33-45	huntingtin	Homo sapiens	16-26
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
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
31546689-0	2019	Parkinsonism with a Hint of Huntington"s from 29 CAG Repeats in HTT.	cytidylyl-3'-5'-guanosine	49-52	huntingtin	Homo sapiens	64-67
31546689-1	2019	Huntington"s disease is caused by at least 36 cytosine-adenine-guanine (CAG) repeats in an HTT gene allele, but repeat tracts in the intermediate range (27-35 repeats) also display a subtle phenotype.	cytidylyl-3'-5'-guanosine	46-70	huntingtin	Homo sapiens	91-94
31546689-1	2019	Huntington"s disease is caused by at least 36 cytosine-adenine-guanine (CAG) repeats in an HTT gene allele, but repeat tracts in the intermediate range (27-35 repeats) also display a subtle phenotype.	cytidylyl-3'-5'-guanosine	72-75	huntingtin	Homo sapiens	91-94
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
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
31893246-1	2019	Background: Huntington disease (HD) is an autosomal dominant late-onset neurodegenerative disease caused by an unstable cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin (HTT) gene.	cytidylyl-3'-5'-guanosine	120-158	huntingtin	Homo sapiens	183-193
31893246-1	2019	Background: Huntington disease (HD) is an autosomal dominant late-onset neurodegenerative disease caused by an unstable cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin (HTT) gene.	cytidylyl-3'-5'-guanosine	120-158	huntingtin	Homo sapiens	195-198
31226569-0	2019	MnFe2O4 nanoparticles accelerate the clearance of mutant huntingtin selectively through ubiquitin-proteasome system.	manganese ferrite	0-7	huntingtin	Homo sapiens	57-67
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)].	manganese ferrite	42-49	huntingtin	Homo sapiens	147-157
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)].	manganese ferrite	42-49	huntingtin	Homo sapiens	159-162
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)].	manganese ferrite	42-49	huntingtin	Homo sapiens	205-208
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
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
31226569-5	2019	UPS, rather than autophagy, was responsible for the efficient Htt(Q74) degradation facilitated by MnFe2O4 NPs.	manganese ferrite	98-105	huntingtin	Homo sapiens	62-65
31226569-6	2019	Meanwhile, we demonstrated that MnFe2O4 NPs enhanced K48-linked ubiquitination of GFP-Htt(Q74).	manganese ferrite	32-39	huntingtin	Homo sapiens	86-89
31226569-7	2019	Moreover, ubiqinlin-1, but not p62/SQSTM1, served as the ubiquitin receptor that mediated the enhanced degradation of Htt(Q74) by MnFe2O4 NPs.	manganese ferrite	130-137	huntingtin	Homo sapiens	118-121
31108174-0	2019	Pridopidine protects neurons from mutant-huntingtin toxicity via the sigma-1 receptor.	pridopidine	0-11	huntingtin	Homo sapiens	41-51
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	165-170	huntingtin	Homo sapiens	99-109
31286142-7	2019	Here, we demonstrate that a gene therapy approach based on the delivery of CYP46A1, the rate-limiting enzyme for cholesterol degradation in the brain, has a long-lasting neuroprotective effect in Huntington"s disease and counteracts multiple detrimental effects of the mutated huntingtin.	Cholesterol	113-124	huntingtin	Homo sapiens	277-287
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
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
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
30891880-8	2019	Some (CAG)n -containing genes including TBP, ATN1 and HTT modified AAO with variance ranging from 0.8% to 3.8% and tended to decrease or delay AAO.	Nitrogen	10-11	huntingtin	Homo sapiens	54-57
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
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	25-28	huntingtin	Homo sapiens	72-76
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	25-28	huntingtin	Homo sapiens	94-104
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	25-28	huntingtin	Homo sapiens	106-109
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	25-28	huntingtin	Homo sapiens	177-180
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	trinucleotide	29-42	huntingtin	Homo sapiens	72-76
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	trinucleotide	29-42	huntingtin	Homo sapiens	94-104
31358058-3	2019	HD is caused by expanded CAG trinucleotide repeats at the N-terminus of IT15 that encodes the huntingtin (HTT) protein, though the molecular mechanisms through which the mutant HTT (mHTT) exerts toxic effects remain obscure.	trinucleotide	29-42	huntingtin	Homo sapiens	106-109
31103960-2	2019	BACKGROUND: Huntington disease (HD) is caused by a mutation in the HTT gene of 36 or more CAG trinucleotide repeats.	trinucleotide	94-107	huntingtin	Homo sapiens	67-70
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
30573872-1	2019	Huntington"s disease (HD) is an autosomal dominant disorder caused by a trinucleotide expansion in the huntingtin gene.	trinucleotide	72-85	huntingtin	Homo sapiens	103-113
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.	N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide	23-31	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	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
31250621-0	2019	Cell-Based Screen Using Amyloid Mimic beta23 Expression Identifies Peucedanocoumarin III as a Novel Inhibitor of alpha-Synuclein and Huntingtin Aggregates.	Peucedanocoumarin III	67-88	huntingtin	Homo sapiens	133-143
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
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
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
31059641-1	2019	BACKGROUND: Huntington"s disease is an autosomal-dominant neurodegenerative disease caused by CAG trinucleotide repeat expansion in HTT, resulting in a mutant huntingtin protein.	cag trinucleotide	94-111	huntingtin	Homo sapiens	132-135
31059641-1	2019	BACKGROUND: Huntington"s disease is an autosomal-dominant neurodegenerative disease caused by CAG trinucleotide repeat expansion in HTT, resulting in a mutant huntingtin protein.	cag trinucleotide	94-111	huntingtin	Homo sapiens	159-169
31059641-2	2019	IONIS-HTTRx (hereafter, HTTRx) is an antisense oligonucleotide designed to inhibit HTT messenger RNA and thereby reduce concentrations of mutant huntingtin.	Oligonucleotides	47-62	huntingtin	Homo sapiens	6-9
31059641-2	2019	IONIS-HTTRx (hereafter, HTTRx) is an antisense oligonucleotide designed to inhibit HTT messenger RNA and thereby reduce concentrations of mutant huntingtin.	Oligonucleotides	47-62	huntingtin	Homo sapiens	145-155
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
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
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
30850940-0	2019	Genistein induces degradation of mutant huntingtin in fibroblasts from Huntington"s disease patients.	Genistein	0-9	huntingtin	Homo sapiens	40-50
30850940-3	2019	We recently used immortalized HEK-293 cells expressing the 1st exon of the mutant HTT gene as a cellular model of HD, and showed that the stimulation of autophagy by genistein corrected the mutant phenotype.	Genistein	166-175	huntingtin	Homo sapiens	82-85
30819925-6	2019	HAP1 interacts with huntingtin and the intracellular Ca2+ channel, inositol 1,4,5-triphosphate receptor to form a ternary complex that mediates endoplasmic reticulum (ER) Ca2+ release upon stimulation with inositol 1,4,5-triphosphate3 Loss of HAP1 prevents the formation of the ternary complex and thus l-asparaginase-mediated ER Ca2+ release.	-triphosphate3	220-234	huntingtin	Homo sapiens	20-30
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
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
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
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
30632085-6	2019	Expansion of cytosine-adenine-guanine (CAG) triplet repeats in the HTT gene results in an abnormal Htt protein.	cytosine-adenine-guanine	13-37	huntingtin	Homo sapiens	67-70
30632085-6	2019	Expansion of cytosine-adenine-guanine (CAG) triplet repeats in the HTT gene results in an abnormal Htt protein.	cytosine-adenine-guanine	13-37	huntingtin	Homo sapiens	99-102
30632085-6	2019	Expansion of cytosine-adenine-guanine (CAG) triplet repeats in the HTT gene results in an abnormal Htt protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	39-42	huntingtin	Homo sapiens	67-70
30632085-6	2019	Expansion of cytosine-adenine-guanine (CAG) triplet repeats in the HTT gene results in an abnormal Htt protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	39-42	huntingtin	Homo sapiens	99-102
30632085-8	2019	Further, excessive accumulation of the HTT gene repeats causes abnormal production of reactive oxygen species (ROS) and the ensuing mitochondrial (MT) oxidative stress in neurons.	Reactive Oxygen Species	86-109	huntingtin	Homo sapiens	39-42
30632085-8	2019	Further, excessive accumulation of the HTT gene repeats causes abnormal production of reactive oxygen species (ROS) and the ensuing mitochondrial (MT) oxidative stress in neurons.	Reactive Oxygen Species	111-114	huntingtin	Homo sapiens	39-42
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
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
30540190-0	2019	TiO2 Nanoparticles Catalyze Oxidation of Huntingtin Exon 1-Derived Peptides Impeding Aggregation: A Quantitative NMR Study of Binding and Kinetics.	titanium dioxide	0-4	huntingtin	Homo sapiens	41-51
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
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	308-318
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
30808748-1	2019	The N-terminal region of the huntingtin protein, encoded by exon-1, comprises an amphiphilic domain (httNT), a polyglutamine (Q n ) tract, and a proline-rich sequence.	Proline	145-152	huntingtin	Homo sapiens	29-39
30538129-0	2019	High-mobility group box 1 links sensing of reactive oxygen species by huntingtin to its nuclear entry.	Reactive Oxygen Species	43-66	huntingtin	Homo sapiens	70-80
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
30538129-3	2019	Huntingtin is normally retained at the endoplasmic reticulum via its N17 amphipathic alpha-helix domain but is released by oxidation of Met-8 during reactive oxygen species (ROS) stress.	met-8	136-141	huntingtin	Homo sapiens	0-10
30538129-3	2019	Huntingtin is normally retained at the endoplasmic reticulum via its N17 amphipathic alpha-helix domain but is released by oxidation of Met-8 during reactive oxygen species (ROS) stress.	Reactive Oxygen Species	149-172	huntingtin	Homo sapiens	0-10
30538129-3	2019	Huntingtin is normally retained at the endoplasmic reticulum via its N17 amphipathic alpha-helix domain but is released by oxidation of Met-8 during reactive oxygen species (ROS) stress.	Reactive Oxygen Species	174-177	huntingtin	Homo sapiens	0-10
30538129-4	2019	Huntingtin enters the nucleus via an importin beta1- and 2-dependent proline-tyrosine nuclear localization signal (PY-NLS), which has a unique intervening sequence in huntingtin.	Proline	69-76	huntingtin	Homo sapiens	0-10
30538129-4	2019	Huntingtin enters the nucleus via an importin beta1- and 2-dependent proline-tyrosine nuclear localization signal (PY-NLS), which has a unique intervening sequence in huntingtin.	Proline	69-76	huntingtin	Homo sapiens	167-177
30538129-4	2019	Huntingtin enters the nucleus via an importin beta1- and 2-dependent proline-tyrosine nuclear localization signal (PY-NLS), which has a unique intervening sequence in huntingtin.	Tyrosine	77-85	huntingtin	Homo sapiens	0-10
30538129-4	2019	Huntingtin enters the nucleus via an importin beta1- and 2-dependent proline-tyrosine nuclear localization signal (PY-NLS), which has a unique intervening sequence in huntingtin.	Tyrosine	77-85	huntingtin	Homo sapiens	167-177
30538129-7	2019	We also found that HMGB1 interacts with the huntingtin N17 region and that this interaction is enhanced by the presence of ROS and phosphorylation of critical serine residues in the N17 region.	Reactive Oxygen Species	123-126	huntingtin	Homo sapiens	44-54
30538129-7	2019	We also found that HMGB1 interacts with the huntingtin N17 region and that this interaction is enhanced by the presence of ROS and phosphorylation of critical serine residues in the N17 region.	Serine	159-165	huntingtin	Homo sapiens	44-54
30538129-8	2019	We conclude that HMGB1 is a huntingtin N17/PY-NLS ROS-dependent interactor, and this protein bridging is essential for relaying ROS sensing by huntingtin to its nuclear entry during ROS stress.	Reactive Oxygen Species	50-53	huntingtin	Homo sapiens	28-38
30538129-8	2019	We conclude that HMGB1 is a huntingtin N17/PY-NLS ROS-dependent interactor, and this protein bridging is essential for relaying ROS sensing by huntingtin to its nuclear entry during ROS stress.	Reactive Oxygen Species	50-53	huntingtin	Homo sapiens	143-153
30538129-8	2019	We conclude that HMGB1 is a huntingtin N17/PY-NLS ROS-dependent interactor, and this protein bridging is essential for relaying ROS sensing by huntingtin to its nuclear entry during ROS stress.	Reactive Oxygen Species	128-131	huntingtin	Homo sapiens	28-38
30538129-8	2019	We conclude that HMGB1 is a huntingtin N17/PY-NLS ROS-dependent interactor, and this protein bridging is essential for relaying ROS sensing by huntingtin to its nuclear entry during ROS stress.	Reactive Oxygen Species	128-131	huntingtin	Homo sapiens	143-153
30538129-8	2019	We conclude that HMGB1 is a huntingtin N17/PY-NLS ROS-dependent interactor, and this protein bridging is essential for relaying ROS sensing by huntingtin to its nuclear entry during ROS stress.	Reactive Oxygen Species	128-131	huntingtin	Homo sapiens	28-38
30538129-8	2019	We conclude that HMGB1 is a huntingtin N17/PY-NLS ROS-dependent interactor, and this protein bridging is essential for relaying ROS sensing by huntingtin to its nuclear entry during ROS stress.	Reactive Oxygen Species	128-131	huntingtin	Homo sapiens	143-153
30563778-4	2019	Eligible patients had clinical onset after age 18 years, 36 or more cytosine-adenine-guanine repeats in the huntingtin gene, motor symptoms (Unified Huntington"s Disease Rating Scale total motor score [UHDRS-TMS] >=25 points), and reduced independence (UHDRS independence score <=90%).	cytosine-adenine-guanine	68-92	huntingtin	Homo sapiens	108-118
30616867-9	2019	Antisense oligonucleotides (ASO) are the only huntingtin-lowering strategies in clinical development.	Oligonucleotides	10-26	huntingtin	Homo sapiens	46-56
30616867-9	2019	Antisense oligonucleotides (ASO) are the only huntingtin-lowering strategies in clinical development.	Oligonucleotides, Antisense	28-31	huntingtin	Homo sapiens	46-56
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
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
30419368-2	2019	It is caused by an expansion of a trinucleotide repeat in the huntingtin gene (HTT) on chromosome 4.	trinucleotide	34-47	huntingtin	Homo sapiens	62-72
30419368-2	2019	It is caused by an expansion of a trinucleotide repeat in the huntingtin gene (HTT) on chromosome 4.	trinucleotide	34-47	huntingtin	Homo sapiens	79-82
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
30540190-7	2019	Catalysis of methionine oxidation within the N-terminal domain of the huntingtin protein may potentially provide a strategy for delaying the onset of Huntington"s disease.	Methionine	13-23	huntingtin	Homo sapiens	70-80
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
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
31727211-1	2019	Huntington disease (HD) is a hereditary neurodegenerative disorder caused by an expanded cytosine-adenine-guanine triplet repeat in the huntingtin gene.	cytosine-adenine-guanine	89-113	huntingtin	Homo sapiens	136-146
30856117-0	2019	Cysteamine Protects Neurons from Mutant Huntingtin Toxicity.	Cysteamine	0-10	huntingtin	Homo sapiens	40-50
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
30594931-1	2019	BACKGROUND: Previous studies suggest that Huntingtin, the protein mutated in Huntington"s disease (HD), is required for actin based changes in cell morphology, and undergoes stimulus induced targeting to plasma membranes where it interacts with phospholipids involved in cell signaling.	Phospholipids	245-258	huntingtin	Homo sapiens	42-52
30856117-5	2019	OBJECTIVE: The objective of this study is to assess the capacity of cysteamine for neuroprotection against mutant Huntingtin in vitro using cellular models of HD, and to provide initial data regarding mechanism of action.	Cysteamine	68-78	huntingtin	Homo sapiens	114-124
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
30856117-7	2019	RESULTS: Cysteamine showed a strong neuroprotective effect (EC50 = 7.1 nM) against mutant Htt-(aa-1-586 82Q) toxicity, in a nuclear condensation cell toxicity assay.	Cysteamine	9-19	huntingtin	Homo sapiens	90-93
31381521-8	2019	However, reduction of the JHD aberrant progenitor populations can be accomplished either by targeting the canonical Notch signaling pathway or by treatment with HTT antisense oligonucleotides (ASOs).	Oligonucleotides	175-191	huntingtin	Homo sapiens	161-164
31381521-8	2019	However, reduction of the JHD aberrant progenitor populations can be accomplished either by targeting the canonical Notch signaling pathway or by treatment with HTT antisense oligonucleotides (ASOs).	Oligonucleotides, Antisense	193-197	huntingtin	Homo sapiens	161-164
30856117-8	2019	Cysteamine also rescued mitochondrial changes induced by mutant Htt.	Cysteamine	0-10	huntingtin	Homo sapiens	64-67
30856117-10	2019	Taurine and Hypotaurine, which are metabolites of cysteamine can protect neurons against Htt toxicity, but the inhibition of the enzyme converting cysteamine to hypotaurine does not block either protective activity, suggesting independent protective pathways.	Taurine	0-7	huntingtin	Homo sapiens	89-92
30856117-10	2019	Taurine and Hypotaurine, which are metabolites of cysteamine can protect neurons against Htt toxicity, but the inhibition of the enzyme converting cysteamine to hypotaurine does not block either protective activity, suggesting independent protective pathways.	hypotaurine	12-23	huntingtin	Homo sapiens	89-92
30856117-10	2019	Taurine and Hypotaurine, which are metabolites of cysteamine can protect neurons against Htt toxicity, but the inhibition of the enzyme converting cysteamine to hypotaurine does not block either protective activity, suggesting independent protective pathways.	Cysteamine	50-60	huntingtin	Homo sapiens	89-92
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
30399392-0	2019	Heterozygous huntingtin promotes cadmium neurotoxicity and neurodegeneration in striatal cells via altered metal transport and protein kinase C delta dependent oxidative stress and apoptosis signaling mechanisms.	Cadmium	33-40	huntingtin	Homo sapiens	13-23
30529228-9	2019	3-nitropropionic acid (3-NP), which is known to induce striatal degeneration, was used to induce cell death in the rat striatal cell line ST14A expressing mutant human huntingtin (Q120) or in ST14A cells expressing normal human huntingtin (Q15), in primary cultured astrocytes, and in BV2 cells.	3-nitropropionic acid	0-21	huntingtin	Homo sapiens	168-178
30529228-9	2019	3-nitropropionic acid (3-NP), which is known to induce striatal degeneration, was used to induce cell death in the rat striatal cell line ST14A expressing mutant human huntingtin (Q120) or in ST14A cells expressing normal human huntingtin (Q15), in primary cultured astrocytes, and in BV2 cells.	3-nitropropionic acid	0-21	huntingtin	Homo sapiens	228-238
30529228-9	2019	3-nitropropionic acid (3-NP), which is known to induce striatal degeneration, was used to induce cell death in the rat striatal cell line ST14A expressing mutant human huntingtin (Q120) or in ST14A cells expressing normal human huntingtin (Q15), in primary cultured astrocytes, and in BV2 cells.	3-nitropropionic acid	23-27	huntingtin	Homo sapiens	168-178
