PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
18845944-0	2008	A function of huntingtin in guanine nucleotide exchange on Rab11.	Guanine Nucleotides	28-46	huntingtin	Mus musculus	14-24
18845944-6	2008	In brain membranes, an antibody against huntingtin immunoprecipitated a nucleotide exchange activity on Rab11 and huntingtin was coprecipitated with Rab11 in the presence of guanosine diphosphate.	Guanosine Diphosphate	174-195	huntingtin	Mus musculus	40-50
18845944-6	2008	In brain membranes, an antibody against huntingtin immunoprecipitated a nucleotide exchange activity on Rab11 and huntingtin was coprecipitated with Rab11 in the presence of guanosine diphosphate.	Guanosine Diphosphate	174-195	huntingtin	Mus musculus	114-124
18632688-1	2008	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disease caused by an expanded polyglutamine tract in the ubiquitously expressed huntingtin protein.	polyglutamine	99-112	huntingtin	Mus musculus	149-159
18658163-7	2008	More importantly, we were able to demonstrate that blocking the expression of a specific isoform of ASIC (asic1a), one of the many molecular targets of Ben, led to an enhancement of UPS activity and this blockade also decreased htt-polyQ aggregation in the striatum of R6/2 mice.	polyglutamine	232-237	huntingtin	Mus musculus	228-231
18558632-1	2008	A number of mouse models expressing mutant huntingtin (htt) with an expanded polyglutamine (polyQ) domain are useful for studying the pathogenesis of Huntington"s disease (HD) and identifying appropriate therapies.	polyglutamine	77-90	huntingtin	Mus musculus	43-53
18721135-2	2008	In the present study, the formation of inclusions caused by the mutation of huntingtin protein and its relationship with changes in energy metabolism and with pathological alterations were investigated both in transgenic and 3-nitropropionic acid-treated mouse models for HD.	3-nitropropionic acid	225-246	huntingtin	Mus musculus	76-86
18721135-11	2008	We then used the mathematical model to develop a hypothesis for a new regulatory interaction that might account for the observed changes; in HD, glyceraldehyde-3-phosphate dehydrogenase may be in closer proximity (perhaps because of the binding of glyceraldehyde-3-phosphate dehydrogenase to huntingtin) with aldolase and engage in channelling for glyceraldehyde-3-phosphate.	Glyceraldehyde 3-Phosphate	145-171	huntingtin	Mus musculus	292-302
18650014-1	2008	Huntington"s disease (HD) is an autosomal dominant inheritable neurodegenerative disorder caused by expansion of a polyglutamine repeat in the amino-terminal region of huntingtin.	polyglutamine	115-128	huntingtin	Mus musculus	168-178
18650014-2	2008	Polyglutamine expansion causes mutant huntingtin to aggregate and accumulate in the nuclei and cytoplasm of neurons.	polyglutamine	0-13	huntingtin	Mus musculus	38-48
18650014-5	2008	We established stably transfected mouse neuroblastoma (N2a) cells that express soluble amino-terminal fragments of huntingtin containing 20 (20Q) or 150 (150Q) glutamine repeats.	Glutamine	160-169	huntingtin	Mus musculus	115-125
18558632-1	2008	A number of mouse models expressing mutant huntingtin (htt) with an expanded polyglutamine (polyQ) domain are useful for studying the pathogenesis of Huntington"s disease (HD) and identifying appropriate therapies.	polyglutamine	77-90	huntingtin	Mus musculus	55-58
18558632-1	2008	A number of mouse models expressing mutant huntingtin (htt) with an expanded polyglutamine (polyQ) domain are useful for studying the pathogenesis of Huntington"s disease (HD) and identifying appropriate therapies.	polyglutamine	92-97	huntingtin	Mus musculus	43-53
18558632-1	2008	A number of mouse models expressing mutant huntingtin (htt) with an expanded polyglutamine (polyQ) domain are useful for studying the pathogenesis of Huntington"s disease (HD) and identifying appropriate therapies.	polyglutamine	92-97	huntingtin	Mus musculus	55-58
18558632-6	2008	Similarly, transgenic monkeys expressing exon-1 htt with a 147-glutamine repeat (147Q) died early and showed abundant neuropil aggregates in swelling neuronal processes.	Glutamine	63-72	huntingtin	Mus musculus	48-51
18602275-0	2008	CEP-1347 reduces mutant huntingtin-associated neurotoxicity and restores BDNF levels in R6/2 mice.	3,9-bis((ethylthio)methyl)-K-252a	0-8	huntingtin	Mus musculus	24-34
18602275-1	2008	Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expanded polyglutamine repeat within the protein Huntingtin (Htt).	polyglutamine	92-105	huntingtin	Mus musculus	132-142
18602275-1	2008	Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expanded polyglutamine repeat within the protein Huntingtin (Htt).	polyglutamine	92-105	huntingtin	Mus musculus	144-147
18669659-1	2008	Huntington"s disease is a dominant autosomal neurodegenerative disorder caused by an expansion of polyglutamines in the huntingtin (Htt) protein, whose cellular function remains controversial.	polyglutamine	98-112	huntingtin	Mus musculus	120-130
18669659-1	2008	Huntington"s disease is a dominant autosomal neurodegenerative disorder caused by an expansion of polyglutamines in the huntingtin (Htt) protein, whose cellular function remains controversial.	polyglutamine	98-112	huntingtin	Mus musculus	132-135
18400759-1	2008	The pathogenesis of Huntington disease (HD) is attributed to the misfolding of huntingtin (htt) caused by an expanded polyglutamine (polyQ) domain.	polyglutamine	118-131	huntingtin	Mus musculus	79-89
18502655-2	2008	The molecular trigger of HD is a polyglutamine expansion in the Huntingtin protein (Htt).	polyglutamine	33-46	huntingtin	Mus musculus	64-74
18502655-2	2008	The molecular trigger of HD is a polyglutamine expansion in the Huntingtin protein (Htt).	polyglutamine	33-46	huntingtin	Mus musculus	84-87
18502655-4	2008	Other lines of investigation suggest that expression of mutant Htt facilitates activity of the NR2B subtype of NMDA receptors and the type 1 inositol 1,4,5-trisphosphate receptors (InsP(3)R1), and that disturbed calcium (Ca(2+)) signaling causes apoptosis of MSNs in HD.	Calcium	212-219	huntingtin	Mus musculus	63-66
18187350-1	2008	Mice lacking the serotonin-transporter (5-HTT-/- mice) develop reduced thermal hyperalgesia after nerve injury, concomitant with reduced serotonin (5-HT) levels in nervous tissue.	Serotonin	17-26	huntingtin	Mus musculus	42-45
18445618-7	2008	Cell stress induced by staurosporine results in the nuclear translocation and activation of C6 and an increase in 586 amino acid fragments of huntingtin in the nucleus.	Staurosporine	23-36	huntingtin	Mus musculus	142-152
18400759-1	2008	The pathogenesis of Huntington disease (HD) is attributed to the misfolding of huntingtin (htt) caused by an expanded polyglutamine (polyQ) domain.	polyglutamine	118-131	huntingtin	Mus musculus	91-94
18400759-1	2008	The pathogenesis of Huntington disease (HD) is attributed to the misfolding of huntingtin (htt) caused by an expanded polyglutamine (polyQ) domain.	polyglutamine	133-138	huntingtin	Mus musculus	79-89
18400759-1	2008	The pathogenesis of Huntington disease (HD) is attributed to the misfolding of huntingtin (htt) caused by an expanded polyglutamine (polyQ) domain.	polyglutamine	133-138	huntingtin	Mus musculus	91-94
18221365-0	2008	Calcineurin is involved in the early activation of NMDA-mediated cell death in mutant huntingtin knock-in striatal cells.	N-Methylaspartate	51-55	huntingtin	Mus musculus	86-96
18293418-1	2008	Huntington"s disease (HD) is a neurodegenerative disorder caused by an elongation of CAG repeats in the HD gene, which encodes a mutant copy of huntingtin with an expanded polyglutatmine repeat.	polyglutatmine	172-186	huntingtin	Mus musculus	144-154
18395459-2	2008	We previously screened the 1040 FDA-approved compounds from the NINDS compound library and found that a compound, nipecotic acid, significantly reduced mutant huntingtin aggregations and blocked cell toxicity in an inducible cell model of HD.	nipecotic acid	114-128	huntingtin	Mus musculus	159-169
18221365-8	2008	Notably, addition of the calcineurin inhibitor FK-506 produced a more robust reduction in cell death in mutant huntingtin knock-in cells than it did in wild-type cells.	Tacrolimus	47-53	huntingtin	Mus musculus	111-121
18241051-4	2008	Another group recently reported that HRD1 suppresses the toxicity of polyglutamine-expanded huntingtin.	polyglutamine	69-82	huntingtin	Mus musculus	92-102
17949690-7	2008	RESULTS: Mice experiencing low maternal care showed deficient gamma-aminobutyric acid-A receptor binding in the amygdala and 5-HTT heterozygous null mice showed decreased serotonin turnover in hippocampus and striatum.	Serotonin	171-180	huntingtin	Mus musculus	127-130
18412970-1	2008	BACKGROUND: The polyglutamine expansion in huntingtin (Htt) protein is a cause of Huntington"s disease (HD).	polyglutamine	16-29	huntingtin	Mus musculus	55-58
18412970-5	2008	The function of Htt in calcium (Ca2+) signaling was analyzed in Ca2+ imaging experiments with generated cell lines.	Calcium	23-30	huntingtin	Mus musculus	16-19
18398004-1	2008	Huntington"s disease (HD) is a fatal, dominant neurodegenerative disease caused by a polyglutamine repeat expansion in exon 1 of the HD gene, which encodes the huntingtin protein.	polyglutamine	85-98	huntingtin	Mus musculus	160-170
18412970-1	2008	BACKGROUND: The polyglutamine expansion in huntingtin (Htt) protein is a cause of Huntington"s disease (HD).	polyglutamine	16-29	huntingtin	Mus musculus	43-53
18394568-7	2008	On the other hand, for dominantly inherited Huntington"s disease (HD), in which an expanded polyglutamine tract imparts to the protein huntingtin a toxic gain of function, repressing expression of the mutant allele in the striatum using RNA interference technology mitigates pathology and delays the phenotype in a mouse model.	polyglutamine	92-105	huntingtin	Mus musculus	135-145
18029446-1	2008	Huntington"s disease (HD) is a neurodegenerative disorder due to an abnormal polyglutamine expansion in the N-terminal region of huntingtin protein (Exp-Htt).	polyglutamine	77-90	huntingtin	Mus musculus	129-139
18199701-4	2008	However, using a cellular model of HD, we found that rapamycin significantly decreased aggregation-prone polyglutamine (polyQ) and expanded huntingtin and its inclusion bodies (IB) in both autophagy-proficient and autophagy-deficient cells (by genetic knockout of the atg5 gene in mouse embryonic fibroblasts).	Sirolimus	53-62	huntingtin	Mus musculus	140-150
17975550-8	2008	We suggest, that the C-terminal domain of exon 1 Huntingtin, namely the proline rich domain, is responsible for mediating a neuroprotective effect against excitotoxicity.	Proline	72-79	huntingtin	Mus musculus	49-59
18079112-0	2008	Histone deacetylase inhibition modulates kynurenine pathway activation in yeast, microglia, and mice expressing a mutant huntingtin fragment.	Kynurenine	41-51	huntingtin	Mus musculus	121-131