30529228-9	2019	3-nitropropionic acid (3-NP), which is known to induce striatal degeneration, was used to induce cell death in the rat striatal cell line ST14A expressing mutant human huntingtin (Q120) or in ST14A cells expressing normal human huntingtin (Q15), in primary cultured astrocytes, and in BV2 cells.	3-nitropropionic acid	23-27	huntingtin	Homo sapiens	228-238
30399392-0	2019	Heterozygous huntingtin promotes cadmium neurotoxicity and neurodegeneration in striatal cells via altered metal transport and protein kinase C delta dependent oxidative stress and apoptosis signaling mechanisms.	Metals	107-112	huntingtin	Homo sapiens	13-23
30399392-3	2019	Thus, we hypothesized that heterozygous huntingtin (HTT), responsible for the majority of cases of HD in patients, in combination with Cd exposure would cause neurotoxicity and neurodegeneration via increased intracellular accumulation of Cd and activation of oxidative stress signaling mechanisms in a mouse striatal cell line model of HD.	Cadmium	239-241	huntingtin	Homo sapiens	40-50
30399392-3	2019	Thus, we hypothesized that heterozygous huntingtin (HTT), responsible for the majority of cases of HD in patients, in combination with Cd exposure would cause neurotoxicity and neurodegeneration via increased intracellular accumulation of Cd and activation of oxidative stress signaling mechanisms in a mouse striatal cell line model of HD.	Cadmium	239-241	huntingtin	Homo sapiens	52-55
30399392-4	2019	We report that heterozygous HTT striatal cells are significantly more susceptible to Cd-induced cytotoxicity as compared to wild-type HTT cells upon exposure for 48 h. The heterozygous HTT and Cd-induced cytotoxicity led to a NADPH oxidase (NOX) mediated oxidative stress that was attenuated by exogenous antioxidants and a NOX inhibitor, apocynin.	Cadmium	85-87	huntingtin	Homo sapiens	28-31
30399392-4	2019	We report that heterozygous HTT striatal cells are significantly more susceptible to Cd-induced cytotoxicity as compared to wild-type HTT cells upon exposure for 48 h. The heterozygous HTT and Cd-induced cytotoxicity led to a NADPH oxidase (NOX) mediated oxidative stress that was attenuated by exogenous antioxidants and a NOX inhibitor, apocynin.	Cadmium	193-195	huntingtin	Homo sapiens	28-31
30399392-4	2019	We report that heterozygous HTT striatal cells are significantly more susceptible to Cd-induced cytotoxicity as compared to wild-type HTT cells upon exposure for 48 h. The heterozygous HTT and Cd-induced cytotoxicity led to a NADPH oxidase (NOX) mediated oxidative stress that was attenuated by exogenous antioxidants and a NOX inhibitor, apocynin.	acetovanillone	339-347	huntingtin	Homo sapiens	28-31
30399392-5	2019	Heterozygous HTT coupled with Cd exposure caused increased expression of protein kinase C delta (PKCdelta) and other key oxidative stress proteins levels, enhanced the activation of caspase-9 and caspase-3 mediated apoptosis, and blocked the overexpression of extracellular signal-regulated kinase (ERK).	Cadmium	30-32	huntingtin	Homo sapiens	13-16
30399392-6	2019	We observed significantly greater intracellular accumulation of Cd and reduced expression of divalent metal transporter 1 (DMT1) protein in the heterozygous HTT striatal cells upon Cd exposure.	Cadmium	64-66	huntingtin	Homo sapiens	157-160
30399392-6	2019	We observed significantly greater intracellular accumulation of Cd and reduced expression of divalent metal transporter 1 (DMT1) protein in the heterozygous HTT striatal cells upon Cd exposure.	Cadmium	181-183	huntingtin	Homo sapiens	157-160
30399392-8	2019	Collectively, these results demonstrate that heterozygous HTT exhibits greater neurotoxic properties when coupled with Cd exposure to cause cell death via caspase mediated apoptosis, altered metal transport, and modulation of ERK and PKCdelta dependent oxidative signaling mechanisms.	Cadmium	119-121	huntingtin	Homo sapiens	58-61
30399392-8	2019	Collectively, these results demonstrate that heterozygous HTT exhibits greater neurotoxic properties when coupled with Cd exposure to cause cell death via caspase mediated apoptosis, altered metal transport, and modulation of ERK and PKCdelta dependent oxidative signaling mechanisms.	Metals	191-196	huntingtin	Homo sapiens	58-61
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
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
30679892-1	2018	AIM: Huntington"s disease (HD) is an inherited disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) that ultimately leads to neurodegeneration.	cytosine-adenine-guanine	81-105	huntingtin	Homo sapiens	127-137
30679892-1	2018	AIM: Huntington"s disease (HD) is an inherited disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) that ultimately leads to neurodegeneration.	cytosine-adenine-guanine	81-105	huntingtin	Homo sapiens	144-147
30679892-1	2018	AIM: Huntington"s disease (HD) is an inherited disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) that ultimately leads to neurodegeneration.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	107-110	huntingtin	Homo sapiens	127-137
30679892-1	2018	AIM: Huntington"s disease (HD) is an inherited disease caused by an expansion of cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) that ultimately leads to neurodegeneration.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	107-110	huntingtin	Homo sapiens	144-147
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
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
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
30256717-6	2018	We additionally observed dysregulated reactive oxygen species (ROS)-dependent huntingtin localization to nuclear speckles in HD cells.	Reactive Oxygen Species	38-61	huntingtin	Homo sapiens	78-88
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
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
30256717-6	2018	We additionally observed dysregulated reactive oxygen species (ROS)-dependent huntingtin localization to nuclear speckles in HD cells.	Reactive Oxygen Species	63-66	huntingtin	Homo sapiens	78-88
30252478-0	2018	Dynamics of the Proline-Rich C-Terminus of Huntingtin Exon-1 Fibrils.	Proline	16-23	huntingtin	Homo sapiens	43-53
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
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
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
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
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
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
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
30007561-1	2018	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	76-79	huntingtin	Homo sapiens	118-128
30007561-1	2018	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin gene.	trinucleotide	80-93	huntingtin	Homo sapiens	118-128
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
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
29979597-0	2018	Calmidazolium Chloride and Its Complex with Serum Albumin Prevent Huntingtin Exon1 Aggregation.	calmidazolium	0-22	huntingtin	Homo sapiens	66-76
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
30069866-4	2018	The N-terminal part of VCP (Cdc48_N domain) interacts with the N-terminal 17-amino acid region of Huntingtin-exon1.	17-amino acid	74-87	huntingtin	Homo sapiens	98-108
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
30002810-8	2018	The same results were obtained in HEK293 cells expressing N-terminal of mutant huntingtin containing 160 CAG repeats.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	105-108	huntingtin	Homo sapiens	79-89
29898922-1	2018	Huntington"s disease (HD) is a rare autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat (TNR) expansion within the HTT gene.	cytosine-adenine-guanine	94-118	huntingtin	Homo sapiens	173-176
29898922-1	2018	Huntington"s disease (HD) is a rare autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat (TNR) expansion within the HTT gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	120-123	huntingtin	Homo sapiens	173-176
29898922-1	2018	Huntington"s disease (HD) is a rare autosomal dominant neurodegenerative disorder caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat (TNR) expansion within the HTT gene.	trinucleotide	125-138	huntingtin	Homo sapiens	173-176
29684586-2	2018	The precise mechanisms of HD progression are poorly understood; however, it is known that there is an expansion of the trinucleotide cytosine-adenine-guanine (CAG) repeat in the Huntingtin gene.	trinucleotide cytosine-adenine-guanine	119-157	huntingtin	Homo sapiens	178-188
29684586-2	2018	The precise mechanisms of HD progression are poorly understood; however, it is known that there is an expansion of the trinucleotide cytosine-adenine-guanine (CAG) repeat in the Huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	159-162	huntingtin	Homo sapiens	178-188
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
29506378-5	2018	One of those, furamidine, reduces the level of binding of HTT mRNA to MID1 and other target proteins in vitro.	furamidine	14-24	huntingtin	Homo sapiens	58-61
28532681-0	2018	Resveratrol protects neuronal-like cells expressing mutant Huntingtin from dopamine toxicity by rescuing ATG4-mediated autophagosome formation.	Resveratrol	0-11	huntingtin	Homo sapiens	59-69
28532681-0	2018	Resveratrol protects neuronal-like cells expressing mutant Huntingtin from dopamine toxicity by rescuing ATG4-mediated autophagosome formation.	Dopamine	75-83	huntingtin	Homo sapiens	59-69
28532681-3	2018	We have previously shown that dopamine-induced oxidative stress triggers apoptotic cell death in dopaminergic neuroblastoma SH-SY5Y cells hyper-expressing the mutant polyQ Huntingtin (polyQ-Htt) protein.	Dopamine	30-38	huntingtin	Homo sapiens	172-182
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
29506378-7	2018	Importantly, furamidine also decreases the protein level of HTT in a HD cell line model.	furamidine	13-23	huntingtin	Homo sapiens	60-63
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
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
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
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
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
29858077-1	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
29802276-2	2018	Huntington disease (HD) is a dominantly inherited neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	99-102	huntingtin	Homo sapiens	131-141
29802276-2	2018	Huntington disease (HD) is a dominantly inherited neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	99-102	huntingtin	Homo sapiens	143-146
29802276-2	2018	Huntington disease (HD) is a dominantly inherited neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin (HTT) gene.	trinucleotide	103-116	huntingtin	Homo sapiens	131-141
29802276-2	2018	Huntington disease (HD) is a dominantly inherited neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin (HTT) gene.	trinucleotide	103-116	huntingtin	Homo sapiens	143-146
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
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
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
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.	Proline	133-140	huntingtin	Homo sapiens	14-24
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
29743609-3	2018	In the current study, we determined whether total Htt protein (normal plus mutant; "tHtt") could be reliably measured in human saliva, a body fluid that is much more accessible compared to cerebral spinal fluid or even blood, and whether salivary levels of tHtt were clinically meaningful.	thtt	84-88	huntingtin	Homo sapiens	50-53
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
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
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
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
29377621-2	2018	The cytosine-adenine-guanine (CAG) triplet expansion encoding glutamine present in the protein huntingtin (Htt), produces widespread neuronal and glial pathology.	cytosine-adenine-guanine	4-28	huntingtin	Homo sapiens	95-105
29218782-2	2018	In 1993, a CAG trinucleotide repeat expansion in the coding region of the huntingtin (HTT) gene was identified as the cause of this disorder.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	11-14	huntingtin	Homo sapiens	74-84
29218782-2	2018	In 1993, a CAG trinucleotide repeat expansion in the coding region of the huntingtin (HTT) gene was identified as the cause of this disorder.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	11-14	huntingtin	Homo sapiens	86-89
29218782-2	2018	In 1993, a CAG trinucleotide repeat expansion in the coding region of the huntingtin (HTT) gene was identified as the cause of this disorder.	trinucleotide	15-28	huntingtin	Homo sapiens	74-84
29218782-2	2018	In 1993, a CAG trinucleotide repeat expansion in the coding region of the huntingtin (HTT) gene was identified as the cause of this disorder.	trinucleotide	15-28	huntingtin	Homo sapiens	86-89
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
29291624-2	2018	It is caused by abnormally large trinucleotide cytosine-adenine-guanine (CAG) repeat expansions on exon 1 of the Huntingtin gene.	trinucleotide cytosine-adenine-guanine	33-71	huntingtin	Homo sapiens	113-123
29291624-2	2018	It is caused by abnormally large trinucleotide cytosine-adenine-guanine (CAG) repeat expansions on exon 1 of the Huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	73-76	huntingtin	Homo sapiens	113-123
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
29377621-2	2018	The cytosine-adenine-guanine (CAG) triplet expansion encoding glutamine present in the protein huntingtin (Htt), produces widespread neuronal and glial pathology.	cytosine-adenine-guanine	4-28	huntingtin	Homo sapiens	107-110
29377621-2	2018	The cytosine-adenine-guanine (CAG) triplet expansion encoding glutamine present in the protein huntingtin (Htt), produces widespread neuronal and glial pathology.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	30-33	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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	30-33	huntingtin	Homo sapiens	107-110
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
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
29620999-0	2018	Dose-Dependent Lowering of Mutant Huntingtin Using Antisense Oligonucleotides in Huntington Disease Patients.	Oligonucleotides	61-77	huntingtin	Homo sapiens	34-44
29620999-2	2018	The results from this Ionis trial have gained much attention from the patient community and the oligonucleotide therapeutics field, since it is the first trial targeting the cause of HD, namely the mutant huntingtin protein, using antisense oligonucleotides (ASOs).	Oligonucleotides	241-257	huntingtin	Homo sapiens	205-215
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
29651271-1	2018	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expansion mutation of the cytosine-adenine-guanine (CAG) trinucleotide in the HTT gene.	cytosine-adenine-guanine (cag) trinucleotide	97-141	huntingtin	Homo sapiens	149-152
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
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
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
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
29358329-5	2018	We confirm that profilin achieves its cellular effects through direct binding to the C-terminal proline-rich region of Htt-NTFs.	Proline	96-103	huntingtin	Homo sapiens	119-122
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.	polyproline	249-260	huntingtin	Homo sapiens	160-163
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
29435951-5	2018	Both level of mutated huntingtin and number of aggregates were significantly decreased in genistein-treated HD cell model.	Genistein	90-99	huntingtin	Homo sapiens	22-32
29440125-0	2018	Small interfering RNAs based on huntingtin trinucleotide repeats are highly toxic to cancer cells.	trinucleotide	43-56	huntingtin	Homo sapiens	32-42
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
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
29435951-7	2018	Autophagy was up-regulated while inhibition of lysosomal functions by chloroquine impaired the genistein-mediated degradation of the mutated huntingtin aggregates.	Chloroquine	70-81	huntingtin	Homo sapiens	141-151
29435951-7	2018	Autophagy was up-regulated while inhibition of lysosomal functions by chloroquine impaired the genistein-mediated degradation of the mutated huntingtin aggregates.	Genistein	95-104	huntingtin	Homo sapiens	141-151
29134321-2	2018	Huntington"s disease (HD) is an inherited NDD caused by autosomal-dominant expanded CAG trinucleotide repeat mutation in the gene coding for Huntingtin (Htt).	trinucleotide	88-101	huntingtin	Homo sapiens	141-151
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
29535594-3	2018	Therapeutic strategies used to date to silence the expression of mutant HTT include antisense oligonucleotides, RNA interference-based approaches and, recently, genome editing with the CRISPR/Cas9 system.	Oligonucleotides	94-110	huntingtin	Homo sapiens	72-75
29670796-1	2018	Huntington"s disease (HD) is an inherited, progressive, and neurodegenerative neuropsychiatric disorder caused by the expansion of cytosine-adenine-guanine (CAG) trinucleotide in Interested Transcript (IT) 15 gene on chromosome 4.	cytosine-adenine-guanine (cag) trinucleotide	131-175	huntingtin	Homo sapiens	179-208
29366651-0	2018	Degradation of huntingtin mediated by a hybrid molecule composed of IAP antagonist linked to phenyldiazenyl benzothiazole derivative.	phenyldiazenyl benzothiazole	93-121	huntingtin	Homo sapiens	15-25
29366651-2	2018	We previously reported protein knockdown of Htt by using hybrid small molecules (Htt degraders) consisting of BE04, a ligand of ubiquitin ligase (E3), linked to probes for protein aggregates.	be04	110-114	huntingtin	Homo sapiens	44-47
29366651-2	2018	We previously reported protein knockdown of Htt by using hybrid small molecules (Htt degraders) consisting of BE04, a ligand of ubiquitin ligase (E3), linked to probes for protein aggregates.	be04	110-114	huntingtin	Homo sapiens	81-84
29422655-5	2018	Using cellular and animal models of Huntington"s disease, we show here that the overexpression of cytotoxic mutant huntingtin protein induces glycogen synthesis in the neurons by activating glycogen synthase and the overexpressed glycogen synthase protected neurons from the cytotoxicity of the mutant huntingtin.	Glycogen	142-150	huntingtin	Homo sapiens	115-125
29422655-5	2018	Using cellular and animal models of Huntington"s disease, we show here that the overexpression of cytotoxic mutant huntingtin protein induces glycogen synthesis in the neurons by activating glycogen synthase and the overexpressed glycogen synthase protected neurons from the cytotoxicity of the mutant huntingtin.	Glycogen	142-150	huntingtin	Homo sapiens	302-312
29422655-8	2018	We also show that the increased neuronal glycogen inhibits the aggregation of mutant huntingtin, and thus could directly contribute to its clearance.	Glycogen	41-49	huntingtin	Homo sapiens	85-95
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
29134321-2	2018	Huntington"s disease (HD) is an inherited NDD caused by autosomal-dominant expanded CAG trinucleotide repeat mutation in the gene coding for Huntingtin (Htt).	trinucleotide	88-101	huntingtin	Homo sapiens	153-156
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
29399649-0	2018	Sphingomyelin and GM1 Influence Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.	Sphingomyelins	0-13	huntingtin	Homo sapiens	32-42
29399649-0	2018	Sphingomyelin and GM1 Influence Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.	G(M1) Ganglioside	18-21	huntingtin	Homo sapiens	32-42
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
29399649-7	2018	The addition of either SM or GM1 decreased htt insertion into the lipid monolayers.	Sphingomyelins	23-25	huntingtin	Homo sapiens	43-46
29399649-7	2018	The addition of either SM or GM1 decreased htt insertion into the lipid monolayers.	G(M1) Ganglioside	29-32	huntingtin	Homo sapiens	43-46