18079112-1	2008	The kynurenine pathway of tryptophan degradation is hypothesized to play an important role in Huntington disease, a neurodegenerative disorder caused by a polyglutamine expansion in the protein huntingtin.	Kynurenine	4-14	huntingtin	Mus musculus	194-204
18079112-1	2008	The kynurenine pathway of tryptophan degradation is hypothesized to play an important role in Huntington disease, a neurodegenerative disorder caused by a polyglutamine expansion in the protein huntingtin.	Tryptophan	26-36	huntingtin	Mus musculus	194-204
18079112-1	2008	The kynurenine pathway of tryptophan degradation is hypothesized to play an important role in Huntington disease, a neurodegenerative disorder caused by a polyglutamine expansion in the protein huntingtin.	polyglutamine	155-168	huntingtin	Mus musculus	194-204
18079112-3	2008	Here we report that expression of a mutant huntingtin fragment was sufficient to induce transcription of the kynurenine pathway in yeast and that this induction was abrogated by impairing the activity of the histone deacetylase Rpd3.	Kynurenine	109-119	huntingtin	Mus musculus	43-53
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	131-141	huntingtin	Mus musculus	49-59
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	131-141	huntingtin	Mus musculus	225-235
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	186-196	huntingtin	Mus musculus	49-59
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	186-196	huntingtin	Mus musculus	225-235
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	48-58	huntingtin	Mus musculus	275-285
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	223-233	huntingtin	Mus musculus	275-285
18288205-1	2008	In Huntington"s disease (HD), mutant Huntingtin, which contains expanded polyglutamine stretches, forms nuclear aggregates in neurons.	polyglutamine	73-86	huntingtin	Mus musculus	37-47
18337408-1	2008	Huntington"s disease (HD) is caused by polyglutamine (polyQ) expansion in huntingtin (htt), a large (350 kDa) protein that localizes predominantly to the cytoplasm.	polyglutamine	39-52	huntingtin	Mus musculus	74-84
18337408-1	2008	Huntington"s disease (HD) is caused by polyglutamine (polyQ) expansion in huntingtin (htt), a large (350 kDa) protein that localizes predominantly to the cytoplasm.	polyglutamine	39-52	huntingtin	Mus musculus	86-89
18337408-1	2008	Huntington"s disease (HD) is caused by polyglutamine (polyQ) expansion in huntingtin (htt), a large (350 kDa) protein that localizes predominantly to the cytoplasm.	polyglutamine	54-59	huntingtin	Mus musculus	74-84
18337408-1	2008	Huntington"s disease (HD) is caused by polyglutamine (polyQ) expansion in huntingtin (htt), a large (350 kDa) protein that localizes predominantly to the cytoplasm.	polyglutamine	54-59	huntingtin	Mus musculus	86-89
18337408-2	2008	Proteolytic cleavage of mutant htt yields polyQ-containing N-terminal fragments that are prone to misfolding and aggregation.	polyglutamine	42-47	huntingtin	Mus musculus	31-34
18337408-8	2008	Reduced ATP level was also found in the synaptosomal fraction isolated from Hdh(CAG)150 knock-in mouse brain.	Adenosine Triphosphate	8-11	huntingtin	Mus musculus	76-79
17925440-1	2007	Huntington"s disease (HD) is a progressive neurodegenerative disease caused by a glutamine expansion within huntingtin protein.	Glutamine	81-90	huntingtin	Mus musculus	108-118
18006350-1	2008	Recent studies indicate altered cholesterol homeostasis in Huntington"s disease (HD) after it was found that cultured human and mice cells expressing mutant huntingtin show reduced mRNA of cholesterol biosynthetic enzymes.	Cholesterol	32-43	huntingtin	Mus musculus	157-167
18006350-1	2008	Recent studies indicate altered cholesterol homeostasis in Huntington"s disease (HD) after it was found that cultured human and mice cells expressing mutant huntingtin show reduced mRNA of cholesterol biosynthetic enzymes.	Cholesterol	189-200	huntingtin	Mus musculus	157-167
17971125-1	2008	Huntington"s disease is caused by a polyglutamine expansion in the huntingtin (htt) protein, and previous data indicate that over-activation of NMDA receptors (NMDARs) may be involved in the selective degeneration of cells expressing NR1/NR2B NMDARs.	polyglutamine	36-49	huntingtin	Mus musculus	67-77
17971125-1	2008	Huntington"s disease is caused by a polyglutamine expansion in the huntingtin (htt) protein, and previous data indicate that over-activation of NMDA receptors (NMDARs) may be involved in the selective degeneration of cells expressing NR1/NR2B NMDARs.	polyglutamine	36-49	huntingtin	Mus musculus	79-82
18078716-0	2008	14-3-3zeta is indispensable for aggregate formation of polyglutamine-expanded huntingtin protein.	polyglutamine	55-68	huntingtin	Mus musculus	78-88
18078716-1	2008	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by polyglutamine (polyQ) expansions in the huntingtin (Htt) protein.	polyglutamine	100-113	huntingtin	Mus musculus	140-150
18078716-1	2008	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by polyglutamine (polyQ) expansions in the huntingtin (Htt) protein.	polyglutamine	100-113	huntingtin	Mus musculus	152-155
18078716-1	2008	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by polyglutamine (polyQ) expansions in the huntingtin (Htt) protein.	polyglutamine	115-120	huntingtin	Mus musculus	140-150
18078716-1	2008	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by polyglutamine (polyQ) expansions in the huntingtin (Htt) protein.	polyglutamine	115-120	huntingtin	Mus musculus	152-155
17704510-1	2007	Huntington"s disease is caused by an expanded polyglutamine tract in huntingtin protein, leading to accumulation of huntingtin in the nuclei of striatal neurons.	polyglutamine	46-59	huntingtin	Mus musculus	69-79
17704510-1	2007	Huntington"s disease is caused by an expanded polyglutamine tract in huntingtin protein, leading to accumulation of huntingtin in the nuclei of striatal neurons.	polyglutamine	46-59	huntingtin	Mus musculus	116-126
17704510-4	2007	A single point mutation in huntingtin 1-18 predicted to disrupt this helical structure displayed striking phenotypes of complete inhibition of polyglutamine-mediated aggregation, increased huntingtin nuclear accumulation and greatly increased mutant huntingtin toxicity in a striatal-derived mouse cell line.	polyglutamine	143-156	huntingtin	Mus musculus	27-37
18067195-0	2008	Inducing huntingtin inclusion formation in primary neuronal cell culture and in vivo by high-capacity adenoviral vectors expressing truncated and full-length huntingtin with polyglutamine expansion.	polyglutamine	174-187	huntingtin	Mus musculus	9-19
18067195-0	2008	Inducing huntingtin inclusion formation in primary neuronal cell culture and in vivo by high-capacity adenoviral vectors expressing truncated and full-length huntingtin with polyglutamine expansion.	polyglutamine	174-187	huntingtin	Mus musculus	158-168
18067195-1	2008	BACKGROUND: Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (htt) gene.	trinucleotide	132-145	huntingtin	Mus musculus	170-180
18067195-1	2008	BACKGROUND: Huntington"s disease (HD) is an inherited autosomal dominant neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (htt) gene.	trinucleotide	132-145	huntingtin	Mus musculus	182-185
17971125-6	2008	Our findings are consistent with up-regulation of components of the stress response pathway in the presence of polyglutamine-expanded htt and NR1/NR2B which may reflect an attempt at the cellular level to ameliorate the detrimental effects of mutant htt expression.	polyglutamine	111-124	huntingtin	Mus musculus	134-137
17971125-6	2008	Our findings are consistent with up-regulation of components of the stress response pathway in the presence of polyglutamine-expanded htt and NR1/NR2B which may reflect an attempt at the cellular level to ameliorate the detrimental effects of mutant htt expression.	polyglutamine	111-124	huntingtin	Mus musculus	250-253
17986219-1	2008	A CAG-repeat gene expansion translated into a pathogenic polyglutamine stretch at the N-terminus of huntingtin triggers Huntington"s Disease.	polyglutamine	57-70	huntingtin	Mus musculus	100-110
17986219-5	2008	For this, we analyzed samples from in vitro and in vivo Huntington"s Disease models by agarose gel electrophoresis and showed that in the brain of transgenic mice huntingtin-aggregates became larger as a function of disease progression.	Sepharose	87-94	huntingtin	Mus musculus	163-173
18078716-2	2008	A hallmark of HD is the presence of aggregates-predominantly composed of NH(2)-terminal fragments of polyQ-expanded Htt-in the nucleus and cytoplasm of affected neurons.	polyglutamine	101-106	huntingtin	Mus musculus	116-119
18078716-5	2008	In this study, analysis of the aggregation-prone protein Htt encoded by HD gene exon 1 containing polyglutamine expansions (Htt86Q) revealed that 17 residues in the NH(2)-terminal of this protein are indispensable for its aggregate formation.	polyglutamine	98-111	huntingtin	Mus musculus	57-60
17947297-0	2008	HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity.	Glutamine	114-124	huntingtin	Mus musculus	8-18
17947297-0	2008	HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity.	Glutamine	114-124	huntingtin	Mus musculus	95-105
17947297-1	2008	Expansion of polymorphic glutamine (Q) numbers present at the protein Huntingtin (Htt) beyond 36Q results in its misfolding and aggregation, and the aggregates recruit several other proteins.	Glutamine	25-34	huntingtin	Mus musculus	70-80
17947297-1	2008	Expansion of polymorphic glutamine (Q) numbers present at the protein Huntingtin (Htt) beyond 36Q results in its misfolding and aggregation, and the aggregates recruit several other proteins.	Glutamine	25-34	huntingtin	Mus musculus	82-85
17947297-4	2008	Fluorescence recovery after photobleaching studies reveal that over-expression of HYPK results in the appearance of Htt poly Q aggregates, which upon bleaching recovers approximately 80% of initial fluorescence intensity within 6 min.	polyglutamine	120-126	huntingtin	Mus musculus	116-119
18537673-1	2008	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by the expansion of a polymorphic CAG trinucleotide repeat encoding a poly-glutamine tract within the Huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	120-123	huntingtin	Mus musculus	188-198
18537673-1	2008	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by the expansion of a polymorphic CAG trinucleotide repeat encoding a poly-glutamine tract within the Huntingtin protein.	trinucleotide	124-137	huntingtin	Mus musculus	188-198
18537673-1	2008	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by the expansion of a polymorphic CAG trinucleotide repeat encoding a poly-glutamine tract within the Huntingtin protein.	Glutamine	161-170	huntingtin	Mus musculus	188-198
17925440-4	2007	Although aggregated polyglutamines may not be inherently toxic, they constitute a biomarker for mutant huntingtin useful for developing therapeutics.	polyglutamine	20-34	huntingtin	Mus musculus	103-113