29399649-9	2018	Pure TBLE bilayers and TBLE bilayers enriched with GM1 developed regions of roughened, granular morphologies upon exposure to htt-exon1, but plateau-like domains with a smoother appearance formed in bilayers enriched with SM.	tble	23-27	huntingtin	Homo sapiens	126-129
29399649-9	2018	Pure TBLE bilayers and TBLE bilayers enriched with GM1 developed regions of roughened, granular morphologies upon exposure to htt-exon1, but plateau-like domains with a smoother appearance formed in bilayers enriched with SM.	G(M1) Ganglioside	51-54	huntingtin	Homo sapiens	126-129
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.	mhtt	106-110	huntingtin	Homo sapiens	84-94
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
29335600-4	2018	Yet, little is known about how mutant huntingtin may affect phospholipids membrane fluidity.	Phospholipids	60-73	huntingtin	Homo sapiens	38-48
29212816-1	2018	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene (HTT).	trinucleotide	84-97	huntingtin	Homo sapiens	112-122
29212816-1	2018	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene (HTT).	trinucleotide	84-97	huntingtin	Homo sapiens	129-132
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
30025395-0	2018	Midazolam Enhances Mutant Huntingtin Protein Accumulation via Impairment of Autophagic Degradation In Vitro.	Midazolam	0-9	huntingtin	Homo sapiens	26-36
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.	trinucleotide	50-63	huntingtin	Homo sapiens	96-106
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
30025395-10	2018	Midazolam led to a 20% decrease in GFP-Htt (Q74)-PC12 cell viability, which could be abrogated by overexpression of cathepsin D.	Midazolam	0-9	huntingtin	Homo sapiens	39-42
30025395-11	2018	CONCLUSIONS: Midazolam increased mHtt levels and decreased Htt (Q74)-PC12 cell viability via impairment of autophagic degradation, which could be restored by overexpression of cathepsin D.	Midazolam	13-22	huntingtin	Homo sapiens	34-37
30409256-1	2018	Huntington"s disease (HD) is a rare monogenic neurodegenerative disorder caused by a trinucleotide CAG repeat expansion in the huntingtin gene resulting in the formation of intranuclear inclusions of mutated huntingtin.	trinucleotide	85-98	huntingtin	Homo sapiens	127-137
28817209-1	2018	Huntington"s disease (HD) is a fully penetrant neurodegenerative disease caused by a dominantly inherited CAG trinucleotide repeat expansion in the huntingtin gene on chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	106-109	huntingtin	Homo sapiens	148-158
28817209-1	2018	Huntington"s disease (HD) is a fully penetrant neurodegenerative disease caused by a dominantly inherited CAG trinucleotide repeat expansion in the huntingtin gene on chromosome 4.	trinucleotide	110-123	huntingtin	Homo sapiens	148-158
30459039-2	2018	Since the identification of an abnormal expansion of a trinucleotide repeat tract in the huntingtin gene as the underlying genetic defect, a broad range of transgenic animal models of the disease has become available and these have helped to unravel the relevant molecular pathways in unprecedented detail.	trinucleotide	55-68	huntingtin	Homo sapiens	89-99
30409256-1	2018	Huntington"s disease (HD) is a rare monogenic neurodegenerative disorder caused by a trinucleotide CAG repeat expansion in the huntingtin gene resulting in the formation of intranuclear inclusions of mutated huntingtin.	trinucleotide	85-98	huntingtin	Homo sapiens	208-218
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
29856033-4	2018	Huntington"s disease (HD), which is caused by a CAG repeat expansion in exon 1 of the huntingtin (HTT) gene and leads to the pathogenic expansion of a polyglutamine (PolyQ ) tract in the N terminus of the huntingtin protein (Htt), is a prime candidate for ASO therapy.State-of-the art translational science techniques can be applied to the development of an ASO targeting HTT RNA, allowing for a data-driven, stepwise progression through the drug development process.	Oligonucleotides, Antisense	256-259	huntingtin	Homo sapiens	86-96
29856033-4	2018	Huntington"s disease (HD), which is caused by a CAG repeat expansion in exon 1 of the huntingtin (HTT) gene and leads to the pathogenic expansion of a polyglutamine (PolyQ ) tract in the N terminus of the huntingtin protein (Htt), is a prime candidate for ASO therapy.State-of-the art translational science techniques can be applied to the development of an ASO targeting HTT RNA, allowing for a data-driven, stepwise progression through the drug development process.	Oligonucleotides, Antisense	256-259	huntingtin	Homo sapiens	98-101
29856033-4	2018	Huntington"s disease (HD), which is caused by a CAG repeat expansion in exon 1 of the huntingtin (HTT) gene and leads to the pathogenic expansion of a polyglutamine (PolyQ ) tract in the N terminus of the huntingtin protein (Htt), is a prime candidate for ASO therapy.State-of-the art translational science techniques can be applied to the development of an ASO targeting HTT RNA, allowing for a data-driven, stepwise progression through the drug development process.	Oligonucleotides, Antisense	256-259	huntingtin	Homo sapiens	205-215
29856033-4	2018	Huntington"s disease (HD), which is caused by a CAG repeat expansion in exon 1 of the huntingtin (HTT) gene and leads to the pathogenic expansion of a polyglutamine (PolyQ ) tract in the N terminus of the huntingtin protein (Htt), is a prime candidate for ASO therapy.State-of-the art translational science techniques can be applied to the development of an ASO targeting HTT RNA, allowing for a data-driven, stepwise progression through the drug development process.	Oligonucleotides, Antisense	256-259	huntingtin	Homo sapiens	225-228
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
30587076-8	2018	This study highlights that the mutant HTT expansion resulted in depletion of cellular ATP concentration and reduced rates of extracellular nucleotide breakdown.	Adenosine Triphosphate	86-89	huntingtin	Homo sapiens	38-41
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
29225330-1	2017	Huntington disease (HD) is a severe neuropsychiatric disorder caused by a cytosine-adenine-guanine (CAG) repeat expansion in the HTT gene.	cytosine-adenine-guanine	74-98	huntingtin	Homo sapiens	129-132
29225330-1	2017	Huntington disease (HD) is a severe neuropsychiatric disorder caused by a cytosine-adenine-guanine (CAG) repeat expansion in the HTT gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	100-103	huntingtin	Homo sapiens	129-132
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
29209494-6	2017	A popular line of research employs siRNA or antisense oligonucleotides (ASO) to knock down mutant Huntingtin mRNA (mHTT).	Oligonucleotides	54-70	huntingtin	Homo sapiens	98-108
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
29209494-6	2017	A popular line of research employs siRNA or antisense oligonucleotides (ASO) to knock down mutant Huntingtin mRNA (mHTT).	Oligonucleotides, Antisense	72-75	huntingtin	Homo sapiens	98-108
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	102-105	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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	102-105	huntingtin	Homo sapiens	183-193
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.	trinucleotide	106-119	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.	trinucleotide	106-119	huntingtin	Homo sapiens	183-193
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
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
28937758-0	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
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
29066943-2	2017	We have previously demonstrated that spliceosome-mediated trans-splicing is a viable molecular strategy to specifically reduce and repair mutant HTT (mtHTT).	mthtt	150-155	huntingtin	Homo sapiens	145-148
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
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	122-125	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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	122-125	huntingtin	Homo sapiens	163-166
29889077-2	2018	The Huntingtin gene (HTT) carries a polymorphic trinucleotide expansion of CAGs in exon 1 that ranges from 9 to 35 in the non-HD affected population.	trinucleotide	48-61	huntingtin	Homo sapiens	4-14
29889077-2	2018	The Huntingtin gene (HTT) carries a polymorphic trinucleotide expansion of CAGs in exon 1 that ranges from 9 to 35 in the non-HD affected population.	trinucleotide	48-61	huntingtin	Homo sapiens	21-24
30103339-1	2018	BACKGROUND: Huntington"s disease is a late onset neurological disorder caused by a trinucleotide CAG repeat expansion mutation in the HTT gene encoding for the protein huntingtin.	trinucleotide	83-96	huntingtin	Homo sapiens	134-137
30103339-1	2018	BACKGROUND: Huntington"s disease is a late onset neurological disorder caused by a trinucleotide CAG repeat expansion mutation in the HTT gene encoding for the protein huntingtin.	trinucleotide	83-96	huntingtin	Homo sapiens	168-178
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).	trinucleotide	94-107	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).	trinucleotide	94-107	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).	trinucleotide	94-107	huntingtin	Homo sapiens	212-215
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
30452421-6	2018	Improving understanding of HTT expression and control may also uncover novel therapeutic approaches for HD through the development of methods to modulate mHTT levels.	mhtt	154-158	huntingtin	Homo sapiens	27-30
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
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
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
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
28920889-3	2017	Huntingtin-lowering strategies include antisense oligonucleotides and RNA interference targeting mRNA, and zinc finger transcriptional repressors and CRISPR-Cas9 methods aiming to reduce transcription by targeting DNA.	Oligonucleotides	49-65	huntingtin	Homo sapiens	0-10
28920889-4	2017	An intrathecally delivered antisense oligonucleotide that aims to lower huntingtin is now well into its first human clinical trial, with other antisense oligonucleotides expected to enter trials in the next 1-2 years and virally delivered RNA interference and zinc finger transcriptional repressors in advanced testing in animal models.	Oligonucleotides	37-52	huntingtin	Homo sapiens	72-82
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
29089980-2	2017	HD is caused by a trinucleotide (CAG) repeat expansion in the gene encoding for huntingtin.	trinucleotide	18-31	huntingtin	Homo sapiens	80-90
29089980-2	2017	HD is caused by a trinucleotide (CAG) repeat expansion in the gene encoding for huntingtin.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	80-90
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
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).	cag-tri-nucleotide	86-104	huntingtin	Homo sapiens	162-172
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
28789621-1	2017	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant disorder, typically characterized by chorea due to a trinucleotide repeat expansion in the HTT gene, although the clinical manifestations of patients with juvenile HD (JHD) are atypical.	trinucleotide	116-129	huntingtin	Homo sapiens	154-157
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
28841744-4	2017	The mutation induces a polyglutamine expansion in the huntingtin protein (HTT).	polyglutamine	23-36	huntingtin	Homo sapiens	54-64
28733489-5	2017	beta-Amyloid, tau, alpha-synuclein and huntingtin are shown to be involved in increased production of reactive oxygen species, which can be generated in mitochondria or can target this organelle.	Reactive Oxygen Species	102-125	huntingtin	Homo sapiens	39-49
28841744-4	2017	The mutation induces a polyglutamine expansion in the huntingtin protein (HTT).	polyglutamine	23-36	huntingtin	Homo sapiens	74-77
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	93-103
27940602-1	2017	Huntington"s disease is a late-onset neurodegenerative disease caused by a CAG trinucleotide repeat in the gene encoding the huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	75-78	huntingtin	Homo sapiens	125-135
27940602-1	2017	Huntington"s disease is a late-onset neurodegenerative disease caused by a CAG trinucleotide repeat in the gene encoding the huntingtin protein.	trinucleotide	79-92	huntingtin	Homo sapiens	125-135
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
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
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
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
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
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.	trinucleotide	87-100	huntingtin	Homo sapiens	139-149
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
28900094-2	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
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
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.	trinucleotide	87-100	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.	trinucleotide	87-100	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	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
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
28638078-5	2017	Using drug screening in C. elegans nematodes with neuronal expression of human exon-1 huntingtin (128Q), we found that 3ss-Methoxy-Pregnenolone (MAP4343), 17ss-oestradiol (17ssE2) and 12 flavonoids including isoquercitrin promote neuronal function in 128Q nematodes.	3ss-methoxy-pregnenolone	119-143	huntingtin	Homo sapiens	86-96
28638078-5	2017	Using drug screening in C. elegans nematodes with neuronal expression of human exon-1 huntingtin (128Q), we found that 3ss-Methoxy-Pregnenolone (MAP4343), 17ss-oestradiol (17ssE2) and 12 flavonoids including isoquercitrin promote neuronal function in 128Q nematodes.	17ss-oestradiol	155-170	huntingtin	Homo sapiens	86-96
28638078-5	2017	Using drug screening in C. elegans nematodes with neuronal expression of human exon-1 huntingtin (128Q), we found that 3ss-Methoxy-Pregnenolone (MAP4343), 17ss-oestradiol (17ssE2) and 12 flavonoids including isoquercitrin promote neuronal function in 128Q nematodes.	17sse2	172-178	huntingtin	Homo sapiens	86-96
28638078-5	2017	Using drug screening in C. elegans nematodes with neuronal expression of human exon-1 huntingtin (128Q), we found that 3ss-Methoxy-Pregnenolone (MAP4343), 17ss-oestradiol (17ssE2) and 12 flavonoids including isoquercitrin promote neuronal function in 128Q nematodes.	Flavonoids	187-197	huntingtin	Homo sapiens	86-96
28638078-5	2017	Using drug screening in C. elegans nematodes with neuronal expression of human exon-1 huntingtin (128Q), we found that 3ss-Methoxy-Pregnenolone (MAP4343), 17ss-oestradiol (17ssE2) and 12 flavonoids including isoquercitrin promote neuronal function in 128Q nematodes.	isoquercitrin	208-221	huntingtin	Homo sapiens	86-96
28674491-1	2017	Huntington"s disease (HD) is an autosomal dominantly inherited neurodegenerative disorder caused by expanded CAG trinucleotide repeats (&gt;36) in exon 1 of HTT gene that encodes huntingtin protein.	trinucleotide	113-126	huntingtin	Homo sapiens	157-160
28674491-1	2017	Huntington"s disease (HD) is an autosomal dominantly inherited neurodegenerative disorder caused by expanded CAG trinucleotide repeats (&gt;36) in exon 1 of HTT gene that encodes huntingtin protein.	trinucleotide	113-126	huntingtin	Homo sapiens	179-189
27740685-1	2017	Huntington disease (HD) is a late onset ultimately fatal neurodegenerative disorder caused by a cytosine-adenine-guanine ( CAG) triplet repeat expansion in the Huntingtin gene which was discovered in 1993.	cytosine-adenine-guanine	96-120	huntingtin	Homo sapiens	160-170
28585930-2	2017	Recently, we showed that both relatively short and relatively long cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) are associated with an increased risk of lifetime depression.	cytosine-adenine-guanine	67-91	huntingtin	Homo sapiens	113-123
28585930-2	2017	Recently, we showed that both relatively short and relatively long cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) are associated with an increased risk of lifetime depression.	cytosine-adenine-guanine	67-91	huntingtin	Homo sapiens	130-133
28585930-2	2017	Recently, we showed that both relatively short and relatively long cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) are associated with an increased risk of lifetime depression.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	93-96	huntingtin	Homo sapiens	113-123
28585930-2	2017	Recently, we showed that both relatively short and relatively long cytosine-adenine-guanine (CAG) repeats in the huntingtin gene (HTT) are associated with an increased risk of lifetime depression.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	93-96	huntingtin	Homo sapiens	130-133
28590448-1	2017	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat encoding an abnormally long polyglutamine tract (PolyQ) in the huntingtin (Htt) protein.	trinucleotide	110-123	huntingtin	Homo sapiens	194-204
28590448-1	2017	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat encoding an abnormally long polyglutamine tract (PolyQ) in the huntingtin (Htt) protein.	trinucleotide	110-123	huntingtin	Homo sapiens	206-209
27740685-1	2017	Huntington disease (HD) is a late onset ultimately fatal neurodegenerative disorder caused by a cytosine-adenine-guanine ( CAG) triplet repeat expansion in the Huntingtin gene which was discovered in 1993.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	123-126	huntingtin	Homo sapiens	160-170
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
28377290-6	2017	HD is one of the most common tandem repeat disorders and is caused by a trinucleotide (CAG) repeat expansion, encoding an extended polyglutamine tract in the huntingtin protein.	trinucleotide	72-85	huntingtin	Homo sapiens	158-168
28377290-6	2017	HD is one of the most common tandem repeat disorders and is caused by a trinucleotide (CAG) repeat expansion, encoding an extended polyglutamine tract in the huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	87-90	huntingtin	Homo sapiens	158-168
28334749-3	2017	HD is caused by expansion of the CAG trinucleotide repeat region in exon 1 of the Huntingtin gene (HTT), leading to the formation of mutant HTT transcripts (muHTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	82-92
28334749-3	2017	HD is caused by expansion of the CAG trinucleotide repeat region in exon 1 of the Huntingtin gene (HTT), leading to the formation of mutant HTT transcripts (muHTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	99-102
28334749-3	2017	HD is caused by expansion of the CAG trinucleotide repeat region in exon 1 of the Huntingtin gene (HTT), leading to the formation of mutant HTT transcripts (muHTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	140-143
28334749-3	2017	HD is caused by expansion of the CAG trinucleotide repeat region in exon 1 of the Huntingtin gene (HTT), leading to the formation of mutant HTT transcripts (muHTT).	trinucleotide	37-50	huntingtin	Homo sapiens	82-92
28334749-3	2017	HD is caused by expansion of the CAG trinucleotide repeat region in exon 1 of the Huntingtin gene (HTT), leading to the formation of mutant HTT transcripts (muHTT).	trinucleotide	37-50	huntingtin	Homo sapiens	99-102
28334749-3	2017	HD is caused by expansion of the CAG trinucleotide repeat region in exon 1 of the Huntingtin gene (HTT), leading to the formation of mutant HTT transcripts (muHTT).	trinucleotide	37-50	huntingtin	Homo sapiens	140-143
28334749-7	2017	We herein present a novel strategy for HD treatment using oligonucleotides (ONs) directly targeting the HTT trinucleotide repeat DNA.	Oligonucleotides	58-74	huntingtin	Homo sapiens	104-107