17500595-1	2007	Huntington"s disease (HD) is a fatal neurodegenerative condition caused by expansion of the polyglutamine tract in the huntingtin (Htt) protein.	polyglutamine	92-105	huntingtin	Mus musculus	131-134
17708681-0	2007	Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism.	polyglutamine	60-73	huntingtin	Mus musculus	49-59
17708681-1	2007	The Huntington"s disease (HD) CAG repeat, encoding a polymorphic glutamine tract in huntingtin, is inversely correlated with cellular energy level, with alleles over approximately 37 repeats leading to the loss of striatal neurons.	Glutamine	65-74	huntingtin	Mus musculus	84-94
17708681-7	2007	Thus, rather than a direct impact on the mitochondrion, the polyglutamine tract may modulate some aspect of huntingtin"s activity in extra-mitochondrial energy metabolism.	polyglutamine	60-73	huntingtin	Mus musculus	108-118
17652581-1	2007	Huntington"s disease (HD) is a neurodegenerative disorder caused by polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	68-81	huntingtin	Mus musculus	103-113
17652581-1	2007	Huntington"s disease (HD) is a neurodegenerative disorder caused by polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	68-81	huntingtin	Mus musculus	123-126
17652581-1	2007	Huntington"s disease (HD) is a neurodegenerative disorder caused by polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	83-88	huntingtin	Mus musculus	103-113
17652581-1	2007	Huntington"s disease (HD) is a neurodegenerative disorder caused by polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	83-88	huntingtin	Mus musculus	123-126
17613541-0	2007	Cholesterol biosynthesis pathway is disturbed in YAC128 mice and is modulated by huntingtin mutation.	Cholesterol	0-11	huntingtin	Mus musculus	81-91
17613541-1	2007	Our recent analyses of the cholesterol biosynthetic pathway in Huntington"s disease (HD) cells, in the R6/2 huntingtin-fragment mouse model of HD as well as in human tissues have provided the first evidence of altered activity of this pathway in genetically identifiable HD samples.	Cholesterol	27-38	huntingtin	Mus musculus	108-118
17250964-0	2007	Mechanical, thermal and formalin-induced nociception is differentially altered in 5-HT1A-/-, 5-HT1B-/-, 5-HT2A-/-, 5-HT3A-/- and 5-HTT-/- knock-out male mice.	Formaldehyde	24-32	huntingtin	Mus musculus	131-134
17373643-8	2007	Furthermore, the 2B4 epitope resides within the proline-rich region of Huntingtin, which is critical for polyQ aggregation and toxicity.	Proline	48-55	huntingtin	Mus musculus	71-81
17360721-3	2007	In cell culture systems, heat-shock protein 27 (Hsp27), a small molecular chaperone, suppresses mutant huntingtin-induced reactive oxygen species formation and cell death.	Oxygen	131-137	huntingtin	Mus musculus	103-113
17272267-1	2007	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that results from a CAG (glutamine) trinucleotide expansion in exon 1 of huntingtin (Htt).	Glutamine	100-109	huntingtin	Mus musculus	148-158
17272267-1	2007	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that results from a CAG (glutamine) trinucleotide expansion in exon 1 of huntingtin (Htt).	Glutamine	100-109	huntingtin	Mus musculus	160-163
17272267-1	2007	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that results from a CAG (glutamine) trinucleotide expansion in exon 1 of huntingtin (Htt).	trinucleotide	111-124	huntingtin	Mus musculus	148-158
17272267-1	2007	Huntington disease (HD) is an autosomal dominant neurodegenerative disease that results from a CAG (glutamine) trinucleotide expansion in exon 1 of huntingtin (Htt).	trinucleotide	111-124	huntingtin	Mus musculus	160-163
17352933-2	2007	The disease is inherited in an autosomal dominant fashion and is caused by a trinucleotide (CAG) repeat expansion in the gene encoding the protein huntingtin.	trinucleotide	77-90	huntingtin	Mus musculus	147-157
17352933-2	2007	The disease is inherited in an autosomal dominant fashion and is caused by a trinucleotide (CAG) repeat expansion in the gene encoding the protein huntingtin.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	92-95	huntingtin	Mus musculus	147-157
17352936-8	2007	Selective phosphorylation of mutant htt on serine 421 may also contribute, as phosphorylation of mutant htt reduces its toxicity and is decreased in the striatum compared to other regions of the brain.	Serine	43-49	huntingtin	Mus musculus	36-39
17352936-8	2007	Selective phosphorylation of mutant htt on serine 421 may also contribute, as phosphorylation of mutant htt reduces its toxicity and is decreased in the striatum compared to other regions of the brain.	Serine	43-49	huntingtin	Mus musculus	104-107
17409241-2	2007	This hereditary disorder is caused by an expansion >35 in the polyglutamine (polyQ) region of the protein huntingtin (htt).	polyglutamine	62-75	huntingtin	Mus musculus	106-116
17409241-2	2007	This hereditary disorder is caused by an expansion >35 in the polyglutamine (polyQ) region of the protein huntingtin (htt).	polyglutamine	62-75	huntingtin	Mus musculus	118-121
17409241-2	2007	This hereditary disorder is caused by an expansion >35 in the polyglutamine (polyQ) region of the protein huntingtin (htt).	polyglutamine	77-82	huntingtin	Mus musculus	106-116
17409241-2	2007	This hereditary disorder is caused by an expansion >35 in the polyglutamine (polyQ) region of the protein huntingtin (htt).	polyglutamine	77-82	huntingtin	Mus musculus	118-121
17472569-1	2007	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (htt) gene.	trinucleotide	110-123	huntingtin	Mus musculus	148-158
17472569-1	2007	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (htt) gene.	trinucleotide	110-123	huntingtin	Mus musculus	160-163
17394466-7	2007	However, when challenged with energy-demanding stimuli (NMDA-receptor activation in pyruvate-based media to accentuate the mitochondria role in Ca2+-handling), Hdh150 neurons are more vulnerable to Ca2+-deregulation than neurons from their wild-type littermates.	Pyruvic Acid	84-92	huntingtin	Mus musculus	160-163
17335925-1	2007	Huntington"s disease (HD) is caused by a mutation causing expanded polyglutamine tracts in the N-terminal fragment of huntingtin.	polyglutamine	67-80	huntingtin	Mus musculus	118-128
17335925-4	2007	In heterozygous knock-in mice with 77 CAG repeats, aggregates of N-terminal fragments of huntingtin were specifically formed in nuclei and neuropils in the striatal projection neurons, and in neuropils in their projection regions.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	38-41	huntingtin	Mus musculus	89-99
17396163-1	2007	Huntington"s disease (HD) is caused by a dominant polyglutamine expansion within the N-terminus of huntingtin protein and results in oxidative stress, energetic insufficiency and striatal degeneration.	polyglutamine	50-63	huntingtin	Mus musculus	99-109
17396163-7	2007	The first 171 amino acids of wild-type huntingtin, and its glutamine expanded mutant form, interacted with copper, but not iron.	Glutamine	59-68	huntingtin	Mus musculus	39-49
17396163-7	2007	The first 171 amino acids of wild-type huntingtin, and its glutamine expanded mutant form, interacted with copper, but not iron.	Copper	107-113	huntingtin	Mus musculus	39-49
17396163-9	2007	Further, copper promoted and metal chelation inhibited aggregation of cell-free huntingtin.	Copper	9-15	huntingtin	Mus musculus	80-90
17396163-9	2007	Further, copper promoted and metal chelation inhibited aggregation of cell-free huntingtin.	Metals	29-34	huntingtin	Mus musculus	80-90
17470275-1	2007	A critical issue in understanding Huntington"s disease (HD) pathogenesis is how the ubiquitously expressed mutant huntingtin (mhtt) with an expanded polyglutamine repeat can cause selective toxicity of striatal and cortical neurons.	polyglutamine	149-162	huntingtin	Mus musculus	114-124
17213233-1	2007	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	Mus musculus	124-134
17213233-1	2007	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	Mus musculus	136-139
17329427-7	2007	Interestingly, phosphorylation of Akt and its substrate huntingtin (htt) decreases during NMDA-induced excitotoxicity by 48 and 31%, respectively.	N-Methylaspartate	90-94	huntingtin	Mus musculus	56-66
17329427-7	2007	Interestingly, phosphorylation of Akt and its substrate huntingtin (htt) decreases during NMDA-induced excitotoxicity by 48 and 31%, respectively.	N-Methylaspartate	90-94	huntingtin	Mus musculus	68-71
17334227-1	2007	Huntington"s disease is caused by CAG trinucleotide expansions in the gene encoding huntingtin.	trinucleotide	38-51	huntingtin	Mus musculus	84-94
17334227-2	2007	N- terminal fragments of huntingtin with polyglutamine produce aggregates in the endosome-lysosomal system, where proteolytic fragments of huntingtin is generated.	polyglutamine	41-54	huntingtin	Mus musculus	25-35
17334227-2	2007	N- terminal fragments of huntingtin with polyglutamine produce aggregates in the endosome-lysosomal system, where proteolytic fragments of huntingtin is generated.	polyglutamine	41-54	huntingtin	Mus musculus	139-149
17027958-1	2006	Hippi functions as an adapter protein that mediates pro-apoptotic signaling from poly-glutamine-expanded huntingtin, an established cause of Huntington disease, to the extrinsic cell death pathway.	poly	81-85	huntingtin	Mus musculus	105-115
17184144-6	2007	Recent experimental evidence through transgenic mice models reveal an interesting interaction between expanded CAG triplets, mutant htt, and the increase in toxic metabolites from the kynurenine pathway.	Kynurenine	184-194	huntingtin	Mus musculus	132-135
18193642-3	2007	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	16-29	huntingtin	Mus musculus	96-106
18193642-3	2007	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	16-29	huntingtin	Mus musculus	108-111
18193642-3	2007	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	31-36	huntingtin	Mus musculus	96-106
18193642-3	2007	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	31-36	huntingtin	Mus musculus	108-111
18193642-4	2007	The connection between polyQ expansion in Htt(exp) and MSN neurodegeneration remains elusive.	polyglutamine	23-28	huntingtin	Mus musculus	42-45
17027958-1	2006	Hippi functions as an adapter protein that mediates pro-apoptotic signaling from poly-glutamine-expanded huntingtin, an established cause of Huntington disease, to the extrinsic cell death pathway.	Glutamine	86-95	huntingtin	Mus musculus	105-115
17215878-2	2006	This CAG expansion results in polyglutamine expansion in the 350 kDa huntingtin protein.	polyglutamine	30-43	huntingtin	Mus musculus	69-79
17147801-1	2006	BACKGROUND: Huntington disease (HD) is an adult onset neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin (htt) protein.	polyglutamine	93-106	huntingtin	Mus musculus	124-134