28334749-7	2017	We herein present a novel strategy for HD treatment using oligonucleotides (ONs) directly targeting the HTT trinucleotide repeat DNA.	Oligonucleotides	76-79	huntingtin	Homo sapiens	104-107
28334749-7	2017	We herein present a novel strategy for HD treatment using oligonucleotides (ONs) directly targeting the HTT trinucleotide repeat DNA.	trinucleotide	108-121	huntingtin	Homo sapiens	104-107
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
28413881-4	2017	Here, with the rigorous study of molecular dynamics simulations, we explored the most possible structures of HTT-N17 in both dodecylphosphocholine (DPC) micelles and aqueous solution, using three commonly applied force fields (OPLS-AA/L, CHARMM36, and AMBER99sb*-ILDNP) to examine the underlying molecular mechanisms and rule out potential artifacts.	dodecylphosphocholine	125-146	huntingtin	Homo sapiens	109-112
28413881-4	2017	Here, with the rigorous study of molecular dynamics simulations, we explored the most possible structures of HTT-N17 in both dodecylphosphocholine (DPC) micelles and aqueous solution, using three commonly applied force fields (OPLS-AA/L, CHARMM36, and AMBER99sb*-ILDNP) to examine the underlying molecular mechanisms and rule out potential artifacts.	dodecylphosphocholine	148-151	huntingtin	Homo sapiens	109-112
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
28499347-4	2017	RESULTS: Rat pheochromocytoma (PC12) cells containing a stably integrated, doxycycline-inducible, eGFP-tagged N-terminal human Htt fragment with an expanded polyQ domain were used to analyse gene expression changes at different stages of mutant Htt aggregation.	Doxycycline	75-86	huntingtin	Homo sapiens	127-130
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
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
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
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
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
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
28356891-2	2017	Trehalose induces abundant autophagy in cultured cells and also reduces the rate of aggregation of the huntingtin protein in the animal model of Huntington disease, a chronic neurological disease in humans.	Trehalose	0-9	huntingtin	Homo sapiens	103-113
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
27104782-9	2017	CONCLUSIONS: 11C-choline-PET/CT-guided HTT is safe and effective in the treatment of LN relapses of prostate cancer in previously treated patients.	methyl carbon-11 choline	13-24	huntingtin	Homo sapiens	39-42
27870408-1	2017	Huntington disease is a neurodegenerative disorder caused by a gene (HTT) with a unique feature of trinucleotide repeats ranging from 10 to 35 in healthy people; when expanded beyond 39 repeats, Huntington disease develops.	trinucleotide	99-112	huntingtin	Homo sapiens	69-72
28085263-7	2017	Such in-depth structural study of Htt presents a number of unique challenges: the long homopolymeric polyQ tract contains nearly identical residues, exon 1 displays a high degree of conformational flexibility leading to a scaling of the NMR chemical shift dispersion, and a large portion of the backbone amide groups are solvent-exposed leading to fast hydrogen exchange and causing extensive line broadening.	Amides	304-309	huntingtin	Homo sapiens	34-37
28085263-7	2017	Such in-depth structural study of Htt presents a number of unique challenges: the long homopolymeric polyQ tract contains nearly identical residues, exon 1 displays a high degree of conformational flexibility leading to a scaling of the NMR chemical shift dispersion, and a large portion of the backbone amide groups are solvent-exposed leading to fast hydrogen exchange and causing extensive line broadening.	Hydrogen	353-361	huntingtin	Homo sapiens	34-37
27104782-1	2017	OBJECTIVE: To report the 3-year toxicity and outcomes of carbon 11 (11C)-choline-positron emission tomography (PET)/computed tomography (CT)-guided radiotherapy (RT), delivered via helical tomotherapy (HTT; Tomotherapy  Hi-Art II  Treatment System, Accuray Inc., Sunnyvale, CA, USA) after lymph node (LN) relapses in patients with prostate cancer.	carbon 11 (11c)	57-72	huntingtin	Homo sapiens	202-205
27104782-1	2017	OBJECTIVE: To report the 3-year toxicity and outcomes of carbon 11 (11C)-choline-positron emission tomography (PET)/computed tomography (CT)-guided radiotherapy (RT), delivered via helical tomotherapy (HTT; Tomotherapy  Hi-Art II  Treatment System, Accuray Inc., Sunnyvale, CA, USA) after lymph node (LN) relapses in patients with prostate cancer.	Choline	73-80	huntingtin	Homo sapiens	202-205
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
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
28265888-1	2017	Huntington disease (HD) is an autosomal dominant neurodegenerative condition caused by a CAG trinucleotide expansion in the huntingtin gene.	trinucleotide	93-106	huntingtin	Homo sapiens	124-134
28205498-2	2017	HD pathology is the result of an extended chain of CAG (cytosine, adenine, guanine) trinucleotide repetitions in the HTT gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	51-54	huntingtin	Homo sapiens	117-120
28205498-2	2017	HD pathology is the result of an extended chain of CAG (cytosine, adenine, guanine) trinucleotide repetitions in the HTT gene.	cytosine, adenine, guanine) trinucleotide	56-97	huntingtin	Homo sapiens	117-120
28947125-1	2017	Huntington disease (HD) is caused by a CAG trinucleotide expansion in the huntingtin gene.	trinucleotide	43-56	huntingtin	Homo sapiens	74-84
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	25-28	huntingtin	Homo sapiens	8-18
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
28606048-2	2017	HD is caused by a trinucleotide (CAG) repeat expansion in the gene encoding the protein huntingtin.	trinucleotide	18-31	huntingtin	Homo sapiens	88-98
28606048-2	2017	HD is caused by a trinucleotide (CAG) repeat expansion in the gene encoding the protein huntingtin.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	33-36	huntingtin	Homo sapiens	88-98
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
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
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
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
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
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
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
29036832-1	2017	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a trinucleotide (CAG) repeat expansion in huntingtin (HTT) on chromosome 4.	trinucleotide	101-114	huntingtin	Homo sapiens	141-151
29036832-1	2017	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a trinucleotide (CAG) repeat expansion in huntingtin (HTT) on chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	116-119	huntingtin	Homo sapiens	141-151
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
29036832-1	2017	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a trinucleotide (CAG) repeat expansion in huntingtin (HTT) on chromosome 4.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	116-119	huntingtin	Homo sapiens	153-156
29036832-1	2017	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a trinucleotide (CAG) repeat expansion in huntingtin (HTT) on chromosome 4.	trinucleotide	101-114	huntingtin	Homo sapiens	153-156
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	132-142
27840125-0	2016	Dopamine exacerbates mutant Huntingtin toxicity via oxidative-mediated inhibition of autophagy in SH-SY5Y neuroblastoma cells: Beneficial effects of anti-oxidant therapeutics.	Dopamine	0-8	huntingtin	Homo sapiens	28-38
28168008-2	2017	The abnormal generation of reactive oxygen species and the resulting oxidative stress-induced mitochondrial damage in neurons upon CAG mutations in the HTT gene have been hypothesized as the contributing factors of neurodegeneration in HD.	Oxygen	36-42	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	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
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.	Dopamine	146-148	huntingtin	Homo sapiens	66-69
27840125-7	2016	We found that the pre-incubation with N-Acetyl-l-Cysteine (a quinone reductase inducer) or Deferoxamine (an iron chelator) prevents the generation of ROS, restores the autophagy degradation of mHtt and preserves the cell viability in SH-SY5Y cells expressing the polyQ Htt and exposed to DA.	Acetylcysteine	38-57	huntingtin	Homo sapiens	194-197
27840125-7	2016	We found that the pre-incubation with N-Acetyl-l-Cysteine (a quinone reductase inducer) or Deferoxamine (an iron chelator) prevents the generation of ROS, restores the autophagy degradation of mHtt and preserves the cell viability in SH-SY5Y cells expressing the polyQ Htt and exposed to DA.	Deferoxamine	91-103	huntingtin	Homo sapiens	194-197
27790650-0	2016	Autophagy-mediated clearance of ubiquitinated mutant huntingtin by graphene oxide.	graphene oxide	67-81	huntingtin	Homo sapiens	53-63
27790650-3	2016	In this report we showed that graphene oxide (GO), an engineered nanomaterial with enormous potential in biomedical applications, effectively enhanced the clearance of mutant huntingtin (Htt), the aggregate-prone protein underlying the pathogenesis of HD.	graphene oxide	30-44	huntingtin	Homo sapiens	175-185
27790650-3	2016	In this report we showed that graphene oxide (GO), an engineered nanomaterial with enormous potential in biomedical applications, effectively enhanced the clearance of mutant huntingtin (Htt), the aggregate-prone protein underlying the pathogenesis of HD.	graphene oxide	30-44	huntingtin	Homo sapiens	187-190
27790650-3	2016	In this report we showed that graphene oxide (GO), an engineered nanomaterial with enormous potential in biomedical applications, effectively enhanced the clearance of mutant huntingtin (Htt), the aggregate-prone protein underlying the pathogenesis of HD.	graphene oxide	46-48	huntingtin	Homo sapiens	175-185
27790650-3	2016	In this report we showed that graphene oxide (GO), an engineered nanomaterial with enormous potential in biomedical applications, effectively enhanced the clearance of mutant huntingtin (Htt), the aggregate-prone protein underlying the pathogenesis of HD.	graphene oxide	46-48	huntingtin	Homo sapiens	187-190
27560450-5	2016	Consistently, the inhibition of the Arg/N-end rule pathway with PCA significantly elevated levels of MAPT and huntingtin aggregates, accompanied by increased numbers of LC3 and SQSTM1 puncta.	Arginine	36-39	huntingtin	Homo sapiens	110-120
27560450-5	2016	Consistently, the inhibition of the Arg/N-end rule pathway with PCA significantly elevated levels of MAPT and huntingtin aggregates, accompanied by increased numbers of LC3 and SQSTM1 puncta.	Nitrogen	40-41	huntingtin	Homo sapiens	110-120
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
27840125-7	2016	We found that the pre-incubation with N-Acetyl-l-Cysteine (a quinone reductase inducer) or Deferoxamine (an iron chelator) prevents the generation of ROS, restores the autophagy degradation of mHtt and preserves the cell viability in SH-SY5Y cells expressing the polyQ Htt and exposed to DA.	Iron	108-112	huntingtin	Homo sapiens	194-197
27840125-7	2016	We found that the pre-incubation with N-Acetyl-l-Cysteine (a quinone reductase inducer) or Deferoxamine (an iron chelator) prevents the generation of ROS, restores the autophagy degradation of mHtt and preserves the cell viability in SH-SY5Y cells expressing the polyQ Htt and exposed to DA.	ros	150-153	huntingtin	Homo sapiens	194-197
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
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
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
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
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
26545340-3	2016	Indeed, many proteins initially characterized in those diseases such as amyloid-beta protein, alpha-synuclein, and huntingtin have been linked to iron neurochemistry.	Iron	146-150	huntingtin	Homo sapiens	115-125
27658206-0	2016	Polyglutamine Tract Expansion Increases S-Nitrosylation of Huntingtin and Ataxin-1.	polyglutamine	0-13	huntingtin	Homo sapiens	59-69
27567324-1	2016	The serotonin neurotransmitter system is modulated in part by the uptake of synaptically released serotonin (5-HT) by the serotonin transporter (5-HTT), and by specific serotonin autoreceptors such as the somatodendritic 5-HT1A receptor, which can limit serotonin neuron depolarization.	Serotonin	4-13	huntingtin	Homo sapiens	147-150
27567324-1	2016	The serotonin neurotransmitter system is modulated in part by the uptake of synaptically released serotonin (5-HT) by the serotonin transporter (5-HTT), and by specific serotonin autoreceptors such as the somatodendritic 5-HT1A receptor, which can limit serotonin neuron depolarization.	Serotonin	98-107	huntingtin	Homo sapiens	147-150
27567324-1	2016	The serotonin neurotransmitter system is modulated in part by the uptake of synaptically released serotonin (5-HT) by the serotonin transporter (5-HTT), and by specific serotonin autoreceptors such as the somatodendritic 5-HT1A receptor, which can limit serotonin neuron depolarization.	Serotonin	98-107	huntingtin	Homo sapiens	147-150
27567324-1	2016	The serotonin neurotransmitter system is modulated in part by the uptake of synaptically released serotonin (5-HT) by the serotonin transporter (5-HTT), and by specific serotonin autoreceptors such as the somatodendritic 5-HT1A receptor, which can limit serotonin neuron depolarization.	Serotonin	98-107	huntingtin	Homo sapiens	147-150
27567324-7	2016	The lack of correlation between 5-HT1A and 5-HTT binding observed in the current study may be due to the different temporal responsiveness of regulatory processes controlling the somatodendritic 5-HT1A receptor and 5-HTT in response to changing availability of intrasynaptic serotonin.	Serotonin	275-284	huntingtin	Homo sapiens	217-220
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
27708610-1	2016	Huntington disease (HD) is caused by an abnormally expanded cytosine-adenine-guanine (CAG) trinucleotide repeat in the HTT gene.	cytosine-adenine-guanine (cag) trinucleotide	60-104	huntingtin	Homo sapiens	119-122
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
27658206-7	2016	Overexpression of nitric oxide synthase increases the S-nitrosylation of normal Htt and the frequency of conspicuous juxtanuclear inclusions of Htt N-terminal fragments in transfected cells.	nitric	18-24	huntingtin	Homo sapiens	80-83
27658206-7	2016	Overexpression of nitric oxide synthase increases the S-nitrosylation of normal Htt and the frequency of conspicuous juxtanuclear inclusions of Htt N-terminal fragments in transfected cells.	nitric	18-24	huntingtin	Homo sapiens	144-147
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
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
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
27264314-7	2016	METHODS: The pulsed-labeled proteins were conjugated with biotin using the click reaction strain-promoted alkyne-azide cycloaddition (SPAAC), and the chase signals were calculated by measuring the reduction percentage of the HTT HTRF signals after pull-down with streptavidin beads.	Biotin	58-64	huntingtin	Homo sapiens	225-228
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
27427935-4	2016	The most attractive advantage of nano-EGCG is that it efficiently protects neuronal cells from the toxic effect of extracellular amyloid beta or intracellular mutant huntingtin protein aggregates by preventing their aggregation.	epigallocatechin gallate	38-42	huntingtin	Homo sapiens	166-176
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
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
27481337-1	2016	We present a novel, general class of disease progression models for Huntington"s disease (HD), a neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) triplet repeat expansion on the huntingtin gene.	cytosine-adenine-guanine	135-159	huntingtin	Homo sapiens	198-208
26748651-8	2016	In HD, Cr in high doses (up to 30 g/day) was shown to slow down brain atrophy in premanifest Huntingtin mutation carriers.	Creatine	7-9	huntingtin	Homo sapiens	93-103
27481337-1	2016	We present a novel, general class of disease progression models for Huntington"s disease (HD), a neurodegenerative disease caused by a cytosine-adenine-guanine (CAG) triplet repeat expansion on the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	161-164	huntingtin	Homo sapiens	198-208
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
27257945-3	2016	RECENT FINDINGS: A genome-wide association study in Huntington"s disease identified genetic disease modifiers involved in controlling DNA repair mechanisms and stability of the HTT trinucleotide repeat expansion.	trinucleotide	181-194	huntingtin	Homo sapiens	177-180
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
27458341-4	2016	These altered kinetics arise from the shift of a proline-induced translational pause site away from Htt"s localization sequence due to the expansion of the CAG-repeat segment between the poly-proline and localization sequences.	Proline	49-56	huntingtin	Homo sapiens	100-103
27458341-4	2016	These altered kinetics arise from the shift of a proline-induced translational pause site away from Htt"s localization sequence due to the expansion of the CAG-repeat segment between the poly-proline and localization sequences.	polyproline	187-199	huntingtin	Homo sapiens	100-103
27479945-1	2016	Age of Huntington"s disease (HD) motoric onset is strongly related to the number of CAG trinucleotide repeats in the huntingtin gene, suggesting that biological tissue age plays an important role in disease etiology.	trinucleotide	88-101	huntingtin	Homo sapiens	117-127
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
27182645-7	2016	5-Azacytidine treatments also resulted in stabilization of TNR expansion within the mutant HTT allele during long-term culture of HD cells.	Azacitidine	0-13	huntingtin	Homo sapiens	91-94
25941077-0	2016	Mutant Huntingtin and Elusive Defects in Oxidative Metabolism and Mitochondrial Calcium Handling.	Calcium	80-87	huntingtin	Homo sapiens	7-17
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
27463137-2	2016	Expanded polyQ leads to htt aggregation.	polyglutamine	9-14	huntingtin	Homo sapiens	24-27
27463137-5	2016	Acetylation of htt-exon1(51Q) and synthetic truncated htt-exon 1 mimicking peptides (Nt(17)-Q35-P10-KK) was achieved using a selective covalent label, sulfo-N-hydroxysuccinimide (NHSA).	N-hydroxysulfosuccinimide	151-177	huntingtin	Homo sapiens	15-18
27463137-5	2016	Acetylation of htt-exon1(51Q) and synthetic truncated htt-exon 1 mimicking peptides (Nt(17)-Q35-P10-KK) was achieved using a selective covalent label, sulfo-N-hydroxysuccinimide (NHSA).	N-hydroxysulfosuccinimide	151-177	huntingtin	Homo sapiens	54-57
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
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
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
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
26957541-2	2016	Cell treatment with trehalose could decrease cytosolic aggregates of potentially pathogenic proteins, including mutant huntingtin, alpha-synuclein, and phosphorylated tau that are associated with neurodegenerative diseases.	Trehalose	20-29	huntingtin	Homo sapiens	119-129
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.	trinucleotide	103-116	huntingtin	Homo sapiens	147-150
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
26908605-0	2016	Mitochondria-targeted molecules MitoQ and SS31 reduce mutant huntingtin-induced mitochondrial toxicity and synaptic damage in Huntington"s disease.	mitoquinone	32-37	huntingtin	Homo sapiens	61-71
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
27080129-1	2016	BACKGROUND: Huntington"s disease (HD) is an incurable hereditary neurodegenerative disorder, which manifests itself as a loss of GABAergic medium spiny (GABA MS) neurons in the striatum and caused by an expansion of the CAG repeat in exon 1 of the huntingtin gene.	gamma-Aminobutyric Acid	129-133	huntingtin	Homo sapiens	248-258
27080129-7	2016	CONCLUSIONS: Our data is the first to demonstrate the direct link of nuclear morphology and SOC calcium deregulation to mutant huntingtin protein expression in iPSCs-derived neurons with disease-mimetic hallmarks, providing a valuable tool for identification of candidate anti-HD drugs.	Calcium	96-103	huntingtin	Homo sapiens	127-137
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
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	64-74
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
26958885-11	2016	Our characterization of Huntingtin"s amino-terminus provides insights into the structural origin of its ability to oligomerize and interact with phospholipid bilayers, processes closely linked to the biological functions of this protein.	Phospholipids	145-157	huntingtin	Homo sapiens	24-34
26831073-0	2016	Huntingtin exon 1 fibrils feature an interdigitated beta-hairpin-based polyglutamine core.	polyglutamine	71-84	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	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
27014581-5	2016	Moreover, a 38 CAG trinucleotide repeat expansion was found on the huntingtin gene, thus configuring a singular CPEO/"reduced penetrance" Huntington disease "double trouble".	trinucleotide	19-32	huntingtin	Homo sapiens	67-77
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
27069383-2	2016	The Huntingtin gene (HTT) has a unique feature of a DNA trinucleotide (triplet) repeat, with repeat length ranging from 10 to 35 in the normal population.	trinucleotide	56-69	huntingtin	Homo sapiens	4-14
27069383-2	2016	The Huntingtin gene (HTT) has a unique feature of a DNA trinucleotide (triplet) repeat, with repeat length ranging from 10 to 35 in the normal population.	trinucleotide	56-69	huntingtin	Homo sapiens	21-24
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
26428929-1	2016	UNLABELLED: Huntington"s disease (HD) is a genetic disease caused by a CAG trinucleotide repeat expansion encoding a polyglutamine tract in the huntingtin (HTT) protein, ultimately leading to neuronal loss and consequent cognitive decline and death.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	71-74	huntingtin	Homo sapiens	144-154
26428929-1	2016	UNLABELLED: Huntington"s disease (HD) is a genetic disease caused by a CAG trinucleotide repeat expansion encoding a polyglutamine tract in the huntingtin (HTT) protein, ultimately leading to neuronal loss and consequent cognitive decline and death.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	71-74	huntingtin	Homo sapiens	156-159
26428929-1	2016	UNLABELLED: Huntington"s disease (HD) is a genetic disease caused by a CAG trinucleotide repeat expansion encoding a polyglutamine tract in the huntingtin (HTT) protein, ultimately leading to neuronal loss and consequent cognitive decline and death.	trinucleotide	75-88	huntingtin	Homo sapiens	144-154
26428929-1	2016	UNLABELLED: Huntington"s disease (HD) is a genetic disease caused by a CAG trinucleotide repeat expansion encoding a polyglutamine tract in the huntingtin (HTT) protein, ultimately leading to neuronal loss and consequent cognitive decline and death.	trinucleotide	75-88	huntingtin	Homo sapiens	156-159
26471164-2	2016	Striatal cells carrying mutated Huntingtin presented increased sensitivity to cadmium (Cd) toxicity, decreased sensitivity to manganese (Mn) toxicity and deficits in Mn uptake.	Cadmium	78-85	huntingtin	Homo sapiens	32-42
26471164-2	2016	Striatal cells carrying mutated Huntingtin presented increased sensitivity to cadmium (Cd) toxicity, decreased sensitivity to manganese (Mn) toxicity and deficits in Mn uptake.	Cadmium	87-89	huntingtin	Homo sapiens	32-42
26471164-2	2016	Striatal cells carrying mutated Huntingtin presented increased sensitivity to cadmium (Cd) toxicity, decreased sensitivity to manganese (Mn) toxicity and deficits in Mn uptake.	Manganese	126-135	huntingtin	Homo sapiens	32-42
26652744-0	2016	Cholesterol Modifies Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.	Cholesterol	0-11	huntingtin	Homo sapiens	21-31
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
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.	cytosine- adenine-guanosine	91-118	huntingtin	Homo sapiens	173-183
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.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	120-123	huntingtin	Homo sapiens	173-183
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
26652744-2	2016	Expanded polyQ domains are directly correlated to disease-related htt aggregation.	polyglutamine	9-14	huntingtin	Homo sapiens	66-69
26652744-6	2016	As the cholesterol content of the membrane increased, the extent of htt insertion decreased.	Cholesterol	7-18	huntingtin	Homo sapiens	68-71
26652744-7	2016	Vesicles containing extra cholesterol were resistant to htt-induced permeabilization.	Cholesterol	26-37	huntingtin	Homo sapiens	56-59
26652744-8	2016	Morphological and mechanical changes in the bilayer associated with exposure to htt were also drastically altered by the presence of cholesterol.	Cholesterol	133-144	huntingtin	Homo sapiens	80-83
26652744-10	2016	In contrast, morphological changes induced by htt in bilayers enriched in cholesterol were plateau-like with a smooth appearance.	Cholesterol	74-85	huntingtin	Homo sapiens	46-49
26652744-11	2016	Collectively, these observations suggest that the presence and amount of cholesterol in lipid membranes play a critical role in htt binding and aggregation on lipid membranes.	Cholesterol	73-84	huntingtin	Homo sapiens	128-131
27578922-2	2016	Although the cause of HD is well described-HD is a genetic disorder caused by a trinucleotide (CAG) repeat expansion in the gene encoding for huntingtin (HTT) on chromosome 4p16.3-the ultimate cause of neuronal death is still uncertain.	trinucleotide	80-93	huntingtin	Homo sapiens	142-152
26881734-2	2016	It results from an expanded unstable trinucleotide repeat in the coding region of the huntingtin gene.	trinucleotide	37-50	huntingtin	Homo sapiens	86-96
27595037-2	2016	We show that expression of a mutant human huntingtin exon-1-GFP fusion construct results in nonspecific gene dysregulation that is significantly reduced by 50% due to coexpression of INT41, an intrabody specific for the proline-rich region of the huntingtin protein.	Proline	220-227	huntingtin	Homo sapiens	42-52
27595037-2	2016	We show that expression of a mutant human huntingtin exon-1-GFP fusion construct results in nonspecific gene dysregulation that is significantly reduced by 50% due to coexpression of INT41, an intrabody specific for the proline-rich region of the huntingtin protein.	Proline	220-227	huntingtin	Homo sapiens	247-257
27578922-2	2016	Although the cause of HD is well described-HD is a genetic disorder caused by a trinucleotide (CAG) repeat expansion in the gene encoding for huntingtin (HTT) on chromosome 4p16.3-the ultimate cause of neuronal death is still uncertain.	trinucleotide	80-93	huntingtin	Homo sapiens	154-157
27578922-2	2016	Although the cause of HD is well described-HD is a genetic disorder caused by a trinucleotide (CAG) repeat expansion in the gene encoding for huntingtin (HTT) on chromosome 4p16.3-the ultimate cause of neuronal death is still uncertain.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	95-98	huntingtin	Homo sapiens	142-152
27578922-2	2016	Although the cause of HD is well described-HD is a genetic disorder caused by a trinucleotide (CAG) repeat expansion in the gene encoding for huntingtin (HTT) on chromosome 4p16.3-the ultimate cause of neuronal death is still uncertain.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	95-98	huntingtin	Homo sapiens	154-157
27144051-2	2016	Huntington"s disease is caused by a polyglutamate expansion of the protein huntingtin.	Polyglutamic Acid	36-49	huntingtin	Homo sapiens	75-85
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
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
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
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.	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
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
26464486-7	2015	In the Mdivil-treated mutant Htt neurons, fission genes were down-regulated, and fusion genes were up-regulated, suggesting that Mdivil decreases fission activity.	mdivil	7-13	huntingtin	Homo sapiens	29-32
26464486-7	2015	In the Mdivil-treated mutant Htt neurons, fission genes were down-regulated, and fusion genes were up-regulated, suggesting that Mdivil decreases fission activity.	mdivil	129-135	huntingtin	Homo sapiens	29-32
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
26490331-3	2015	Mutant huntingtin cleavage has been linked to the overactivation of proteases due to mitochondrial dysfunction and calcium derangements.	Calcium	115-122	huntingtin	Homo sapiens	7-17
26636579-1	2015	Huntington"s Disease (HD) is a devastating neurodegenerative disorder that is caused by an expanded CAG trinucleotide repeat in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	100-103	huntingtin	Homo sapiens	132-142
26636579-1	2015	Huntington"s Disease (HD) is a devastating neurodegenerative disorder that is caused by an expanded CAG trinucleotide repeat in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	100-103	huntingtin	Homo sapiens	144-147
26636579-1	2015	Huntington"s Disease (HD) is a devastating neurodegenerative disorder that is caused by an expanded CAG trinucleotide repeat in the Huntingtin (HTT) gene.	trinucleotide	104-117	huntingtin	Homo sapiens	132-142
26636579-1	2015	Huntington"s Disease (HD) is a devastating neurodegenerative disorder that is caused by an expanded CAG trinucleotide repeat in the Huntingtin (HTT) gene.	trinucleotide	104-117	huntingtin	Homo sapiens	144-147
26409001-0	2015	Differential ERK activation during autophagy induced by europium hydroxide nanorods and trehalose: Maximum clearance of huntingtin aggregates through combined treatment.	europium hydroxide	56-74	huntingtin	Homo sapiens	120-130
26409001-0	2015	Differential ERK activation during autophagy induced by europium hydroxide nanorods and trehalose: Maximum clearance of huntingtin aggregates through combined treatment.	Trehalose	88-97	huntingtin	Homo sapiens	120-130
26409001-2	2015	In our earlier report, we have demonstrated the enhanced degradation of mutant huntingtin protein aggregates through autophagy process induced by europium hydroxide nanorods [EHNs: Eu(III)(OH)3], but the underlying molecular mechanism of EHNs mediated autophagy was unclear.	europium hydroxide nanorods	146-173	huntingtin	Homo sapiens	79-89
26409001-2	2015	In our earlier report, we have demonstrated the enhanced degradation of mutant huntingtin protein aggregates through autophagy process induced by europium hydroxide nanorods [EHNs: Eu(III)(OH)3], but the underlying molecular mechanism of EHNs mediated autophagy was unclear.	ehns	175-179	huntingtin	Homo sapiens	79-89
26409001-2	2015	In our earlier report, we have demonstrated the enhanced degradation of mutant huntingtin protein aggregates through autophagy process induced by europium hydroxide nanorods [EHNs: Eu(III)(OH)3], but the underlying molecular mechanism of EHNs mediated autophagy was unclear.	eu(iii)(oh)3	181-193	huntingtin	Homo sapiens	79-89
26409001-2	2015	In our earlier report, we have demonstrated the enhanced degradation of mutant huntingtin protein aggregates through autophagy process induced by europium hydroxide nanorods [EHNs: Eu(III)(OH)3], but the underlying molecular mechanism of EHNs mediated autophagy was unclear.	ehns	238-242	huntingtin	Homo sapiens	79-89
26409001-4	2015	The inhibition of ERK1/2 phosphorylation using the specific MEK inhibitor U0126 partially abrogates the autophagy as well as the clearance of mutant huntingtin protein aggregates mediated by EHNs suggesting that nanorods stimulate the activation of MEK/ERK1/2 signaling pathway during autophagy process.	U 0126	74-79	huntingtin	Homo sapiens	149-159
26409001-4	2015	The inhibition of ERK1/2 phosphorylation using the specific MEK inhibitor U0126 partially abrogates the autophagy as well as the clearance of mutant huntingtin protein aggregates mediated by EHNs suggesting that nanorods stimulate the activation of MEK/ERK1/2 signaling pathway during autophagy process.	ehns	191-195	huntingtin	Homo sapiens	149-159
26409001-6	2015	Interestingly, the combined treatment of EHNs and trehalose leads to more degradation of mutant huntingtin protein aggregates than that obtained with single treatment of either nanorods or trehalose.	ehns	41-45	huntingtin	Homo sapiens	96-106
26409001-6	2015	Interestingly, the combined treatment of EHNs and trehalose leads to more degradation of mutant huntingtin protein aggregates than that obtained with single treatment of either nanorods or trehalose.	Trehalose	50-59	huntingtin	Homo sapiens	96-106
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
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.	trinucleotide	126-139	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.	trinucleotide	126-139	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	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
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
26307082-6	2015	The strongest and most uniform immune response was to a combination of three non-overlapping HTT Exon1 coded peptides, conjugated to KLH, delivered with alum adjuvant.	alum adjuvant	153-166	huntingtin	Homo sapiens	93-96
26201449-8	2015	Antisense oligonucleotides complementary to the deletion reduce mutant A1 HTT mRNA by 78% in patient cells while sparing wild-type HTT expression.	Oligonucleotides	10-26	huntingtin	Homo sapiens	74-77
26201449-8	2015	Antisense oligonucleotides complementary to the deletion reduce mutant A1 HTT mRNA by 78% in patient cells while sparing wild-type HTT expression.	Oligonucleotides	10-26	huntingtin	Homo sapiens	131-134
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
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
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
26222265-0	2015	Allele-Selective Inhibition of Mutant Huntingtin with 2-Thio- and C5- Triazolylphenyl-Deoxythymidine-Modified Antisense Oligonucleotides.	-thio	55-60	huntingtin	Homo sapiens	38-48
26222265-0	2015	Allele-Selective Inhibition of Mutant Huntingtin with 2-Thio- and C5- Triazolylphenyl-Deoxythymidine-Modified Antisense Oligonucleotides.	triazolylphenyl-deoxythymidine	70-100	huntingtin	Homo sapiens	38-48
26222265-0	2015	Allele-Selective Inhibition of Mutant Huntingtin with 2-Thio- and C5- Triazolylphenyl-Deoxythymidine-Modified Antisense Oligonucleotides.	Oligonucleotides	120-136	huntingtin	Homo sapiens	38-48
26222265-1	2015	We report the effect of introducing a single incorporation of 2-thio-deoxythymidine (2S-dT) or C5-Triazolylphenyl-deoxythymidine (5-TrPh-dT) at four positions within the gap region of RNase H gapmer antisense oligonucleotides (ASOs) for reducing wild-type and mutant huntingtin mRNA in human patient fibroblasts.	2-thio-deoxythymidine	62-83	huntingtin	Homo sapiens	267-277
26222265-1	2015	We report the effect of introducing a single incorporation of 2-thio-deoxythymidine (2S-dT) or C5-Triazolylphenyl-deoxythymidine (5-TrPh-dT) at four positions within the gap region of RNase H gapmer antisense oligonucleotides (ASOs) for reducing wild-type and mutant huntingtin mRNA in human patient fibroblasts.	5-trph-dt	130-139	huntingtin	Homo sapiens	267-277
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
26264576-1	2015	Huntington"s disease (HD) is an autosomal-dominant degenerative disease caused by a cytosine-adenine-guanine trinucleotide expansion in the Huntingtin (htt) gene.	cytosine-adenine-guanine trinucleotide	84-122	huntingtin	Homo sapiens	140-150
26264576-1	2015	Huntington"s disease (HD) is an autosomal-dominant degenerative disease caused by a cytosine-adenine-guanine trinucleotide expansion in the Huntingtin (htt) gene.	cytosine-adenine-guanine trinucleotide	84-122	huntingtin	Homo sapiens	152-155
26450664-0	2015	Conformational switch of polyglutamine-expanded huntingtin into benign aggregates leads to neuroprotective effect.	polyglutamine	25-38	huntingtin	Homo sapiens	48-58
26439718-1	2015	Huntington disease (HD) is caused by expansion of a CAG trinucleotide repeat in the first exon of the Huntingtin (HTT) gene.	trinucleotide	56-69	huntingtin	Homo sapiens	102-112
26439718-1	2015	Huntington disease (HD) is caused by expansion of a CAG trinucleotide repeat in the first exon of the Huntingtin (HTT) gene.	trinucleotide	56-69	huntingtin	Homo sapiens	114-117
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
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
26165689-0	2015	Huntingtin proteolysis releases non-polyQ fragments that cause toxicity through dynamin 1 dysregulation.	polyglutamine	36-41	huntingtin	Homo sapiens	0-10
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
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
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
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
26300964-5	2015	This stretch is encoded by a trinucleotide CAG repetition in exon 1 of HTT.	trinucleotide	29-42	huntingtin	Homo sapiens	71-74
26293574-3	2015	METHODS: We analyzed HTT and ZO1 expression as well as the HTT phosphoserine 421-activated form (S421-P-HTT) in human breast cancer tissues by quantitative reverse transcription polymerase chain reaction and immunohistochemistry.	Phosphoserine	63-76	huntingtin	Homo sapiens	59-62
26293574-3	2015	METHODS: We analyzed HTT and ZO1 expression as well as the HTT phosphoserine 421-activated form (S421-P-HTT) in human breast cancer tissues by quantitative reverse transcription polymerase chain reaction and immunohistochemistry.	Phosphoserine	63-76	huntingtin	Homo sapiens	59-62
26106822-0	2015	Detection of huntingtin exon 1 phosphorylation by Phos-Tag SDS-PAGE: Predominant phosphorylation on threonine 3 and regulation by IKKbeta.	Sodium Dodecyl Sulfate	59-62	huntingtin	Homo sapiens	13-23
26106822-0	2015	Detection of huntingtin exon 1 phosphorylation by Phos-Tag SDS-PAGE: Predominant phosphorylation on threonine 3 and regulation by IKKbeta.	Threonine	100-109	huntingtin	Homo sapiens	13-23
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
26106822-5	2015	Using a modified SDS-PAGE protocol (Phos-Tag) followed by Western blotting with specific anti-HUNTINGTIN antibodies, we efficiently resolved huntingtin fragments expressed in cellular contexts based on the presence of phosphorylated residues, we defined threonine 3 as the major site of huntingtin N17 phosphorylation and, finally, we identified IKK-beta as a kinase capable of phosphorylating threonine 3 in N-terminal hungtingtin fragments.	Sodium Dodecyl Sulfate	17-20	huntingtin	Homo sapiens	141-151
26106822-5	2015	Using a modified SDS-PAGE protocol (Phos-Tag) followed by Western blotting with specific anti-HUNTINGTIN antibodies, we efficiently resolved huntingtin fragments expressed in cellular contexts based on the presence of phosphorylated residues, we defined threonine 3 as the major site of huntingtin N17 phosphorylation and, finally, we identified IKK-beta as a kinase capable of phosphorylating threonine 3 in N-terminal hungtingtin fragments.	Threonine	254-263	huntingtin	Homo sapiens	94-104
26106822-5	2015	Using a modified SDS-PAGE protocol (Phos-Tag) followed by Western blotting with specific anti-HUNTINGTIN antibodies, we efficiently resolved huntingtin fragments expressed in cellular contexts based on the presence of phosphorylated residues, we defined threonine 3 as the major site of huntingtin N17 phosphorylation and, finally, we identified IKK-beta as a kinase capable of phosphorylating threonine 3 in N-terminal hungtingtin fragments.	Threonine	254-263	huntingtin	Homo sapiens	141-151