17147801-1	2006	BACKGROUND: Huntington disease (HD) is an adult onset neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin (htt) protein.	polyglutamine	93-106	huntingtin	Mus musculus	136-139
16884969-6	2006	Imipramine and fluoxetine, antagonists with specificity for 5-HTT, show the highest potency to antagonize [125I]RTI-55 binding in the MLO-Y4 cells.	Imipramine	0-10	huntingtin	Mus musculus	62-65
16884969-6	2006	Imipramine and fluoxetine, antagonists with specificity for 5-HTT, show the highest potency to antagonize [125I]RTI-55 binding in the MLO-Y4 cells.	Fluoxetine	15-25	huntingtin	Mus musculus	62-65
17065224-0	2006	Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin.	Dopamine	0-8	huntingtin	Mus musculus	85-95
17065224-0	2006	Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin.	polyglutamine	62-75	huntingtin	Mus musculus	85-95
17065224-1	2006	An expansion in the CAG repeat of the IT15 (huntingtin) gene underlies the development of Huntington"s disease (HD), but the basis for the specific vulnerability of dopamine-receptive striatal neurons remains unclear.	Dopamine	165-173	huntingtin	Mus musculus	38-42
17065224-1	2006	An expansion in the CAG repeat of the IT15 (huntingtin) gene underlies the development of Huntington"s disease (HD), but the basis for the specific vulnerability of dopamine-receptive striatal neurons remains unclear.	Dopamine	165-173	huntingtin	Mus musculus	44-54
17065224-8	2006	These findings indicate that dopamine contributes to the deleterious effects of mutated huntingtin on striatal function, and this is accompanied by enhanced formation of huntingtin aggregates.	Dopamine	29-37	huntingtin	Mus musculus	88-98
17065224-8	2006	These findings indicate that dopamine contributes to the deleterious effects of mutated huntingtin on striatal function, and this is accompanied by enhanced formation of huntingtin aggregates.	Dopamine	29-37	huntingtin	Mus musculus	170-180
16973623-0	2006	Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: functional consequences.	Calcium	51-58	huntingtin	Mus musculus	7-17
17055784-1	2006	Huntington"s disease (HD) is a fatal, dominantly inherited disorder caused by polyglutamine repeat expansion in the huntingtin (htt) gene.	polyglutamine	78-91	huntingtin	Mus musculus	116-126
17055784-1	2006	Huntington"s disease (HD) is a fatal, dominantly inherited disorder caused by polyglutamine repeat expansion in the huntingtin (htt) gene.	polyglutamine	78-91	huntingtin	Mus musculus	128-131
16777606-5	2006	Furthermore, caspase-6-resistant mutant htt mice are protected against neurotoxicity induced by multiple stressors including NMDA, quinolinic acid (QA), and staurosporine.	N-Methylaspartate	125-129	huntingtin	Mus musculus	40-43
16983659-2	2006	This mutation results in the presence of an abnormally long polyglutamine tract in the encoded protein, huntingtin (htt).	polyglutamine	60-73	huntingtin	Mus musculus	104-114
16983659-2	2006	This mutation results in the presence of an abnormally long polyglutamine tract in the encoded protein, huntingtin (htt).	polyglutamine	60-73	huntingtin	Mus musculus	116-119
17018277-1	2006	Huntington"s disease (HD) is an inherited neurodegenerative disease caused by a glutamine repeat expansion in huntingtin protein.	Glutamine	80-89	huntingtin	Mus musculus	110-120
16751280-1	2006	Huntington"s disease (HD) is a fatal, genetic, neurological disorder resulting from a trinucleotide repeat expansion in the gene that encodes for the protein huntingtin.	trinucleotide	86-99	huntingtin	Mus musculus	158-168
16766198-1	2006	Huntington"s disease is a neurodegenerative disease caused by an expanded polyglutamine stretch within the huntingtin protein.	polyglutamine	74-87	huntingtin	Mus musculus	107-117
16766198-5	2006	Transfection with a htt exon1 construct containing uninterrupted polyglutamine or a polyglutamine region engineered to form a compact beta structure resulted in cell toxicity.	polyglutamine	84-97	huntingtin	Mus musculus	20-23
16777606-5	2006	Furthermore, caspase-6-resistant mutant htt mice are protected against neurotoxicity induced by multiple stressors including NMDA, quinolinic acid (QA), and staurosporine.	Quinolinic Acid	131-146	huntingtin	Mus musculus	40-43
16777606-5	2006	Furthermore, caspase-6-resistant mutant htt mice are protected against neurotoxicity induced by multiple stressors including NMDA, quinolinic acid (QA), and staurosporine.	Quinolinic Acid	148-150	huntingtin	Mus musculus	40-43
16777606-5	2006	Furthermore, caspase-6-resistant mutant htt mice are protected against neurotoxicity induced by multiple stressors including NMDA, quinolinic acid (QA), and staurosporine.	Staurosporine	157-170	huntingtin	Mus musculus	40-43
16647250-6	2006	CoQ10 resulted in a marked improvement in motor performance and grip strength, with a reduction in weight loss, brain atrophy, and huntingtin inclusions in treated R6/2 mice.	coenzyme Q10	0-5	huntingtin	Mus musculus	131-141
16699508-2	2006	Here we show that huntingtin (htt) is normally palmitoylated at cysteine 214, which is essential for its trafficking and function.	Cysteine	64-72	huntingtin	Mus musculus	18-28
16699508-2	2006	Here we show that huntingtin (htt) is normally palmitoylated at cysteine 214, which is essential for its trafficking and function.	Cysteine	64-72	huntingtin	Mus musculus	30-33
16699508-4	2006	Expansion of the polyglutamine tract of htt, which causes Huntington disease, results in reduced interaction between mutant htt and HIP14 and consequently in a marked reduction in palmitoylation.	polyglutamine	17-30	huntingtin	Mus musculus	40-43
16699508-4	2006	Expansion of the polyglutamine tract of htt, which causes Huntington disease, results in reduced interaction between mutant htt and HIP14 and consequently in a marked reduction in palmitoylation.	polyglutamine	17-30	huntingtin	Mus musculus	124-127
16699508-7	2006	These results suggest that the expansion of the polyglutamine tract in htt results in decreased palmitoylation, which contributes to the formation of inclusion bodies and enhanced neuronal toxicity.	polyglutamine	48-61	huntingtin	Mus musculus	71-74
16600988-3	2006	HD is inherited in an autosomal dominant fashion and caused by a trinucleotide repeat expansion (CAG) in the gene encoding the protein huntingtin.	trinucleotide	65-78	huntingtin	Mus musculus	135-145
16364609-8	2006	In addition, combined minocycline and CoQ10 treatment attenuated gross brain atrophy, striatal neuron atrophy, and huntingtin aggregation in the R6/2 mice relative to individual treatment.	Minocycline	22-33	huntingtin	Mus musculus	115-125
16364609-8	2006	In addition, combined minocycline and CoQ10 treatment attenuated gross brain atrophy, striatal neuron atrophy, and huntingtin aggregation in the R6/2 mice relative to individual treatment.	coenzyme Q10	38-43	huntingtin	Mus musculus	115-125
16571604-1	2006	Huntington disease is an adult-onset neurodegenerative disorder that is caused by the expansion of a polyglutamine tract within the Huntingtin (htt) protein.	polyglutamine	101-114	huntingtin	Mus musculus	132-142
16571604-1	2006	Huntington disease is an adult-onset neurodegenerative disorder that is caused by the expansion of a polyglutamine tract within the Huntingtin (htt) protein.	polyglutamine	101-114	huntingtin	Mus musculus	144-147
16423528-5	2006	Mutant htt fully degraded in cathepsin-L-treated lysates but formed stable N-mhtt fragments upon exposure to cathepsin D.	n-mhtt	75-81	huntingtin	Mus musculus	7-10
16443291-2	2006	Transgenic mice expressing the N-terminal of huntingtin, containing 82 glutamines, exhibit a progressive disorder, which resembles to the human disease.	Glutamine	71-81	huntingtin	Mus musculus	45-55
16516148-0	2006	Curcumin enhances the polyglutamine-expanded truncated N-terminal huntingtin-induced cell death by promoting proteasomal malfunction.	Curcumin	0-8	huntingtin	Mus musculus	66-76
16516148-0	2006	Curcumin enhances the polyglutamine-expanded truncated N-terminal huntingtin-induced cell death by promoting proteasomal malfunction.	polyglutamine	22-35	huntingtin	Mus musculus	66-76
16516148-4	2006	Here, we found that the treatment of curcumin increases the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-dependent cell death.	Curcumin	37-45	huntingtin	Mus musculus	104-114
16516148-4	2006	Here, we found that the treatment of curcumin increases the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-dependent cell death.	Curcumin	37-45	huntingtin	Mus musculus	123-133
16516148-4	2006	Here, we found that the treatment of curcumin increases the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-dependent cell death.	Curcumin	37-45	huntingtin	Mus musculus	123-133
16516148-4	2006	Here, we found that the treatment of curcumin increases the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-dependent cell death.	polyglutamine	60-73	huntingtin	Mus musculus	104-114
16516148-4	2006	Here, we found that the treatment of curcumin increases the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-dependent cell death.	polyglutamine	60-73	huntingtin	Mus musculus	123-133
16516148-4	2006	Here, we found that the treatment of curcumin increases the polyglutamine-expanded truncated N-terminal huntingtin (mutant huntingtin) aggregation and mutant huntingtin-dependent cell death.	polyglutamine	60-73	huntingtin	Mus musculus	123-133
16516148-5	2006	Curcumin also causes rapid proteasomal malfunction in the mutant huntingtin expressing cells in comparison with normal glutamine repeat expressing cells.	Curcumin	0-8	huntingtin	Mus musculus	65-75
16516148-6	2006	Finally, we show that N-acetyl cysteine (NAC), a potent antioxidant, reverted the curcumin-induced mutant huntingtin aggregation and proteasomal malfunction in the mutant huntingtin expressing cells.	Acetylcysteine	22-39	huntingtin	Mus musculus	106-116
16516148-6	2006	Finally, we show that N-acetyl cysteine (NAC), a potent antioxidant, reverted the curcumin-induced mutant huntingtin aggregation and proteasomal malfunction in the mutant huntingtin expressing cells.	Acetylcysteine	22-39	huntingtin	Mus musculus	171-181
16516148-6	2006	Finally, we show that N-acetyl cysteine (NAC), a potent antioxidant, reverted the curcumin-induced mutant huntingtin aggregation and proteasomal malfunction in the mutant huntingtin expressing cells.	Acetylcysteine	41-44	huntingtin	Mus musculus	106-116
16516148-6	2006	Finally, we show that N-acetyl cysteine (NAC), a potent antioxidant, reverted the curcumin-induced mutant huntingtin aggregation and proteasomal malfunction in the mutant huntingtin expressing cells.	Acetylcysteine	41-44	huntingtin	Mus musculus	171-181
16516148-6	2006	Finally, we show that N-acetyl cysteine (NAC), a potent antioxidant, reverted the curcumin-induced mutant huntingtin aggregation and proteasomal malfunction in the mutant huntingtin expressing cells.	Curcumin	82-90	huntingtin	Mus musculus	106-116
16516148-6	2006	Finally, we show that N-acetyl cysteine (NAC), a potent antioxidant, reverted the curcumin-induced mutant huntingtin aggregation and proteasomal malfunction in the mutant huntingtin expressing cells.	Curcumin	82-90	huntingtin	Mus musculus	171-181
16516148-8	2006	Our result suggests that curcumin promotes mutant huntingtin-induced cell death by mimicking proteasomal dysfunction.	Curcumin	25-33	huntingtin	Mus musculus	50-60
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	Mus musculus	89-93
16403806-1	2006	Huntingtin (htt), the protein encoded by the Huntington"s disease (HD) gene, contains a polymorphic stretch of glutamines (polyQ) near its N-terminus.	Glutamine	111-121	huntingtin	Mus musculus	0-10
16403806-1	2006	Huntingtin (htt), the protein encoded by the Huntington"s disease (HD) gene, contains a polymorphic stretch of glutamines (polyQ) near its N-terminus.	Glutamine	111-121	huntingtin	Mus musculus	12-15
16403806-3	2006	However, the role of the normal polyQ stretch in the function of htt is still unknown.	polyglutamine	32-37	huntingtin	Mus musculus	65-68
16403806-9	2006	Taken altogether, these results suggest that htt"s polyQ stretch is required for modulating longevity in culture and support the hypothesis that the polyQ stretch may also modulate a htt function involved in regulating energy homeostasis.	polyglutamine	51-56	huntingtin	Mus musculus	45-48
16403806-9	2006	Taken altogether, these results suggest that htt"s polyQ stretch is required for modulating longevity in culture and support the hypothesis that the polyQ stretch may also modulate a htt function involved in regulating energy homeostasis.	polyglutamine	51-56	huntingtin	Mus musculus	183-186
16403806-9	2006	Taken altogether, these results suggest that htt"s polyQ stretch is required for modulating longevity in culture and support the hypothesis that the polyQ stretch may also modulate a htt function involved in regulating energy homeostasis.	polyglutamine	149-154	huntingtin	Mus musculus	45-48
16403806-9	2006	Taken altogether, these results suggest that htt"s polyQ stretch is required for modulating longevity in culture and support the hypothesis that the polyQ stretch may also modulate a htt function involved in regulating energy homeostasis.	polyglutamine	149-154	huntingtin	Mus musculus	183-186
16417581-4	2006	NMDA receptor activation induced by intrastriatal injection of quinolinic acid initiated a form of apoptotic neurodegeneration within the striatum of mice that was associated with caspase-3 cleavage of huntingtin in neurons and astrocytes, decreased levels of full-length huntingtin, and the generation of a specific N-terminal caspase cleavage product of huntingtin.	Quinolinic Acid	63-78	huntingtin	Mus musculus	202-212
16405500-10	2006	Moreover, interaction of both mutant and wild-type huntingtin exon 1 fragments with brain lipids caused bilayer perturbation, mediated through a proline-rich region adjacent to the polyglutamines.	Proline	145-152	huntingtin	Mus musculus	51-61
16405500-10	2006	Moreover, interaction of both mutant and wild-type huntingtin exon 1 fragments with brain lipids caused bilayer perturbation, mediated through a proline-rich region adjacent to the polyglutamines.	polyglutamine	181-195	huntingtin	Mus musculus	51-61
16150600-2	2006	In order to facilitate studies of pathogenesis and therapeutics, we have generated a new inducible mouse model of HD expressing full-length huntingtin (Htt) using a tetracycline-regulated promoter.	Tetracycline	165-177	huntingtin	Mus musculus	140-150
16150600-2	2006	In order to facilitate studies of pathogenesis and therapeutics, we have generated a new inducible mouse model of HD expressing full-length huntingtin (Htt) using a tetracycline-regulated promoter.	Tetracycline	165-177	huntingtin	Mus musculus	152-155
16150600-3	2006	In double transgenic mice Htt was expressed widely in the brain under the control of the tet-transactivator (tTA) driven by the prion promoter PrP (in the absence of doxycycline).	Doxycycline	166-177	huntingtin	Mus musculus	26-29
16165367-1	2006	Huntington disease (HD), caused by expansion >35 of a polyglutamine tract in huntingtin, results in degeneration of striatal medium spiny neurons (MSNs).	polyglutamine	54-67	huntingtin	Mus musculus	77-87
16365166-5	2005	As a result, mutant huntingtin (htt) reduces glutamate uptake in cultured astrocytes and HD mouse brains.	Glutamic Acid	45-54	huntingtin	Mus musculus	20-30
16365166-5	2005	As a result, mutant huntingtin (htt) reduces glutamate uptake in cultured astrocytes and HD mouse brains.	Glutamic Acid	45-54	huntingtin	Mus musculus	32-35
16365166-7	2005	Mutant htt in cultured astrocytes decreased their protection of neurons against glutamate excitotoxicity.	Glutamic Acid	80-89	huntingtin	Mus musculus	7-10
16365166-8	2005	These findings suggest that decreased glutamate uptake caused by glial mutant htt may critically contribute to neuronal excitotoxicity in HD.	Glutamic Acid	38-47	huntingtin	Mus musculus	78-81
16445565-3	2005	Much progress has been made in the past decade in understanding how a trinucleotide (CAG) repeat expansion, encoding an expanded polyglutamine tract in the huntingtin protein, induces dysfunction at molecular and cellular levels.	trinucleotide	70-83	huntingtin	Mus musculus	156-166
16445565-3	2005	Much progress has been made in the past decade in understanding how a trinucleotide (CAG) repeat expansion, encoding an expanded polyglutamine tract in the huntingtin protein, induces dysfunction at molecular and cellular levels.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	85-88	huntingtin	Mus musculus	156-166
16445565-3	2005	Much progress has been made in the past decade in understanding how a trinucleotide (CAG) repeat expansion, encoding an expanded polyglutamine tract in the huntingtin protein, induces dysfunction at molecular and cellular levels.	polyglutamine	129-142	huntingtin	Mus musculus	156-166
16452687-7	2006	Finally, we show that administration of FK506 to mice increases huntingtin S421 phosphorylation in brain.	Tacrolimus	40-45	huntingtin	Mus musculus	64-74
16417581-4	2006	NMDA receptor activation induced by intrastriatal injection of quinolinic acid initiated a form of apoptotic neurodegeneration within the striatum of mice that was associated with caspase-3 cleavage of huntingtin in neurons and astrocytes, decreased levels of full-length huntingtin, and the generation of a specific N-terminal caspase cleavage product of huntingtin.	Quinolinic Acid	63-78	huntingtin	Mus musculus	272-282
16417581-4	2006	NMDA receptor activation induced by intrastriatal injection of quinolinic acid initiated a form of apoptotic neurodegeneration within the striatum of mice that was associated with caspase-3 cleavage of huntingtin in neurons and astrocytes, decreased levels of full-length huntingtin, and the generation of a specific N-terminal caspase cleavage product of huntingtin.	Quinolinic Acid	63-78	huntingtin	Mus musculus	272-282
16095740-2	2005	It is caused by an expanded polyglutamine (poly Q) tract in the corresponding protein, huntingtin (htt), and therefore suppressing the huntingtin expression in brain neurons is expected to delay the onset and mitigate the severity of the disease.	polyglutamine	28-41	huntingtin	Mus musculus	87-97
16095740-2	2005	It is caused by an expanded polyglutamine (poly Q) tract in the corresponding protein, huntingtin (htt), and therefore suppressing the huntingtin expression in brain neurons is expected to delay the onset and mitigate the severity of the disease.	polyglutamine	28-41	huntingtin	Mus musculus	99-102
16095740-2	2005	It is caused by an expanded polyglutamine (poly Q) tract in the corresponding protein, huntingtin (htt), and therefore suppressing the huntingtin expression in brain neurons is expected to delay the onset and mitigate the severity of the disease.	polyglutamine	28-41	huntingtin	Mus musculus	135-145
16095740-2	2005	It is caused by an expanded polyglutamine (poly Q) tract in the corresponding protein, huntingtin (htt), and therefore suppressing the huntingtin expression in brain neurons is expected to delay the onset and mitigate the severity of the disease.	polyglutamine	43-49	huntingtin	Mus musculus	87-97
16095740-2	2005	It is caused by an expanded polyglutamine (poly Q) tract in the corresponding protein, huntingtin (htt), and therefore suppressing the huntingtin expression in brain neurons is expected to delay the onset and mitigate the severity of the disease.	polyglutamine	43-49	huntingtin	Mus musculus	99-102
16095740-2	2005	It is caused by an expanded polyglutamine (poly Q) tract in the corresponding protein, huntingtin (htt), and therefore suppressing the huntingtin expression in brain neurons is expected to delay the onset and mitigate the severity of the disease.	polyglutamine	43-49	huntingtin	Mus musculus	135-145
16251441-1	2005	The expansion of a polyglutamine tract in the ubiquitously expressed huntingtin protein causes Huntington"s disease (HD), a dominantly inherited neurodegenerative disease.	polyglutamine	19-32	huntingtin	Mus musculus	69-79
16251441-6	2005	Finally, the addition of exogenous cholesterol to striatal neurons expressing mutant huntingtin prevents their death in a dose-dependent manner.	Cholesterol	35-46	huntingtin	Mus musculus	85-95
16019264-1	2005	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by the presence of an abnormally expanded polyglutamine domain in the N-terminus of huntingtin.	polyglutamine	113-126	huntingtin	Mus musculus	155-165
16091361-1	2005	Huntington disease is caused by a polyglutamine expansion in the huntingtin protein (Htt) and is associated with excitotoxic death of striatal neurons.	polyglutamine	34-47	huntingtin	Mus musculus	65-75
16091361-1	2005	Huntington disease is caused by a polyglutamine expansion in the huntingtin protein (Htt) and is associated with excitotoxic death of striatal neurons.	polyglutamine	34-47	huntingtin	Mus musculus	85-88
16262645-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat encoding an extended polyglutamine tract in the huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	80-83	huntingtin	Mus musculus	153-163
16262645-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat encoding an extended polyglutamine tract in the huntingtin protein.	trinucleotide	84-97	huntingtin	Mus musculus	153-163
16019264-5	2005	The reduction in mHtt was concomitant with a reduction in the size and number of neuronal intranuclear inclusions and a small but significant normalization of the steady-state levels of preproenkephalin and dopamine- and cAMP-responsive phosphoprotein 32 kDa mRNA.	Dopamine	207-215	huntingtin	Mus musculus	17-21
16019264-5	2005	The reduction in mHtt was concomitant with a reduction in the size and number of neuronal intranuclear inclusions and a small but significant normalization of the steady-state levels of preproenkephalin and dopamine- and cAMP-responsive phosphoprotein 32 kDa mRNA.	Cyclic AMP	221-225	huntingtin	Mus musculus	17-21