26106822-5	2015	Using a modified SDS-PAGE protocol (Phos-Tag) followed by Western blotting with specific anti-HUNTINGTIN antibodies, we efficiently resolved huntingtin fragments expressed in cellular contexts based on the presence of phosphorylated residues, we defined threonine 3 as the major site of huntingtin N17 phosphorylation and, finally, we identified IKK-beta as a kinase capable of phosphorylating threonine 3 in N-terminal hungtingtin fragments.	Threonine	394-403	huntingtin	Homo sapiens	94-104
26106822-5	2015	Using a modified SDS-PAGE protocol (Phos-Tag) followed by Western blotting with specific anti-HUNTINGTIN antibodies, we efficiently resolved huntingtin fragments expressed in cellular contexts based on the presence of phosphorylated residues, we defined threonine 3 as the major site of huntingtin N17 phosphorylation and, finally, we identified IKK-beta as a kinase capable of phosphorylating threonine 3 in N-terminal hungtingtin fragments.	Threonine	394-403	huntingtin	Homo sapiens	141-151
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
26239075-4	2015	Furthermore, DEX increased huntingtin (Htt) protein levels via glucocorticoid receptor (GR) activation, and reduction in the amount of Htt by a specific shRNA reversed the action of DEX on BDNF vesicle transport.	Dexamethasone	13-16	huntingtin	Homo sapiens	27-37
26239075-4	2015	Furthermore, DEX increased huntingtin (Htt) protein levels via glucocorticoid receptor (GR) activation, and reduction in the amount of Htt by a specific shRNA reversed the action of DEX on BDNF vesicle transport.	Dexamethasone	13-16	huntingtin	Homo sapiens	39-42
26239075-4	2015	Furthermore, DEX increased huntingtin (Htt) protein levels via glucocorticoid receptor (GR) activation, and reduction in the amount of Htt by a specific shRNA reversed the action of DEX on BDNF vesicle transport.	Dexamethasone	182-185	huntingtin	Homo sapiens	135-138
25596342-1	2015	Huntington disease (HD), an autosomal dominant neurodegenerative disorder caused by an abnormal expansion of CAG trinucleotide repeat in the Huntingtin (HTT) gene, is characterized by extensive neurodegeneration of striatum and cortex and severe diffuse atrophy at MRI.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	109-112	huntingtin	Homo sapiens	141-151
25596342-1	2015	Huntington disease (HD), an autosomal dominant neurodegenerative disorder caused by an abnormal expansion of CAG trinucleotide repeat in the Huntingtin (HTT) gene, is characterized by extensive neurodegeneration of striatum and cortex and severe diffuse atrophy at MRI.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	109-112	huntingtin	Homo sapiens	153-156
25596342-1	2015	Huntington disease (HD), an autosomal dominant neurodegenerative disorder caused by an abnormal expansion of CAG trinucleotide repeat in the Huntingtin (HTT) gene, is characterized by extensive neurodegeneration of striatum and cortex and severe diffuse atrophy at MRI.	trinucleotide	113-126	huntingtin	Homo sapiens	141-151
25596342-1	2015	Huntington disease (HD), an autosomal dominant neurodegenerative disorder caused by an abnormal expansion of CAG trinucleotide repeat in the Huntingtin (HTT) gene, is characterized by extensive neurodegeneration of striatum and cortex and severe diffuse atrophy at MRI.	trinucleotide	113-126	huntingtin	Homo sapiens	153-156
25596342-5	2015	It is likely that mutant HTT decreases the maturation of SREBP and the up-regulation LXR and LXR-targeted genes (SREBP, ABCG1 and ABCG4, HMGCoA reductase, ApoE) resulting into a lower synthesis and transport of cholesterol from astrocytes to neurons via ApoE.	Cholesterol	211-222	huntingtin	Homo sapiens	25-28
25596342-6	2015	In primary oligodendrocytes, mutant HTT inhibited the regulatory effect of PGC1alpha on cholesterol metabolism and on the expression of MBP.	Cholesterol	88-99	huntingtin	Homo sapiens	36-39
26174131-4	2015	The sensitivity of huntingtin IP-FCM enables accurate detection of mutant huntingtin protein in the cerebrospinal fluid of HD patients and model mice, demonstrating that mutant huntingtin levels in cerebrospinal fluid reflect brain levels, increasing with disease stage and decreasing following brain huntingtin suppression.	ip-fcm	30-36	huntingtin	Homo sapiens	19-29
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
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
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
25847392-5	2015	We apply the method to estimate the cumulative risk of developing Huntington"s disease (HD) from subjects with huntingtin gene mutation using a large collaborative HD study data and illustrate an inverse relationship between the cumulative risk of HD and the length of cytosine-adenine-guanine repeats in the huntingtin gene.	cytosine-adenine-guanine	269-293	huntingtin	Homo sapiens	111-121
25847392-5	2015	We apply the method to estimate the cumulative risk of developing Huntington"s disease (HD) from subjects with huntingtin gene mutation using a large collaborative HD study data and illustrate an inverse relationship between the cumulative risk of HD and the length of cytosine-adenine-guanine repeats in the huntingtin gene.	cytosine-adenine-guanine	269-293	huntingtin	Homo sapiens	309-319
26174131-4	2015	The sensitivity of huntingtin IP-FCM enables accurate detection of mutant huntingtin protein in the cerebrospinal fluid of HD patients and model mice, demonstrating that mutant huntingtin levels in cerebrospinal fluid reflect brain levels, increasing with disease stage and decreasing following brain huntingtin suppression.	ip-fcm	30-36	huntingtin	Homo sapiens	74-84
25995452-1	2015	Huntington disease, a neurodegenerative disorder characterized by functional deficits and loss of striatal neurons, is linked to an expanded and unstable CAG trinucleotide repeat in the huntingtin gene (HTT).	trinucleotide	158-171	huntingtin	Homo sapiens	186-196
25995452-1	2015	Huntington disease, a neurodegenerative disorder characterized by functional deficits and loss of striatal neurons, is linked to an expanded and unstable CAG trinucleotide repeat in the huntingtin gene (HTT).	trinucleotide	158-171	huntingtin	Homo sapiens	203-206
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
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
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
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
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
25673747-1	2015	The Q175 knockin mouse model of Huntington"s disease (HD) carries a CAG trinucleotide expansion of the human mutant huntingtin allele in its native mouse genomic context and recapitulates the genotype more closely than transgenic models.	trinucleotide	72-85	huntingtin	Homo sapiens	116-126
25726852-1	2015	OBJECTIVES: Huntington"s disease is a neurodegenerative disorder characterized by motor, cognitive, and psychiatric symptoms that are caused by huntingtin gene (HTT) CAG trinucleotide repeat alleles of 36 or more units.	trinucleotide	170-183	huntingtin	Homo sapiens	144-154
25726852-1	2015	OBJECTIVES: Huntington"s disease is a neurodegenerative disorder characterized by motor, cognitive, and psychiatric symptoms that are caused by huntingtin gene (HTT) CAG trinucleotide repeat alleles of 36 or more units.	trinucleotide	170-183	huntingtin	Homo sapiens	161-164
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
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.	trinucleotide cag	105-122	huntingtin	Homo sapiens	144-147
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
25640796-1	2015	Huntington"s disease is an incurable neurodegenerative disease caused by inheritance of an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat within the Huntingtin gene.	cytosine-adenine-guanine (	100-126	huntingtin	Homo sapiens	163-173
25640796-1	2015	Huntington"s disease is an incurable neurodegenerative disease caused by inheritance of an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat within the Huntingtin gene.	cag) trinucleotide	126-144	huntingtin	Homo sapiens	163-173
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
25301063-4	2015	Astrocytes bearing the huntingtin protein containing increasing CAG repeats secreted less apoE-lipoprotein-bound cholesterol in the medium.	Cholesterol	113-124	huntingtin	Homo sapiens	23-33
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
25687118-1	2015	Huntington"s disease (HD) is a neurological genetic disorder caused by the expansion of the CAG trinucleotide repeats (TNR) in the N-terminal region of coding sequence of the Huntingtin"s (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	92-95	huntingtin	Homo sapiens	175-187
25687118-1	2015	Huntington"s disease (HD) is a neurological genetic disorder caused by the expansion of the CAG trinucleotide repeats (TNR) in the N-terminal region of coding sequence of the Huntingtin"s (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	92-95	huntingtin	Homo sapiens	189-192
25687118-1	2015	Huntington"s disease (HD) is a neurological genetic disorder caused by the expansion of the CAG trinucleotide repeats (TNR) in the N-terminal region of coding sequence of the Huntingtin"s (HTT) gene.	trinucleotide	96-109	huntingtin	Homo sapiens	175-187
25687118-1	2015	Huntington"s disease (HD) is a neurological genetic disorder caused by the expansion of the CAG trinucleotide repeats (TNR) in the N-terminal region of coding sequence of the Huntingtin"s (HTT) gene.	trinucleotide	96-109	huntingtin	Homo sapiens	189-192
25687118-2	2015	This results in the addition of a poly-glutamine tract within the Huntingtin protein, resulting in its pathological form.	poly	34-38	huntingtin	Homo sapiens	66-76
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
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
27188817-2	2015	The disease is caused by an expanded CAG trinucleotide repeat (of variable length) in HTT, the gene that encodes the protein huntingtin.	trinucleotide	41-54	huntingtin	Homo sapiens	86-89
27188817-2	2015	The disease is caused by an expanded CAG trinucleotide repeat (of variable length) in HTT, the gene that encodes the protein huntingtin.	trinucleotide	41-54	huntingtin	Homo sapiens	125-135
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
25888196-6	2015	Further diagnostic tests were performed, and a genetic screening for Huntington disease revealed 45 repeats of the CAG nucleotide in the IT-15 gene.	cag nucleotide	115-129	huntingtin	Homo sapiens	137-142
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).	Glucose	63-70	huntingtin	Homo sapiens	160-170
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
25799558-5	2015	For scalable production of full-length normal (17Q) and mutant (46Q and 128Q) Htt we have established two different systems, the first based on doxycycline-inducible Htt expression in stable cell lines, the second on "gutless" adenovirus mediated gene transfer.	Doxycycline	144-155	huntingtin	Homo sapiens	166-169
25762330-0	2015	Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulations.	Phospholipids	49-61	huntingtin	Homo sapiens	12-22
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
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
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
25738228-5	2015	Gpr52 modulates Htt via cAMP-dependent but PKA independent mechanisms.	Cyclic AMP	24-28	huntingtin	Homo sapiens	16-19
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
25686248-5	2015	In mammalian cells, Huntingtin physically interacts with the autophagy cargo receptor p62 to facilitate its association with the integral autophagosome component LC3 and with Lys-63-linked ubiquitin-modified substrates.	Lysine	175-178	huntingtin	Homo sapiens	20-30
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
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
25699594-4	2015	Furthermore, by overexpressing huntingtin with 74 CAG repeats (EGFP-HTT 74) in PC-12 cells, neferine reduces both the protein level and toxicity of mutant huntingtin through an autophagy-related gene 7 (Atg7)-dependent mechanism.	neferine	92-100	huntingtin	Homo sapiens	31-41
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
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
25449906-11	2015	By contrast, overexpression of SIGMAR1 reduced the accumulation of NIs containing mutant huntingtin.	Nickel	67-70	huntingtin	Homo sapiens	89-99
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
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).	cytosine-adenine-guanine	129-153	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).	cytosine-adenine-guanine	129-153	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
25446099-6	2015	Deletion of HTT-N17 leads to formation of tinier, SDS-soluble nuclear aggregates formed by N-terminal mutant HTT.	Sodium Dodecyl Sulfate	50-53	huntingtin	Homo sapiens	12-19
25446099-6	2015	Deletion of HTT-N17 leads to formation of tinier, SDS-soluble nuclear aggregates formed by N-terminal mutant HTT.	Sodium Dodecyl Sulfate	50-53	huntingtin	Homo sapiens	12-15
25927346-0	2015	PRMT5- mediated symmetric arginine dimethylation is attenuated by mutant huntingtin and is impaired in Huntington"s disease (HD).	Arginine	26-34	huntingtin	Homo sapiens	73-83
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
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
25927346-2	2015	Here, we explored a functional interaction of Htt with protein arginine methyltransferase 5 (PRMT5), an enzyme mediating symmetrical dimethylation of arginine (sDMA) of key cellular proteins, including histones, and spliceosomal Sm proteins.	Arginine	63-71	huntingtin	Homo sapiens	46-49
25927346-2	2015	Here, we explored a functional interaction of Htt with protein arginine methyltransferase 5 (PRMT5), an enzyme mediating symmetrical dimethylation of arginine (sDMA) of key cellular proteins, including histones, and spliceosomal Sm proteins.	symmetric dimethylarginine	160-164	huntingtin	Homo sapiens	46-49
25927346-9	2015	These studies revealed a potential new mechanism for disruption of gene expression and RNA processing in HD, involving a loss of normal function of Htt in facilitation of PRMT5, supporting the idea that epigenetic regulation of gene transcription may be involved in HD and highlighting symmetric dimethylation of arginine as potential new therapeutic target.	Arginine	313-321	huntingtin	Homo sapiens	148-151
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
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
25205327-4	2015	Following its clinical and pathologic characterization, the causative genetic mutation in HD was subsequently identified as a trinucleotide (CAG) repeat expansion in the huntingtin (HTT) gene, and consequently, the HTT gene and huntingtin protein have been studied in great detail.	trinucleotide	126-139	huntingtin	Homo sapiens	170-180
25205327-4	2015	Following its clinical and pathologic characterization, the causative genetic mutation in HD was subsequently identified as a trinucleotide (CAG) repeat expansion in the huntingtin (HTT) gene, and consequently, the HTT gene and huntingtin protein have been studied in great detail.	trinucleotide	126-139	huntingtin	Homo sapiens	182-185
25205327-4	2015	Following its clinical and pathologic characterization, the causative genetic mutation in HD was subsequently identified as a trinucleotide (CAG) repeat expansion in the huntingtin (HTT) gene, and consequently, the HTT gene and huntingtin protein have been studied in great detail.	trinucleotide	126-139	huntingtin	Homo sapiens	215-218
25205327-4	2015	Following its clinical and pathologic characterization, the causative genetic mutation in HD was subsequently identified as a trinucleotide (CAG) repeat expansion in the huntingtin (HTT) gene, and consequently, the HTT gene and huntingtin protein have been studied in great detail.	trinucleotide	126-139	huntingtin	Homo sapiens	228-238
25205327-4	2015	Following its clinical and pathologic characterization, the causative genetic mutation in HD was subsequently identified as a trinucleotide (CAG) repeat expansion in the huntingtin (HTT) gene, and consequently, the HTT gene and huntingtin protein have been studied in great detail.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	141-144	huntingtin	Homo sapiens	170-180
25205327-4	2015	Following its clinical and pathologic characterization, the causative genetic mutation in HD was subsequently identified as a trinucleotide (CAG) repeat expansion in the huntingtin (HTT) gene, and consequently, the HTT gene and huntingtin protein have been studied in great detail.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	141-144	huntingtin	Homo sapiens	182-185
25601683-0	2015	Lysine residues in the N-terminal huntingtin amphipathic alpha-helix play a key role in peptide aggregation.	Lysine	0-6	huntingtin	Homo sapiens	34-44
26443925-8	2015	Length of cytosine-adenine-guanine (CAG) repeat in the huntingtin gene was significantly correlated to measures of weight with longer CAG repeats being associated with more severe weight reduction.	cytosine-adenine-guanine	10-34	huntingtin	Homo sapiens	55-65
26443925-8	2015	Length of cytosine-adenine-guanine (CAG) repeat in the huntingtin gene was significantly correlated to measures of weight with longer CAG repeats being associated with more severe weight reduction.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	36-39	huntingtin	Homo sapiens	55-65
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
25601683-2	2015	Here, htt aggregate structure has been examined using hydrogen-deuterium exchange techniques coupled with tandem mass spectrometry.	Hydrogen	54-62	huntingtin	Homo sapiens	6-9
25601683-2	2015	Here, htt aggregate structure has been examined using hydrogen-deuterium exchange techniques coupled with tandem mass spectrometry.	Deuterium	63-72	huntingtin	Homo sapiens	6-9
25601683-8	2015	Evidence for protected residues is observed in the 17-residue N-terminal tract and specifically points to lysine residues as potentially playing a significant role in htt aggregation.	Lysine	106-112	huntingtin	Homo sapiens	167-170
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
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
26865404-0	2014	Effect of 2"-O-methyl/thiophosphonoacetate-modified antisense oligonucleotides on huntingtin expression in patient-derived cells.	2"-o-methyl/thiophosphonoacetate	10-42	huntingtin	Homo sapiens	82-92
26865404-0	2014	Effect of 2"-O-methyl/thiophosphonoacetate-modified antisense oligonucleotides on huntingtin expression in patient-derived cells.	Oligonucleotides	62-78	huntingtin	Homo sapiens	82-92
26865404-3	2014	In this report we examine the potential of thiophosphonoacetate (thioPACE)-modified 2"-O-methyl oligoribonucleotides as inhibitors of human huntingtin (HTT) expression.	thiophosphonoacetate	43-63	huntingtin	Homo sapiens	140-150
26865404-3	2014	In this report we examine the potential of thiophosphonoacetate (thioPACE)-modified 2"-O-methyl oligoribonucleotides as inhibitors of human huntingtin (HTT) expression.	thiophosphonoacetate	43-63	huntingtin	Homo sapiens	152-155
26865404-3	2014	In this report we examine the potential of thiophosphonoacetate (thioPACE)-modified 2"-O-methyl oligoribonucleotides as inhibitors of human huntingtin (HTT) expression.	thiopace	65-73	huntingtin	Homo sapiens	140-150
26865404-3	2014	In this report we examine the potential of thiophosphonoacetate (thioPACE)-modified 2"-O-methyl oligoribonucleotides as inhibitors of human huntingtin (HTT) expression.	thiopace	65-73	huntingtin	Homo sapiens	152-155
26865404-3	2014	In this report we examine the potential of thiophosphonoacetate (thioPACE)-modified 2"-O-methyl oligoribonucleotides as inhibitors of human huntingtin (HTT) expression.	2"-o-methyl oligoribonucleotides	84-116	huntingtin	Homo sapiens	140-150
26865404-3	2014	In this report we examine the potential of thiophosphonoacetate (thioPACE)-modified 2"-O-methyl oligoribonucleotides as inhibitors of human huntingtin (HTT) expression.	2"-o-methyl oligoribonucleotides	84-116	huntingtin	Homo sapiens	152-155
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