15983033-0	2005	Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin.	Adenosine Triphosphate	30-33	huntingtin	Mus musculus	108-118
16137562-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an elongated glutamine repeat in huntingtin.	Glutamine	81-90	huntingtin	Mus musculus	101-111
15901794-9	2005	(+)-Norfenfluramine induced similar aortic contraction in wild-type and 5-HTT-targeted mutation mice, and these contractions were inhibited by fluoxetine (1 microM).	Norfenfluramine	0-19	huntingtin	Mus musculus	74-77
15901794-9	2005	(+)-Norfenfluramine induced similar aortic contraction in wild-type and 5-HTT-targeted mutation mice, and these contractions were inhibited by fluoxetine (1 microM).	Fluoxetine	143-153	huntingtin	Mus musculus	74-77
16109169-1	2005	BACKGROUND: Huntingtin, the HD gene encoded protein mutated by polyglutamine expansion in Huntington"s disease, is required in extraembryonic tissues for proper gastrulation, implicating its activities in nutrition or patterning of the developing embryo.	polyglutamine	63-76	huntingtin	Mus musculus	12-22
15983033-12	2005	These findings demonstrate that the presence of mutant huntingtin impairs mitochondrial ATP production through one or more mechanisms that do not directly affect the function of the respiration complexes.	Adenosine Triphosphate	88-91	huntingtin	Mus musculus	55-65
16087879-0	2005	Clioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington"s disease mouse model.	Clioquinol	0-10	huntingtin	Mus musculus	33-43
16087879-1	2005	In investigating the role of metal ions in the pathogenesis of Huntington"s disease, we examined the effects of clioquinol, a metal-binding compound currently in clinical trials for Alzheimer"s disease treatment, on mutant huntingtin-expressing cells.	Clioquinol	112-122	huntingtin	Mus musculus	223-233
16087879-4	2005	Clioquinol treatment of transgenic Huntington"s mice (R6/2) improved behavioral and pathologic phenotypes, including decreased huntingtin aggregate accumulation, decreased striatal atrophy, improved rotarod performance, reduction of weight loss, normalization of blood glucose and insulin levels, and extension of lifespan.	Clioquinol	0-10	huntingtin	Mus musculus	127-137
16103364-1	2005	Huntington"s disease (HD), an inherited neurodegenerative disorder, results from an abnormal polyglutamine extension in the N-terminal region of the huntingtin protein.	polyglutamine	93-106	huntingtin	Mus musculus	149-159
16103364-5	2005	Using primary cultures of striatal neurons transiently expressing GFP-tagged-exon 1 of mutated huntingtin, we show that low doses of DA (100 microM) act synergistically with mutated huntingtin to activate the proapoptotic transcription factor c-Jun.	Dopamine	133-135	huntingtin	Mus musculus	95-105
16103364-5	2005	Using primary cultures of striatal neurons transiently expressing GFP-tagged-exon 1 of mutated huntingtin, we show that low doses of DA (100 microM) act synergistically with mutated huntingtin to activate the proapoptotic transcription factor c-Jun.	Dopamine	133-135	huntingtin	Mus musculus	182-192
16103364-6	2005	Surprisingly, DA also increases aggregate formation of mutated huntingtin in all cellular compartments, including neurites, soma, and nuclei.	Dopamine	14-16	huntingtin	Mus musculus	63-73
16103364-10	2005	Blocking ROS production, JNK activation, or D2 receptor stimulation significantly reversed DA aggravation of mutated huntingtin-induced striatal death.	Reactive Oxygen Species	9-12	huntingtin	Mus musculus	117-127
16103364-10	2005	Blocking ROS production, JNK activation, or D2 receptor stimulation significantly reversed DA aggravation of mutated huntingtin-induced striatal death.	Dopamine	91-93	huntingtin	Mus musculus	117-127
16103364-11	2005	The combined treatment with the ROS scavenger and D2 antagonist totally reversed DA"s effects on mutated huntingtin-induced striatal death.	Reactive Oxygen Species	32-35	huntingtin	Mus musculus	105-115
16103364-11	2005	The combined treatment with the ROS scavenger and D2 antagonist totally reversed DA"s effects on mutated huntingtin-induced striatal death.	Dopamine	81-83	huntingtin	Mus musculus	105-115
16109169-11	2005	This knowledge may prove to be important for understanding the mechanism by which the dominant polyglutamine expansion in huntingtin determines the loss of neurons in Huntington"s disease.	polyglutamine	95-108	huntingtin	Mus musculus	122-132
15996546-2	2005	Mutant huntingtin (mHtt) with expanded polyglutamine (polyQ) binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity in neuronal cultures.	polyglutamine	54-59	huntingtin	Mus musculus	7-17
15996546-2	2005	Mutant huntingtin (mHtt) with expanded polyglutamine (polyQ) binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity in neuronal cultures.	polyglutamine	39-52	huntingtin	Mus musculus	7-17
15996546-2	2005	Mutant huntingtin (mHtt) with expanded polyglutamine (polyQ) binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity in neuronal cultures.	polyglutamine	39-52	huntingtin	Mus musculus	19-23
15843398-0	2005	Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo.	Serine	30-36	huntingtin	Mus musculus	0-10
15996546-2	2005	Mutant huntingtin (mHtt) with expanded polyglutamine (polyQ) binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity in neuronal cultures.	polyglutamine	54-59	huntingtin	Mus musculus	19-23
15843398-0	2005	Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo.	polyglutamine	89-102	huntingtin	Mus musculus	0-10
15843398-1	2005	Huntington disease (HD) results from polyglutamine expansion in the huntingtin protein (htt).	polyglutamine	37-50	huntingtin	Mus musculus	68-78
15843398-1	2005	Huntington disease (HD) results from polyglutamine expansion in the huntingtin protein (htt).	polyglutamine	37-50	huntingtin	Mus musculus	88-91
15843398-3	2005	Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinase Akt (PKB) and this has been previously shown to be protective against the toxicity of polyglutamine-expanded htt in cell culture.	Serine	32-38	huntingtin	Mus musculus	0-10
15843398-3	2005	Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinase Akt (PKB) and this has been previously shown to be protective against the toxicity of polyglutamine-expanded htt in cell culture.	Serine	32-38	huntingtin	Mus musculus	204-207
15934928-7	2005	In addition, reduced BDNF expression causes decreased dopamine receptor expression in mutant huntingtin mice.	Dopamine	54-62	huntingtin	Mus musculus	93-103
15935052-10	2005	Polyglutamine expansions in huntingtin produced an early increased resistance to calcium in striatal mitochondria suggesting mitochondria undergo compensatory changes in calcium sensitivity in response to the many cellular changes wrought by polyglutamine expansion.	polyglutamine	0-13	huntingtin	Mus musculus	28-38
15829505-7	2005	The testis of YAC128+/+ mice showed atrophy and degeneration, which was markedly worsened in the absence of wild-type htt (P = 0.001).	yac128	14-20	huntingtin	Mus musculus	118-121
15935052-10	2005	Polyglutamine expansions in huntingtin produced an early increased resistance to calcium in striatal mitochondria suggesting mitochondria undergo compensatory changes in calcium sensitivity in response to the many cellular changes wrought by polyglutamine expansion.	Calcium	81-88	huntingtin	Mus musculus	28-38
15935052-10	2005	Polyglutamine expansions in huntingtin produced an early increased resistance to calcium in striatal mitochondria suggesting mitochondria undergo compensatory changes in calcium sensitivity in response to the many cellular changes wrought by polyglutamine expansion.	Calcium	170-177	huntingtin	Mus musculus	28-38
15935052-10	2005	Polyglutamine expansions in huntingtin produced an early increased resistance to calcium in striatal mitochondria suggesting mitochondria undergo compensatory changes in calcium sensitivity in response to the many cellular changes wrought by polyglutamine expansion.	polyglutamine	242-255	huntingtin	Mus musculus	28-38
15911879-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	80-93	huntingtin	Mus musculus	115-125
15911879-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	80-93	huntingtin	Mus musculus	127-130
15911879-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	95-100	huntingtin	Mus musculus	115-125
15911879-1	2005	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	95-100	huntingtin	Mus musculus	127-130
15911879-2	2005	Mutant htt toxicity is exposed after htt cleavage by caspases and other proteases release NH(2)-terminal fragments containing the polyQ expansion.	polyglutamine	130-135	huntingtin	Mus musculus	7-10
15911879-2	2005	Mutant htt toxicity is exposed after htt cleavage by caspases and other proteases release NH(2)-terminal fragments containing the polyQ expansion.	polyglutamine	130-135	huntingtin	Mus musculus	37-40
15911879-7	2005	This result can be accounted for by the polyQ-expanded htt fragments reducing the interaction between cdk5 and its activator p35.	polyglutamine	40-45	huntingtin	Mus musculus	55-58
15829505-8	2005	YAC128+/+ mice also showed a male specific deficit in survival compared with WT mice which was exacerbated by the loss of wild-type htt (12-month-male survival, P < 0.001).	yac128	0-6	huntingtin	Mus musculus	132-135
15811941-2	2005	HD results from polyglutamine repeat expansion (CAG codon, Q) in exon 1 of HD, conferring a toxic gain of function on the protein huntingtin (htt).	polyglutamine	16-29	huntingtin	Mus musculus	130-140
15836623-1	2005	Huntington disease is caused by polyglutamine (polyQ) expansion in huntingtin.	polyglutamine	32-45	huntingtin	Mus musculus	67-77
15836623-1	2005	Huntington disease is caused by polyglutamine (polyQ) expansion in huntingtin.	polyglutamine	47-52	huntingtin	Mus musculus	67-77
15781153-0	2005	BAG-1 associates with the polyglutamine-expanded huntingtin aggregates.	polyglutamine	26-39	huntingtin	Mus musculus	49-59
15781153-1	2005	Huntington"s disease (HD) is characterised by the proteolytic production of N-terminal fragments of huntingtin containing polyglutamine repeats that forms intracellular ubiquitinated aggregates in the affected neurons.	polyglutamine	122-135	huntingtin	Mus musculus	100-110
15843398-3	2005	Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinase Akt (PKB) and this has been previously shown to be protective against the toxicity of polyglutamine-expanded htt in cell culture.	polyglutamine	181-194	huntingtin	Mus musculus	0-10
15843398-3	2005	Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinase Akt (PKB) and this has been previously shown to be protective against the toxicity of polyglutamine-expanded htt in cell culture.	polyglutamine	181-194	huntingtin	Mus musculus	204-207
15843398-6	2005	In cell cultures and in YAC transgenic mice, the endogenous phosphorylation of polyglutamine-expanded htt is significantly reduced relative to wild-type htt.	polyglutamine	79-92	huntingtin	Mus musculus	102-105
15843398-6	2005	In cell cultures and in YAC transgenic mice, the endogenous phosphorylation of polyglutamine-expanded htt is significantly reduced relative to wild-type htt.	polyglutamine	79-92	huntingtin	Mus musculus	153-156
15811941-2	2005	HD results from polyglutamine repeat expansion (CAG codon, Q) in exon 1 of HD, conferring a toxic gain of function on the protein huntingtin (htt).	polyglutamine	16-29	huntingtin	Mus musculus	142-145
15816854-1	2005	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a CAG trinucleotide expansion in exon 1 of the Huntingtin (Htt) gene.	trinucleotide	93-106	huntingtin	Mus musculus	134-144
15695335-1	2005	Huntington"s disease (HD) is caused by polyglutamine expansion (exp) in huntingtin.	polyglutamine	39-52	huntingtin	Mus musculus	72-82
15816854-1	2005	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a CAG trinucleotide expansion in exon 1 of the Huntingtin (Htt) gene.	trinucleotide	93-106	huntingtin	Mus musculus	146-149
15816854-7	2005	Since AMPK is a master switch for energy metabolism, modulation of energy dysfunction caused by the mutant Htt might contribute to the beneficial effects of CGS.	2-(4-(2-carboxyethyl)phenethylamino)-5'-N-ethylcarboxamidoadenosine	157-160	huntingtin	Mus musculus	107-110
15649316-8	2005	Of these, both juglone and celastrol were effective in reversing the abnormal cellular localization of full-length mutant huntingtin observed in mutant HdhQ111/Q111 striatal cells.	juglone	15-22	huntingtin	Mus musculus	122-132
15590702-8	2005	Apaf-1 also was found to colocalize with huntingtin-containing aggregates in a murine model and HD brain, suggesting a common role for Dark/Apaf-1 in polyglutamine pathogenesis in invertebrates, mice and man.	polyglutamine	150-163	huntingtin	Mus musculus	41-51
15654337-0	2005	Polyglutamine expansion of huntingtin impairs its nuclear export.	polyglutamine	0-13	huntingtin	Mus musculus	27-37
15654337-3	2005	N-terminal fragments of mutant htt, which contain a polyQ expansion (>37 glutamines), have no conserved nuclear localization sequences or nuclear export sequences but can accumulate in the nucleus and cause neurological problems in transgenic mice.	polyglutamine	52-57	huntingtin	Mus musculus	31-34
15654337-3	2005	N-terminal fragments of mutant htt, which contain a polyQ expansion (>37 glutamines), have no conserved nuclear localization sequences or nuclear export sequences but can accumulate in the nucleus and cause neurological problems in transgenic mice.	Glutamine	73-83	huntingtin	Mus musculus	31-34
15654337-6	2005	PolyQ expansion and aggregation decrease this interaction and increase the nuclear accumulation of htt.	polyglutamine	0-5	huntingtin	Mus musculus	99-102
15654337-8	2005	These results suggest that Tpr has a role in the nuclear export of N-terminal htt and that polyQ expansion reduces this nuclear export to cause the nuclear accumulation of htt.	polyglutamine	91-96	huntingtin	Mus musculus	172-175
15649316-0	2005	Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation.	polyglutamine	94-107	huntingtin	Mus musculus	33-43
15649316-1	2005	BACKGROUND: Huntington"s disease (HD) is an inherited neurodegenerative disorder triggered by an expanded polyglutamine tract in huntingtin that is thought to confer a new conformational property on this large protein.	polyglutamine	106-119	huntingtin	Mus musculus	129-139
15649316-8	2005	Of these, both juglone and celastrol were effective in reversing the abnormal cellular localization of full-length mutant huntingtin observed in mutant HdhQ111/Q111 striatal cells.	celastrol	27-36	huntingtin	Mus musculus	122-132
15379999-0	2004	HAP1 facilitates effects of mutant huntingtin on inositol 1,4,5-trisphosphate-induced Ca release in primary culture of striatal medium spiny neurons.	Inositol 1,4,5-Trisphosphate	49-77	huntingtin	Mus musculus	35-45
15379999-1	2004	Huntington"s disease is caused by polyglutamine expansion (exp) in huntingtin (Htt).	polyglutamine	34-47	huntingtin	Mus musculus	67-77
15379999-1	2004	Huntington"s disease is caused by polyglutamine expansion (exp) in huntingtin (Htt).	polyglutamine	34-47	huntingtin	Mus musculus	79-82
15379887-2	2004	We found that a 60-kDa protein was increased in Neuro2a cells expressing the N-terminal portion of huntingtin with expanded polyglutamine.	polyglutamine	124-137	huntingtin	Mus musculus	99-109
15336977-2	2004	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	16-29	huntingtin	Mus musculus	96-106
15336977-2	2004	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	16-29	huntingtin	Mus musculus	108-111
15336977-2	2004	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	31-36	huntingtin	Mus musculus	96-106
15336977-2	2004	HD is caused by polyglutamine (polyQ) expansion (exp) in the amino-terminal region of a protein huntingtin (Htt).	polyglutamine	31-36	huntingtin	Mus musculus	108-111
15190011-1	2004	Huntington"s disease (HD) results from the expansion of a glutamine repeat near the N-terminus of huntingtin (htt).	Glutamine	58-67	huntingtin	Mus musculus	98-108
15371500-5	2004	Activation of IKK is likely mediated by direct interaction with mutant Htt, because the expanded polyglutamine stretch and adjacent proline-rich motifs in mutant Htt interact with IKKgamma, a regulatory subunit of IKK.	polyglutamine	97-110	huntingtin	Mus musculus	71-74
15371500-5	2004	Activation of IKK is likely mediated by direct interaction with mutant Htt, because the expanded polyglutamine stretch and adjacent proline-rich motifs in mutant Htt interact with IKKgamma, a regulatory subunit of IKK.	polyglutamine	97-110	huntingtin	Mus musculus	162-165
15371500-5	2004	Activation of IKK is likely mediated by direct interaction with mutant Htt, because the expanded polyglutamine stretch and adjacent proline-rich motifs in mutant Htt interact with IKKgamma, a regulatory subunit of IKK.	Proline	132-139	huntingtin	Mus musculus	71-74
15371500-5	2004	Activation of IKK is likely mediated by direct interaction with mutant Htt, because the expanded polyglutamine stretch and adjacent proline-rich motifs in mutant Htt interact with IKKgamma, a regulatory subunit of IKK.	Proline	132-139	huntingtin	Mus musculus	162-165
15359012-1	2004	Huntington"s disease results from a polyglutamine expansion in the N-terminal region of huntingtin (htt).	polyglutamine	36-49	huntingtin	Mus musculus	88-98
15359012-1	2004	Huntington"s disease results from a polyglutamine expansion in the N-terminal region of huntingtin (htt).	polyglutamine	36-49	huntingtin	Mus musculus	100-103
15190011-1	2004	Huntington"s disease (HD) results from the expansion of a glutamine repeat near the N-terminus of huntingtin (htt).	Glutamine	58-67	huntingtin	Mus musculus	110-113
15190011-3	2004	This pathology has been reproduced in transgenic mice expressing the first 171 amino acids of htt with 82 glutamines along with losses of motoric function, hypoactivity and abbreviated life-span.	Glutamine	106-116	huntingtin	Mus musculus	94-97
15280037-1	2004	Nuclear aggregates of enhanced green fluorescent protein and nuclear localization signal-fused truncated N-terminal huntingtin containing 150 repeats of glutamine residue were purified from ecdysine-inducible mutant neuro2A cell line by sequential extraction of nuclear soluble proteins.	Glutamine	153-162	huntingtin	Mus musculus	116-126
15146184-5	2004	This protects against polyglutamine toxicity, as the specific mTOR inhibitor rapamycin attenuates huntingtin accumulation and cell death in cell models of Huntington disease, and inhibition of autophagy has the converse effects.	Sirolimus	77-86	huntingtin	Mus musculus	98-108
15163634-0	2004	Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release.	Calcium	75-82	huntingtin	Mus musculus	7-17
15163634-1	2004	Huntington"s disease (HD) is initiated by an abnormally expanded polyglutamine stretch in the huntingtin protein, conferring a novel property on the protein that leads to the loss of striatal neurons.	polyglutamine	65-78	huntingtin	Mus musculus	94-104
15163634-6	2004	We further demonstrated that a recombinant truncated mutant huntingtin protein, but not a wild-type, directly induced mitochondrial permeability transition (MPT) pore opening in isolated mouse liver mitochondria, an effect that was prevented completely by cyclosporin A (CSA) and ATP.	Cyclosporine	256-269	huntingtin	Mus musculus	60-70
15163634-6	2004	We further demonstrated that a recombinant truncated mutant huntingtin protein, but not a wild-type, directly induced mitochondrial permeability transition (MPT) pore opening in isolated mouse liver mitochondria, an effect that was prevented completely by cyclosporin A (CSA) and ATP.	Cyclosporine	271-274	huntingtin	Mus musculus	60-70
15163634-6	2004	We further demonstrated that a recombinant truncated mutant huntingtin protein, but not a wild-type, directly induced mitochondrial permeability transition (MPT) pore opening in isolated mouse liver mitochondria, an effect that was prevented completely by cyclosporin A (CSA) and ATP.	Adenosine Triphosphate	280-283	huntingtin	Mus musculus	60-70
15163634-9	2004	The mutant huntingtin protein-induced MPT pore opening was accompanied by a significant release of cytochrome c, an effect completely inhibited by CSA.	Cyclosporine	147-150	huntingtin	Mus musculus	11-21
14981075-1	2004	Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) tract expansion near the N terminus of huntingtin (Htt).	polyglutamine	70-83	huntingtin	Mus musculus	131-141
14981075-1	2004	Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) tract expansion near the N terminus of huntingtin (Htt).	polyglutamine	70-83	huntingtin	Mus musculus	143-146
14981075-1	2004	Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) tract expansion near the N terminus of huntingtin (Htt).	polyglutamine	85-90	huntingtin	Mus musculus	131-141
14981075-1	2004	Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) tract expansion near the N terminus of huntingtin (Htt).	polyglutamine	85-90	huntingtin	Mus musculus	143-146
14981075-4	2004	Here, we identify two calpain cleavage sites in Htt and show that mutation of these sites renders the polyQ expanded Htt less susceptible to proteolysis and aggregation, resulting in decreased toxicity in an in vitro cell culture model.	polyglutamine	102-107	huntingtin	Mus musculus	48-51
14981075-4	2004	Here, we identify two calpain cleavage sites in Htt and show that mutation of these sites renders the polyQ expanded Htt less susceptible to proteolysis and aggregation, resulting in decreased toxicity in an in vitro cell culture model.	polyglutamine	102-107	huntingtin	Mus musculus	117-120
15147313-1	2004	Huntington"s disease (HD) is a fatal neurodegenerative disease caused by a CAG repeat expansion coding for an expanded polyglutamine tract in the huntingtin protein.	polyglutamine	119-132	huntingtin	Mus musculus	146-156