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
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
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
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&gt;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&gt;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
25099302-0	2014	BDNF and Huntingtin protein modifications by manganese: implications for striatal medium spiny neuron pathology in manganese neurotoxicity.	Manganese	45-54	huntingtin	Homo sapiens	9-19
25099302-0	2014	BDNF and Huntingtin protein modifications by manganese: implications for striatal medium spiny neuron pathology in manganese neurotoxicity.	Manganese	115-124	huntingtin	Homo sapiens	9-19
25099302-2	2014	The Huntingtin (HTT) gene has been functionally linked to cortical brain-derived neurotrophic factor (BDNF) support of striatal MSNs via phosphorylation at serine 421.	Serine	156-162	huntingtin	Homo sapiens	4-14
25099302-2	2014	The Huntingtin (HTT) gene has been functionally linked to cortical brain-derived neurotrophic factor (BDNF) support of striatal MSNs via phosphorylation at serine 421.	Serine	156-162	huntingtin	Homo sapiens	16-19
25099302-7	2014	Mn exposure decreased serine 421 phosphorylation of Htt in cortical and hippocampal neurons and increased total Htt levels.	Serine	22-28	huntingtin	Homo sapiens	52-55
25358814-2	2014	In Huntington"s disease (HD), a neurodegenerative disease caused by a tri-nucleotide repeat expansion in the huntingtin gene, extensive transcriptional dysregulation has been reported.	tri-nucleotide	70-84	huntingtin	Homo sapiens	109-119
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
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
25351248-6	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
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
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
25149514-0	2014	Huntingtin regulates Ca(2+) chemotaxis and K(+)-facilitated cAMP chemotaxis, in conjunction with the monovalent cation/H(+) exchanger Nhe1, in a model developmental system: insights into its possible role in Huntington s disease.	Cyclic AMP	60-64	huntingtin	Homo sapiens	0-10
25149514-1	2014	Huntington s disease is a neurodegenerative disorder, attributable to an expanded trinucleotide repeat in the coding region of the human HTT gene, which encodes the protein huntingtin.	trinucleotide	82-95	huntingtin	Homo sapiens	137-140
25149514-1	2014	Huntington s disease is a neurodegenerative disorder, attributable to an expanded trinucleotide repeat in the coding region of the human HTT gene, which encodes the protein huntingtin.	trinucleotide	82-95	huntingtin	Homo sapiens	173-183
25034271-1	2014	Huntington disease (HD), the most common inherited cause of chorea, is an autosomal dominant disorder, caused by an expanded trinucleotide CAG repeat (>39) in the HTT gene on chromosome 4p16.3.	trinucleotide	125-138	huntingtin	Homo sapiens	163-166
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
24903509-4	2014	In lipid rafts, interactions of glycosphingolipids, including ganglioside, with proteins may be responsible for the misfolding events that cause the fibril and/or aggregate processing of disease-specific proteins, such as alpha-synuclein, in Parkinson"s disease, huntingtin protein in Huntington"s disease, and copper-zinc superoxide dismutase in amyotrophic lateral sclerosis.	Glycosphingolipids	32-50	huntingtin	Homo sapiens	263-273
24903509-4	2014	In lipid rafts, interactions of glycosphingolipids, including ganglioside, with proteins may be responsible for the misfolding events that cause the fibril and/or aggregate processing of disease-specific proteins, such as alpha-synuclein, in Parkinson"s disease, huntingtin protein in Huntington"s disease, and copper-zinc superoxide dismutase in amyotrophic lateral sclerosis.	Gangliosides	62-73	huntingtin	Homo sapiens	263-273
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	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	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
25642374-0	2014	Trinucleotide repeats and haplotypes at the huntingtin locus in an Indian sample overlaps with European haplogroup a. Huntington"s disease (HD), an autosomal dominant neurodegenerative syndrome, has a world-wide distribution.	trinucleotide	0-13	huntingtin	Homo sapiens	44-54
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
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
25124273-5	2014	Data from genetic HD models indicate that mutant huntingtin disrupts mitochondrial bioenergetics and prevents adenosine triphosphate (ATP) generation, implying altered energy metabolism as an important component of HD pathogenesis.	Adenosine	110-119	huntingtin	Homo sapiens	49-59
25124273-5	2014	Data from genetic HD models indicate that mutant huntingtin disrupts mitochondrial bioenergetics and prevents adenosine triphosphate (ATP) generation, implying altered energy metabolism as an important component of HD pathogenesis.	Adenosine Triphosphate	134-137	huntingtin	Homo sapiens	49-59
25154728-5	2014	In past decades, genetics, the study of DNA sequence variation and its consequences, provided the tools to map the HD gene to chromosome 4 and ultimately to identify its mutation as an expanded CAG trinucleotide repeat in the coding sequence of a large protein, dubbed huntingtin.	trinucleotide	198-211	huntingtin	Homo sapiens	269-279
25155142-2	2014	Among the most promising is reducing expression of mutant huntingtin protein (mHTT) with RNA interference or antisense oligonucleotides; human trials are now being planned.	Oligonucleotides	119-135	huntingtin	Homo sapiens	58-68
25164989-0	2014	Huntingtin-lowering strategies in Huntington"s disease: antisense oligonucleotides, small RNAs, and gene editing.	Oligonucleotides	66-82	huntingtin	Homo sapiens	0-10
25207939-0	2014	Allele-specific suppression of mutant huntingtin using antisense oligonucleotides: providing a therapeutic option for all Huntington disease patients.	Oligonucleotides	65-81	huntingtin	Homo sapiens	38-48
25207939-7	2014	We describe our structure-activity relationship studies for ASO design and find that adjusting the SNP position within the gap, chemical modifications of the wings, and shortening the unmodified gap are critical for potent, specific, and well tolerated silencing of mutant huntingtin.	Oligonucleotides, Antisense	60-63	huntingtin	Homo sapiens	273-283
24895024-0	2014	Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement.	Tryptophan	125-135	huntingtin	Homo sapiens	93-103
24705354-1	2014	HIP14 is the most highly conserved of 23 human palmitoyl acyltransferases (PATs) that catalyze the post-translational addition of palmitate to proteins, including huntingtin (HTT).	Palmitates	130-139	huntingtin	Homo sapiens	163-173
24705354-1	2014	HIP14 is the most highly conserved of 23 human palmitoyl acyltransferases (PATs) that catalyze the post-translational addition of palmitate to proteins, including huntingtin (HTT).	Palmitates	130-139	huntingtin	Homo sapiens	175-178
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
24802331-2	2014	This issue has been addressed in a number of molecular imaging studies by positron emission tomography or single-photon emission computed tomography of serotonin reuptake sites (5-HTT) in the brain of patients with MDD, with strikingly disparate conclusions.	Serotonin	152-161	huntingtin	Homo sapiens	180-183
25210621-13	2014	In contradiction to these observations, it is presumed that miR-10b-5p upregulation in HD exerts a neuroprotective role in response to the mutation in the huntingtin gene.	CHEMBL3740941	68-70	huntingtin	Homo sapiens	155-165
25091984-1	2014	BACKGROUND: In Huntington"s disease (HD), the ratio between normal and mutant Huntingtin (polyQ-hHtt) is crucial in the onset and progression of the disease.	polyq-hhtt	90-100	huntingtin	Homo sapiens	78-88
25091984-2	2014	As a result, addition of normal Htt was shown to improve polyQ-hHtt-induced defects.	polyq-hhtt	57-67	huntingtin	Homo sapiens	32-35
25091984-3	2014	Therefore, we recently identified, within human Htt, a 23aa peptide (P42) that prevents aggregation and polyQ-hHtt-induced phenotypes in HD Drosophila model.	polyq-hhtt	104-114	huntingtin	Homo sapiens	48-51
25054562-6	2014	Importantly the expression of mRNAs of huntingtin is upregulated by repeated applications of serotonin, a modulatory transmitter released during learning in Aplysia.	Serotonin	93-102	huntingtin	Homo sapiens	39-49
25054562-7	2014	Furthermore, we find that huntingtin expression levels are critical, not only in presynaptic sensory neurons, but also in the postsynaptic motor neurons for serotonin-induced long-term facilitation at the sensory-to-motor neuron synapse of the Aplysia gill-withdrawal reflex.	Serotonin	157-166	huntingtin	Homo sapiens	26-36
24646433-3	2014	Huntington disease (HD) is an autosomal dominant disorder caused by an expanded CAG trinucleotide repeat in the Huntingtin gene (HTT).	trinucleotide	84-97	huntingtin	Homo sapiens	112-122
24646433-3	2014	Huntington disease (HD) is an autosomal dominant disorder caused by an expanded CAG trinucleotide repeat in the Huntingtin gene (HTT).	trinucleotide	84-97	huntingtin	Homo sapiens	129-132
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
24603212-5	2014	Mutant Htt expression changes striatal excitatory synaptic activity by decreasing glutamate uptake and increasing signaling at N-methyl-d-aspartate receptors (NMDAR).	Glutamic Acid	82-91	huntingtin	Homo sapiens	7-10
24415136-0	2014	Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations.	Phospholipids	70-82	huntingtin	Homo sapiens	24-34
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
24415136-2	2014	As with other amyloid proteins, misfolding of huntingtin is related to Huntington"s disease through pathways that can involve interactions with phospholipid membranes.	Phospholipids	144-156	huntingtin	Homo sapiens	46-56
24415136-3	2014	Experimental results suggest that the N-terminal 17-amino-acid sequence (htt(NT)) positioned just before the Q(N) region is important for the binding of huntingtin to membranes.	17-amino-acid	49-62	huntingtin	Homo sapiens	153-163
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
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
24976932-1	2014	Huntington"s disease (HD) is a progressive and fatal neurodegenerative disorder caused by an expanded trinucleotide CAG sequence in huntingtin gene (HTT) on chromosome 4.	trinucleotide	102-115	huntingtin	Homo sapiens	132-142
24976932-1	2014	Huntington"s disease (HD) is a progressive and fatal neurodegenerative disorder caused by an expanded trinucleotide CAG sequence in huntingtin gene (HTT) on chromosome 4.	trinucleotide	102-115	huntingtin	Homo sapiens	149-152
24837276-1	2014	We describe the quantitative [2 + 2] photocycloaddition of crystalline trans-2,4-dichloro-6-styrylpyrimidine to produce the corresponding htt r-ctt cyclobutane dimer, and we present (1)H NMR analysis of the photolysis of this and six other mono-, di-, and triazastilbenes in solid and solution states.	trans-2,4-dichloro-6-styrylpyrimidine	71-108	huntingtin	Homo sapiens	138-141
24837276-1	2014	We describe the quantitative [2 + 2] photocycloaddition of crystalline trans-2,4-dichloro-6-styrylpyrimidine to produce the corresponding htt r-ctt cyclobutane dimer, and we present (1)H NMR analysis of the photolysis of this and six other mono-, di-, and triazastilbenes in solid and solution states.	r-ctt cyclobutane	142-159	huntingtin	Homo sapiens	138-141
24837276-1	2014	We describe the quantitative [2 + 2] photocycloaddition of crystalline trans-2,4-dichloro-6-styrylpyrimidine to produce the corresponding htt r-ctt cyclobutane dimer, and we present (1)H NMR analysis of the photolysis of this and six other mono-, di-, and triazastilbenes in solid and solution states.	mono-, di-, and triazastilbenes	240-271	huntingtin	Homo sapiens	138-141
24837276-3	2014	These energies mirror the relative polarization of the stilbene moieties and can be quantitatively correlated with the rate of reaction and selective formation of the htt r-ctt dimers.	Stilbenes	55-63	huntingtin	Homo sapiens	167-170
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
24452335-2	2014	HD is caused by a trinucleotide CAG repeat expansion that encodes a polyglutamine stretch in the huntingtin (HTT) protein.	trinucleotide	18-31	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.	trinucleotide	18-31	huntingtin	Homo sapiens	109-112
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
24459296-4	2014	We now demonstrate the existence of a new post-translational modification of HTT: the addition of the 14 carbon fatty acid myristate to a glycine residue exposed on a caspase-3-cleaved fragment (post-translational myristoylation) and that myristoylation of this fragment is altered in a physiologically relevant model of mutant HTT.	carbon fatty acid	105-122	huntingtin	Homo sapiens	77-80
24459296-4	2014	We now demonstrate the existence of a new post-translational modification of HTT: the addition of the 14 carbon fatty acid myristate to a glycine residue exposed on a caspase-3-cleaved fragment (post-translational myristoylation) and that myristoylation of this fragment is altered in a physiologically relevant model of mutant HTT.	carbon fatty acid	105-122	huntingtin	Homo sapiens	328-331
24459296-4	2014	We now demonstrate the existence of a new post-translational modification of HTT: the addition of the 14 carbon fatty acid myristate to a glycine residue exposed on a caspase-3-cleaved fragment (post-translational myristoylation) and that myristoylation of this fragment is altered in a physiologically relevant model of mutant HTT.	Glycine	138-145	huntingtin	Homo sapiens	77-80
24459296-4	2014	We now demonstrate the existence of a new post-translational modification of HTT: the addition of the 14 carbon fatty acid myristate to a glycine residue exposed on a caspase-3-cleaved fragment (post-translational myristoylation) and that myristoylation of this fragment is altered in a physiologically relevant model of mutant HTT.	Glycine	138-145	huntingtin	Homo sapiens	328-331
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
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
24436303-7	2014	Here, we show that highly selective pharmacological inhibition of Drosophila Sir2 and mammalian SirT1 using the novel inhibitor selisistat (selisistat; 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide) can suppress HD pathology caused by mutant huntingtin exon 1 fragments in Drosophila, mammalian cells and mice.	6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide	128-138	huntingtin	Homo sapiens	251-261
24436303-7	2014	Here, we show that highly selective pharmacological inhibition of Drosophila Sir2 and mammalian SirT1 using the novel inhibitor selisistat (selisistat; 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide) can suppress HD pathology caused by mutant huntingtin exon 1 fragments in Drosophila, mammalian cells and mice.	6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide	140-150	huntingtin	Homo sapiens	251-261
24436303-7	2014	Here, we show that highly selective pharmacological inhibition of Drosophila Sir2 and mammalian SirT1 using the novel inhibitor selisistat (selisistat; 6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide) can suppress HD pathology caused by mutant huntingtin exon 1 fragments in Drosophila, mammalian cells and mice.	6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide	152-206	huntingtin	Homo sapiens	251-261
24741770-2	2014	Studies have revealed that mutant huntingtin, polyglutamine-expanded ataxin-1 and ataxin-3 can cause elevated levels of reactive oxygen species in neuronal cells.	Oxygen	129-135	huntingtin	Homo sapiens	34-44
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
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).	trinucleotide	23-36	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).	trinucleotide	23-36	huntingtin	Homo sapiens	83-93
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
24334607-5	2014	The ability to form one or the other type of inclusion can be influenced by the phosphorylation state of serine residues at amino acid positions 13 and 16 within the huntingtin protein.	Serine	105-111	huntingtin	Homo sapiens	166-176
24334607-7	2014	We hypothesize that the protective effect of N17 phosphorylation or phospho-mimicry seen in animal models, at the level of protein inclusions with elevated huntingtin levels, is to induce a conformation of the huntingtin amino-terminus that causes fragments to form tightly packed inclusions that do not exit the insoluble phase, and hence exert less toxicity.	3-(4-Methyl-1h-Imidazol-1-Yl)-N-[4-(Pyridin-4-Yloxy)phenyl]benzamide	45-48	huntingtin	Homo sapiens	156-166
24334607-7	2014	We hypothesize that the protective effect of N17 phosphorylation or phospho-mimicry seen in animal models, at the level of protein inclusions with elevated huntingtin levels, is to induce a conformation of the huntingtin amino-terminus that causes fragments to form tightly packed inclusions that do not exit the insoluble phase, and hence exert less toxicity.	3-(4-Methyl-1h-Imidazol-1-Yl)-N-[4-(Pyridin-4-Yloxy)phenyl]benzamide	45-48	huntingtin	Homo sapiens	210-220
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
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
24525128-6	2014	In primary oligodendrocytes, mutant huntingtin inhibits the regulatory effect of PGC1alpha on cholesterol metabolism and the expression of Myelin Basic Protein.	Cholesterol	94-105	huntingtin	Homo sapiens	36-46
24374792-6	2014	The fact remains that the mutant Htt protein was seen to be associated with mitochondria directly, and as the striatum is highly enriched with dopamine and glutamate, it may make the striatal mitochondria more vulnerable because of the presence of dopa-quinones, and due to an imbalance in Ca(2+).	Dopamine	143-151	huntingtin	Homo sapiens	33-36
24374792-6	2014	The fact remains that the mutant Htt protein was seen to be associated with mitochondria directly, and as the striatum is highly enriched with dopamine and glutamate, it may make the striatal mitochondria more vulnerable because of the presence of dopa-quinones, and due to an imbalance in Ca(2+).	Glutamic Acid	156-165	huntingtin	Homo sapiens	33-36
24374792-6	2014	The fact remains that the mutant Htt protein was seen to be associated with mitochondria directly, and as the striatum is highly enriched with dopamine and glutamate, it may make the striatal mitochondria more vulnerable because of the presence of dopa-quinones, and due to an imbalance in Ca(2+).	Dihydroxyphenylalanine	143-147	huntingtin	Homo sapiens	33-36
24374792-6	2014	The fact remains that the mutant Htt protein was seen to be associated with mitochondria directly, and as the striatum is highly enriched with dopamine and glutamate, it may make the striatal mitochondria more vulnerable because of the presence of dopa-quinones, and due to an imbalance in Ca(2+).	Quinones	253-261	huntingtin	Homo sapiens	33-36
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
24711024-2	2014	METHODS: Concentration gradients of betaine were introduced into the sequencing system by taking the 5" terminal of Nogo-B cDNA (Am-Nogo-B) (G-C%=72%, without trinucleotide repeats) and 5" terminal of Huntingtin cDNA (Am-HTT) (G-C%=74%, with abundant CAG and CCG repeats) the results of sequencing were compared.	Betaine	36-43	huntingtin	Homo sapiens	201-211
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
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.	Galactose	161-170	huntingtin	Homo sapiens	50-60
24296361-1	2014	Huntington"s disease is an inherited disorder caused by expanded stretch of consecutive trinucleotides (cytosine-adenosine-guanine, CAG) within the first exon of the huntingtin (HTT) gene on chromosome 4 (p16.3).	trinucleotides	88-102	huntingtin	Homo sapiens	166-176
24296361-1	2014	Huntington"s disease is an inherited disorder caused by expanded stretch of consecutive trinucleotides (cytosine-adenosine-guanine, CAG) within the first exon of the huntingtin (HTT) gene on chromosome 4 (p16.3).	trinucleotides	88-102	huntingtin	Homo sapiens	178-181
24296361-1	2014	Huntington"s disease is an inherited disorder caused by expanded stretch of consecutive trinucleotides (cytosine-adenosine-guanine, CAG) within the first exon of the huntingtin (HTT) gene on chromosome 4 (p16.3).	Adenosine	113-122	huntingtin	Homo sapiens	166-176
24296361-1	2014	Huntington"s disease is an inherited disorder caused by expanded stretch of consecutive trinucleotides (cytosine-adenosine-guanine, CAG) within the first exon of the huntingtin (HTT) gene on chromosome 4 (p16.3).	Adenosine	113-122	huntingtin	Homo sapiens	178-181
24296361-1	2014	Huntington"s disease is an inherited disorder caused by expanded stretch of consecutive trinucleotides (cytosine-adenosine-guanine, CAG) within the first exon of the huntingtin (HTT) gene on chromosome 4 (p16.3).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	132-135	huntingtin	Homo sapiens	166-176
24296361-1	2014	Huntington"s disease is an inherited disorder caused by expanded stretch of consecutive trinucleotides (cytosine-adenosine-guanine, CAG) within the first exon of the huntingtin (HTT) gene on chromosome 4 (p16.3).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	132-135	huntingtin	Homo sapiens	178-181
24505464-0	2014	Phosphorylation of mutant huntingtin at serine 116 modulates neuronal toxicity.	Serine	40-46	huntingtin	Homo sapiens	26-36
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	18-28
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
24196395-1	2014	Huntington disease is a monogenic, autosomal dominant, progressive neurodegenerative disorder caused by a trinucleotide CAG repeat expansion in exon 1 of the huntingtin (HTT) gene; age of onset of clinical symptoms inversely correlates with expanded CAG repeat length.	trinucleotide	106-119	huntingtin	Homo sapiens	158-168
24196395-1	2014	Huntington disease is a monogenic, autosomal dominant, progressive neurodegenerative disorder caused by a trinucleotide CAG repeat expansion in exon 1 of the huntingtin (HTT) gene; age of onset of clinical symptoms inversely correlates with expanded CAG repeat length.	trinucleotide	106-119	huntingtin	Homo sapiens	170-173
24346757-6	2014	Maximal predicted reuptake inhibition for 5-HTT was 84% for duloxetine and 80% for escitalopram, and that for NET was 67% and 14%, respectively.	Duloxetine Hydrochloride	60-70	huntingtin	Homo sapiens	44-47
24346757-6	2014	Maximal predicted reuptake inhibition for 5-HTT was 84% for duloxetine and 80% for escitalopram, and that for NET was 67% and 14%, respectively.	Citalopram	83-95	huntingtin	Homo sapiens	44-47
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
24333873-7	2014	In addition, we systemically administered baclofen to a HD model containing the entire human huntingtin gene with 128 CAG repeats (YAC128).	Baclofen	42-50	huntingtin	Homo sapiens	93-103
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
24556732-8	2014	We show that peanut leaves contain a hydroxycinnamoyl-CoA:tartaric acid hydroxycinnamoyl transferase (HTT) activity capable of transferring p-coumaroyl, caffeoyl, and feruloyl moieties from CoA to tartaric acid (specific activities of 11 +- 2.8, 8 +- 1.8, 4 +- 0.8 pkat mg(-1) crude protein, respectively).	p-coumaroyl	140-151	huntingtin	Homo sapiens	102-105
24556732-8	2014	We show that peanut leaves contain a hydroxycinnamoyl-CoA:tartaric acid hydroxycinnamoyl transferase (HTT) activity capable of transferring p-coumaroyl, caffeoyl, and feruloyl moieties from CoA to tartaric acid (specific activities of 11 +- 2.8, 8 +- 1.8, 4 +- 0.8 pkat mg(-1) crude protein, respectively).	caffeoyl	153-161	huntingtin	Homo sapiens	102-105
24556732-8	2014	We show that peanut leaves contain a hydroxycinnamoyl-CoA:tartaric acid hydroxycinnamoyl transferase (HTT) activity capable of transferring p-coumaroyl, caffeoyl, and feruloyl moieties from CoA to tartaric acid (specific activities of 11 +- 2.8, 8 +- 1.8, 4 +- 0.8 pkat mg(-1) crude protein, respectively).	Coenzyme A	54-57	huntingtin	Homo sapiens	102-105
24556732-8	2014	We show that peanut leaves contain a hydroxycinnamoyl-CoA:tartaric acid hydroxycinnamoyl transferase (HTT) activity capable of transferring p-coumaroyl, caffeoyl, and feruloyl moieties from CoA to tartaric acid (specific activities of 11 +- 2.8, 8 +- 1.8, 4 +- 0.8 pkat mg(-1) crude protein, respectively).	tartaric acid	58-71	huntingtin	Homo sapiens	102-105
24556732-9	2014	The HTT activity was used to make cis- and trans-p-coumaroyl- and -feruloyl-tartaric acid in vitro.	cis- and trans-p-coumaroyl- and -feruloyl-tartaric acid	34-89	huntingtin	Homo sapiens	4-7
24556732-14	2014	An HTT gene could also provide a means by genetic engineering for producing caffeoyl- and other hydroxycinnamoyl-tartaric acid esters in forage crops that lack them.	caffeoyl- and	76-89	huntingtin	Homo sapiens	3-6
24556732-14	2014	An HTT gene could also provide a means by genetic engineering for producing caffeoyl- and other hydroxycinnamoyl-tartaric acid esters in forage crops that lack them.	hydroxycinnamoyl-tartaric acid esters	96-133	huntingtin	Homo sapiens	3-6
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
24412394-0	2014	Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.	Proline	91-98	huntingtin	Homo sapiens	114-124
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
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
24412394-5	2014	This autoinhibitory structure regulates interaction between the WW domain of HYPB and the proline-rich region (PRR) of Htt, as evidenced by NMR and immunofluorescence techniques.	Proline	90-97	huntingtin	Homo sapiens	119-122
24459107-7	2014	Glucan-encapsulated small interfering RNA particles were used to lower huntingtin levels in human Huntington"s disease monocytes/macrophages, resulting in a reversal of huntingtin-induced elevated cytokine production and transcriptional changes.	Glucans	0-6	huntingtin	Homo sapiens	71-81
24459107-7	2014	Glucan-encapsulated small interfering RNA particles were used to lower huntingtin levels in human Huntington"s disease monocytes/macrophages, resulting in a reversal of huntingtin-induced elevated cytokine production and transcriptional changes.	Glucans	0-6	huntingtin	Homo sapiens	169-179
24459107-8	2014	These findings improve our understanding of the role of innate immunity in neurodegeneration, introduce glucan-encapsulated small interfering RNA particles as tool for studying cellular pathogenesis ex vivo in human cells and raise the prospect of immune cell-directed HTT-lowering as a therapeutic in Huntington"s disease.	Glucans	104-110	huntingtin	Homo sapiens	269-272
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
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
24587280-7	2014	Epoxomicin increases the activated caspase-3, HSP70, huntingtin, ubiquitinated proteins and ROS levels in both HD and controls.	epoxomicin	0-10	huntingtin	Homo sapiens	53-63
24587280-8	2014	Treatment with trehalose counteracts the increase in ROS, ubiquitinated proteins, huntingtin and activated caspase-3 levels induced by epoxomicin, and also increases the LC3 levels more in HD fibroblast than controls.	Trehalose	15-24	huntingtin	Homo sapiens	82-92
24587280-8	2014	Treatment with trehalose counteracts the increase in ROS, ubiquitinated proteins, huntingtin and activated caspase-3 levels induced by epoxomicin, and also increases the LC3 levels more in HD fibroblast than controls.	epoxomicin	135-145	huntingtin	Homo sapiens	82-92
24503862-1	2014	Huntington"s disease (HD) is a devastating, genetic neurodegenerative disease caused by a tri-nucleotide expansion in exon 1 of the huntingtin gene.	tri-nucleotide	90-104	huntingtin	Homo sapiens	132-142
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
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
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
24169003-0	2014	Accelerating the clearance of mutant huntingtin protein aggregates through autophagy induction by europium hydroxide nanorods.	europium hydroxide	98-116	huntingtin	Homo sapiens	37-47
24169003-3	2014	In the present article, we have demonstrated that europium hydroxide [Eu(III)(OH)3] nanorods can reduce huntingtin protein aggregation (EGFP-tagged huntingtin protein with 74 polyQ repeats), responsible for neurodegenerative diseases.	europium hydroxide	50-68	huntingtin	Homo sapiens	104-114
24169003-3	2014	In the present article, we have demonstrated that europium hydroxide [Eu(III)(OH)3] nanorods can reduce huntingtin protein aggregation (EGFP-tagged huntingtin protein with 74 polyQ repeats), responsible for neurodegenerative diseases.	europium hydroxide	50-68	huntingtin	Homo sapiens	148-158
24169003-5	2014	Furthermore, depression of protein aggregation clearance through the autophagy blockade has also been observed by using specific inhibitors (wortmannin and chloroquine), indicating that autophagy is involved in the degradation of huntingtin protein aggregation.	Wortmannin	141-151	huntingtin	Homo sapiens	230-240
24169003-5	2014	Furthermore, depression of protein aggregation clearance through the autophagy blockade has also been observed by using specific inhibitors (wortmannin and chloroquine), indicating that autophagy is involved in the degradation of huntingtin protein aggregation.	Chloroquine	156-167	huntingtin	Homo sapiens	230-240
24968783-3	2014	The cause is an expansion in CAG (glutamine) repeats in the HTT gene.	Glutamine	34-43	huntingtin	Homo sapiens	60-63
24266403-3	2013	Here we test how UNA substitutions affect allele-selective inhibition of expression of trinucleotide repeat genes Huntingtin (HTT) and Ataxin-3 (ATX-3).	trinucleotide	87-100	huntingtin	Homo sapiens	114-124
24266403-3	2013	Here we test how UNA substitutions affect allele-selective inhibition of expression of trinucleotide repeat genes Huntingtin (HTT) and Ataxin-3 (ATX-3).	trinucleotide	87-100	huntingtin	Homo sapiens	126-129
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
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
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.	Calcium	187-194	huntingtin	Homo sapiens	109-119
24330821-8	2013	The mitochondrial impairment observed in mutant cells and cortical neurons expressing Q104-GFP was prevented by pre-treatment with cyclosporine A (CsA) but not by FK506 (an inhibitor of calcineurin), indicating a potential role for mPTP opening in the mitochondrial dysfunction induced by calcium stress in mutant huntingtin cells.	Cyclosporine	131-145	huntingtin	Homo sapiens	314-324
24330821-8	2013	The mitochondrial impairment observed in mutant cells and cortical neurons expressing Q104-GFP was prevented by pre-treatment with cyclosporine A (CsA) but not by FK506 (an inhibitor of calcineurin), indicating a potential role for mPTP opening in the mitochondrial dysfunction induced by calcium stress in mutant huntingtin cells.	Cyclosporine	147-150	huntingtin	Homo sapiens	314-324
24532984-11	2013	In PD, polymorphisms of the COMT, MAO, DAT, NET, and 5- HTT genes may change the levels of biogenic amines and their metabolic products.	Amines	100-106	huntingtin	Homo sapiens	56-59
24165128-0	2013	Lithium down-regulates histone deacetylase 1 (HDAC1) and induces degradation of mutant huntingtin.	Lithium	0-7	huntingtin	Homo sapiens	87-97
24165128-6	2013	We also showed that depletion of HDAC1 is essential for the neuroprotective effects of lithium and for the lithium-mediated degradation of mutant huntingtin through the autophagic pathway.	Lithium	107-114	huntingtin	Homo sapiens	146-156
24555239-1	2013	BACKGROUND: Huntington"s disease is a progressive neurodegenerative disease, genetically determined by CAG trinucleotide expansions in the IT15 gene.	trinucleotide	107-120	huntingtin	Homo sapiens	139-143
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
23893755-1	2013	The 17- amino acid N-terminal segment of the Huntingtin protein, htt(NT), grows into stable alpha-helix rich oligomeric aggregates when incubated under physiological conditions.	17- amino acid	4-18	huntingtin	Homo sapiens	45-55
23893755-1	2013	The 17- amino acid N-terminal segment of the Huntingtin protein, htt(NT), grows into stable alpha-helix rich oligomeric aggregates when incubated under physiological conditions.	17- amino acid	4-18	huntingtin	Homo sapiens	65-68
23906595-1	2013	Huntington"s disease (HD) is a neurodegenerative disease caused by cytosine-adenine-guanine (CAG)-repeat expansion in the huntingtin (HTT) gene.	cytosine-adenine-guanine	67-91	huntingtin	Homo sapiens	122-132
23906595-1	2013	Huntington"s disease (HD) is a neurodegenerative disease caused by cytosine-adenine-guanine (CAG)-repeat expansion in the huntingtin (HTT) gene.	cytosine-adenine-guanine	67-91	huntingtin	Homo sapiens	134-137
23906595-1	2013	Huntington"s disease (HD) is a neurodegenerative disease caused by cytosine-adenine-guanine (CAG)-repeat expansion in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	93-96	huntingtin	Homo sapiens	122-132
23906595-1	2013	Huntington"s disease (HD) is a neurodegenerative disease caused by cytosine-adenine-guanine (CAG)-repeat expansion in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	93-96	huntingtin	Homo sapiens	134-137
23963702-0	2013	Rational design of antisense oligonucleotides targeting single nucleotide polymorphisms for potent and allele selective suppression of mutant Huntingtin in the CNS.	Oligonucleotides	29-45	huntingtin	Homo sapiens	142-152
23963702-6	2013	The resulting oligonucleotides demonstrate >100-fold discrimination for a single nucleotide change at an SNP site in the disease causing huntingtin mRNA, in patient cells and in a completely humanized mouse model of HD.	Oligonucleotides	14-30	huntingtin	Homo sapiens	137-147
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
23641925-4	2013	RESULTS: We found that expression of mutant huntingtin (mutHTT) protein in primary cultured neurons triggers significant production of nitric oxide (NO).	Nitric Oxide	135-147	huntingtin	Homo sapiens	44-54
23463025-1	2013	Huntington disease (HD) is a neurodegenerative disorder resulting from the expansion of a CAG trinucleotide repeat in the huntingtin (HTT) gene.	trinucleotide	94-107	huntingtin	Homo sapiens	122-132
23463025-1	2013	Huntington disease (HD) is a neurodegenerative disorder resulting from the expansion of a CAG trinucleotide repeat in the huntingtin (HTT) gene.	trinucleotide	94-107	huntingtin	Homo sapiens	134-137
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
24278347-1	2013	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by the expansion of a CAG trinucleotide repeat in the HTT gene encoding huntingtin.	trinucleotide	111-124	huntingtin	Homo sapiens	139-142
24278347-1	2013	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by the expansion of a CAG trinucleotide repeat in the HTT gene encoding huntingtin.	trinucleotide	111-124	huntingtin	Homo sapiens	157-167
23601559-3	2013	Serotonin (5-HT) has been shown to be involved in PH by inducing PASMC proliferation through the activation of 5-HT1B receptors (5-HT1BR) and 5-HT transporter (5-HTT).	Serotonin	0-9	huntingtin	Homo sapiens	162-165
23601559-3	2013	Serotonin (5-HT) has been shown to be involved in PH by inducing PASMC proliferation through the activation of 5-HT1B receptors (5-HT1BR) and 5-HT transporter (5-HTT).	pasmc	65-70	huntingtin	Homo sapiens	162-165
23601559-5	2013	Therefore, we hypothesized that 5-HT induces decreases in PASMC apoptosis through 5-HT1BR and 5-HTT.	pasmc	58-63	huntingtin	Homo sapiens	96-99
23601559-9	2013	The effects of 5-HT on the proliferation and apoptosis of PASMCs were similar to those of 5-HT1BR agonists and were markedly prevented by 5-HT1BR antagonist, 5-HTT antagonist, combined 5-HT1BR/5-HTT antagonists, EPI, or DCA.	pasmcs	58-64	huntingtin	Homo sapiens	160-163
23601559-9	2013	The effects of 5-HT on the proliferation and apoptosis of PASMCs were similar to those of 5-HT1BR agonists and were markedly prevented by 5-HT1BR antagonist, 5-HTT antagonist, combined 5-HT1BR/5-HTT antagonists, EPI, or DCA.	pasmcs	58-64	huntingtin	Homo sapiens	195-198
23601559-10	2013	CONCLUSIONS: 5-HT inhibits PASMC apoptosis through 5-HT1BR or 5-HTT.	pasmc	27-32	huntingtin	Homo sapiens	64-67
23601559-11	2013	pERK1/2 and PDK are involved in the process of 5-HT inhibition PASMC apoptosis through 5-HT1BR or 5-HTT.	pasmc	63-68	huntingtin	Homo sapiens	100-103
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
23966247-0	2013	HTRF analysis of soluble huntingtin in PHAROS PBMCs.	pharos	39-45	huntingtin	Homo sapiens	25-35
23966247-7	2013	CONCLUSIONS: The HTRF assay can effectively measure mtHtt in multicenter sample sets and may be useful in trials of therapies targeting huntingtin.	mthtt	52-57	huntingtin	Homo sapiens	136-146
23908352-0	2013	Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes.	polyglutamine	9-22	huntingtin	Homo sapiens	45-55
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
23898200-4	2013	Using Forster resonance energy transfer, we describe an intramolecular proximity between the N17 domain and the downstream polyproline region that flanks the polyglutamine tract of huntingtin.	polyproline	123-134	huntingtin	Homo sapiens	181-191
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	trinucleotide	68-81	huntingtin	Homo sapiens	130-140
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	trinucleotide	68-81	huntingtin	Homo sapiens	147-150
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
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	trinucleotide	68-81	huntingtin	Homo sapiens	169-179
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	trinucleotide	68-81	huntingtin	Homo sapiens	189-192
23975930-0	2013	A flexible polyglutamine hinge opens new doors for understanding huntingtin function.	polyglutamine	11-24	huntingtin	Homo sapiens	65-75
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
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	cytosine-adenine-guanine	87-111	huntingtin	Homo sapiens	130-140
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
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	cytosine-adenine-guanine	87-111	huntingtin	Homo sapiens	147-150
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	cytosine-adenine-guanine	87-111	huntingtin	Homo sapiens	169-179
23953200-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by trinucleotide CAG (Cytosine-Adenine-Guanine) expansion on the Huntingtin gene (HTT) encoding for the Huntingtin protein (Htt).	cytosine-adenine-guanine	87-111	huntingtin	Homo sapiens	189-192
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
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
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
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
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
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.	Peptides	51-59	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
23931318-3	2013	Here, we determined the high-resolution structure of huntingtin 1-17 in dodecyl phosphocholine micelles and the topology of its helical domain in oriented phosphatidylcholine bilayers.	dodecylphosphocholine	72-94	huntingtin	Homo sapiens	53-63
23931318-3	2013	Here, we determined the high-resolution structure of huntingtin 1-17 in dodecyl phosphocholine micelles and the topology of its helical domain in oriented phosphatidylcholine bilayers.	Phosphatidylcholines	155-174	huntingtin	Homo sapiens	53-63
23931318-5	2013	In a next step a set of four solid-state NMR angular restraints was obtained from huntingtin 1-17 labeled with (15)N and (2)H at selected sites.	Nitrogen	41-42	huntingtin	Homo sapiens	82-92
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
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
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
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