14962977-1	2004	Extensive striatal neuronal loss occurs in Huntington"s disease (HD), which is caused by an expanded polyglutamine tract in huntingtin (htt).	polyglutamine	101-114	huntingtin	Mus musculus	124-134
14962977-1	2004	Extensive striatal neuronal loss occurs in Huntington"s disease (HD), which is caused by an expanded polyglutamine tract in huntingtin (htt).	polyglutamine	101-114	huntingtin	Mus musculus	136-139
14962977-9	2004	These data show that mutant htt specifically increases cell vulnerability to mitochondrial complex II inhibition and further switched the type of cell death induced by complex II inhibition from apoptosis to a non-apoptotic form, caused by mitochondrial membrane depolarization, probably initiated by mitochondrial calcium overload and subsequent PTP opening.	Calcium	315-322	huntingtin	Mus musculus	28-31
15048901-0	2004	Paroxetine retards disease onset and progression in Huntingtin mutant mice.	Paroxetine	0-10	huntingtin	Mus musculus	52-62
15048901-1	2004	We report that administration of paroxetine, a widely prescribed antidepressant drug that acts by inhibiting reuptake of the neurotransmitter serotonin, suppresses the neurodegenerative process and increases the survival of huntingtin mutant mice, an animal model of Huntington"s disease (HD).	Paroxetine	33-43	huntingtin	Mus musculus	224-234
15048901-1	2004	We report that administration of paroxetine, a widely prescribed antidepressant drug that acts by inhibiting reuptake of the neurotransmitter serotonin, suppresses the neurodegenerative process and increases the survival of huntingtin mutant mice, an animal model of Huntington"s disease (HD).	Serotonin	142-151	huntingtin	Mus musculus	224-234
14713958-8	2004	Binding of caspase-2 to Htt is polyglutamine repeat-length dependent, and therefore may serve as a critical initiation step in HD cell death.	polyglutamine	31-44	huntingtin	Mus musculus	24-27
14999077-1	2004	Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by a CAG repeat expansion encoding an extended polyglutamine tract in the huntingtin protein.	polyglutamine	124-137	huntingtin	Mus musculus	151-161
15033175-2	2004	We tested the hypothesis that enhanced NMDAR-mediated excitotoxicity is mediated by the mitochondrial-associated apoptotic pathway in cultured MSNs from YAC transgenic mice expressing full-length huntingtin (htt) with a polyglutamine (polyQ) expansion of 46 or 72 (YAC46 or YAC72).	polyglutamine	220-233	huntingtin	Mus musculus	208-211
14522959-2	2003	Early events in the disease cascade, which predate overt pathology in Hdh CAG knock-in mouse striatum, implicate enhanced N-methyl-D-aspartate (NMDA) receptor activation, with excitotoxity caused by aberrant Ca2+ influx.	N-Methylaspartate	122-142	huntingtin	Mus musculus	70-73
14667455-2	2004	The disease is caused by an unstable expanded trinucleotide (CAG) repeat encoding a polyglutamine stretch in the IT15 gene for huntingtin, a protein of unknown function.	trinucleotide	46-59	huntingtin	Mus musculus	113-117
14667455-2	2004	The disease is caused by an unstable expanded trinucleotide (CAG) repeat encoding a polyglutamine stretch in the IT15 gene for huntingtin, a protein of unknown function.	trinucleotide	46-59	huntingtin	Mus musculus	127-137
14667455-2	2004	The disease is caused by an unstable expanded trinucleotide (CAG) repeat encoding a polyglutamine stretch in the IT15 gene for huntingtin, a protein of unknown function.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	61-64	huntingtin	Mus musculus	113-117
14667455-2	2004	The disease is caused by an unstable expanded trinucleotide (CAG) repeat encoding a polyglutamine stretch in the IT15 gene for huntingtin, a protein of unknown function.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	61-64	huntingtin	Mus musculus	127-137
14667455-2	2004	The disease is caused by an unstable expanded trinucleotide (CAG) repeat encoding a polyglutamine stretch in the IT15 gene for huntingtin, a protein of unknown function.	polyglutamine	84-97	huntingtin	Mus musculus	113-117
14667455-2	2004	The disease is caused by an unstable expanded trinucleotide (CAG) repeat encoding a polyglutamine stretch in the IT15 gene for huntingtin, a protein of unknown function.	polyglutamine	84-97	huntingtin	Mus musculus	127-137
15105254-6	2004	The inheritance of polyglutamine-expanded huntingtin may promote neuronal degeneration in Huntington"s disease (HD), in part, by increasing MAOS.	polyglutamine	19-32	huntingtin	Mus musculus	42-52
14522959-2	2003	Early events in the disease cascade, which predate overt pathology in Hdh CAG knock-in mouse striatum, implicate enhanced N-methyl-D-aspartate (NMDA) receptor activation, with excitotoxity caused by aberrant Ca2+ influx.	N-Methylaspartate	144-148	huntingtin	Mus musculus	70-73
14522959-4	2003	Elevated levels of activated Ser(P)473-Akt are detected in extracts of Hdh(Q111/Q111) striatum and cultured mutant STHdh(Q111/Q111) striatal cells, compared with their wild type counterparts.	Serine	29-32	huntingtin	Mus musculus	71-74
12657678-8	2003	Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments.	Glutamine	132-141	huntingtin	Mus musculus	43-53
14643383-1	2003	N-Methyl-D-aspartate receptor (NMDAR)-mediated excitotoxicity has been proposed to play a role in Huntington disease (HD), caused by expansion of a polyglutamine tract in the protein huntingtin.	polyglutamine	148-161	huntingtin	Mus musculus	183-193
12969246-1	2003	Huntington"s disease (HD) is an autosomal dominant disorder caused by an expansion in the number of glutamine repeats in the N-terminal region of the huntingtin protein.	Glutamine	100-109	huntingtin	Mus musculus	150-160
12787055-6	2003	Neuropathological sequelae of gross brain and neuronal atrophy and huntingtin aggregates were delayed in creatine-treated R6/2 mice started at 6 weeks.	Creatine	105-113	huntingtin	Mus musculus	67-77
12706247-1	2003	Huntington"s disease (HD) is a neurodegenerative disorder caused by expansion of a polyglutamine tract in a protein called huntingtin.	polyglutamine	83-96	huntingtin	Mus musculus	123-133
12589027-2	2003	We show that the progression of neuropathological (formation of huntingtin inclusions and apoptotic protease activation), behavioral (motor dysfunction), and metabolic (glucose intolerance and tissue wasting) abnormalities in huntingtin mutant mice, an animal model of HD, are retarded when the mice are maintained on a dietary restriction (DR) feeding regimen resulting in an extension of their life span.	Glucose	169-176	huntingtin	Mus musculus	226-236
12588797-4	2003	Furthermore, cAMP levels in Hdh(Q111) striatum declined from an early age (10 weeks), and cAMP was significantly decreased in HD postmortem brain and lymphoblastoid cells, attesting to a chronic deficit in man.	Cyclic AMP	13-17	huntingtin	Mus musculus	28-31
12559971-7	2003	These results suggest that the mitochondrial calcium handling defects seen in Huntington"s disease cell lines and transgenic mice may be due, in part, to direct, deleterious effects of mutant huntingtin on mitochondria.	Calcium	45-52	huntingtin	Mus musculus	192-202
12554681-1	2003	Somatic instability of expanded HD CAG repeats that encode the polyglutamine tract in mutant huntingtin has been implicated in the striatal selectivity of Huntington"s disease (HD) pathology.	polyglutamine	63-76	huntingtin	Mus musculus	93-103
12554681-4	2003	The absence of Msh2 also eliminated striatal mutant huntingtin with somatically expanded glutamine tracts and caused an approximately 5 month delay in nuclear mutant protein accumulation, but did not alter the striatal specificity of this early phenotype.	Glutamine	89-98	huntingtin	Mus musculus	52-62
12554681-5	2003	Thus, somatic HD CAG instability appears to be a consequence of a striatal-selective disease process that accelerates the timing of an early disease phenotype, via expansion of the glutamine tract in mutant huntingtin.	Glutamine	181-190	huntingtin	Mus musculus	207-217
14653308-5	2003	5-HTT null mutants on the 129S6 background showed reduced 5-HT(1A) receptor binding (as measured by quantitative autoradiography) and reduced 5-HT(1A) receptor function (as measured by 8-OH-DPAT-induced hypothermia).	8-Hydroxy-2-(di-n-propylamino)tetralin	185-194	huntingtin	Mus musculus	2-5
12913073-0	2003	Abnormal association of mutant huntingtin with synaptic vesicles inhibits glutamate release.	Glutamic Acid	74-83	huntingtin	Mus musculus	31-41
12913073-1	2003	In Huntington disease (HD), polyglutamine expansion causes the disease protein huntingtin to aggregate and accumulate in the nucleus and cytoplasm.	polyglutamine	28-41	huntingtin	Mus musculus	79-89
12891671-3	2003	Because the tetracyclines have also been reported to inhibit aggregation in other amyloid disorders, we have investigated their ability to inhibit huntingtin aggregation and further explored their efficacy in preclinical mouse trials.	Tetracyclines	12-25	huntingtin	Mus musculus	147-157
12891671-4	2003	We show that tetracyclines are potent inhibitors of huntingtin aggregation in a hippocampal slice culture model of HD at an effective concentration of 30 microM.	Tetracyclines	13-26	huntingtin	Mus musculus	52-62
12890790-1	2003	Huntington"s disease (HD) is caused by a polyglutamine expansion in the disease protein huntingtin.	polyglutamine	41-54	huntingtin	Mus musculus	88-98
12890790-2	2003	The polyglutamine expansion causes huntingtin to interact abnormally with a number of proteins.	polyglutamine	4-17	huntingtin	Mus musculus	35-45
12657678-8	2003	Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments.	Glutamine	132-141	huntingtin	Mus musculus	82-92
12657678-8	2003	Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments.	Glutamine	132-141	huntingtin	Mus musculus	82-92
12657678-8	2003	Transfection of cultured cells with mutant huntingtin revealed that an N-terminal huntingtin fragment (amino acids 1-208 plus a 120 glutamine repeat) caused a greater increase in caspase activity than did exon 1 huntingtin and longer huntingtin fragments.	Glutamine	132-141	huntingtin	Mus musculus	82-92
12089530-5	2002	Thus, mitochondrial calcium abnormalities occur early in HD pathogenesis and may be a direct effect of mutant huntingtin on the organelle.	Calcium	20-27	huntingtin	Mus musculus	110-120
12586550-5	2002	Disrupted expression of a subset of transcription factors in pancreatic beta cells by a polyglutamine expansion tract in the huntingtin protein selectively impairs insulin gene expression to result in insulin deficiency and diabetes.	polyglutamine	88-101	huntingtin	Mus musculus	125-135
12417652-1	2002	Aggregates of green fluorescent protein (GFP)-fused truncated N-terminal huntingtin containing abnormally long polyglutamine tracts (150 repeats of glutamine residue) were purified from an ecdysone-inducible mutant neuro2A cell line (HD150Q-28) by using a fluorescence-activated cell sorter.	polyglutamine	111-124	huntingtin	Mus musculus	73-83
12417652-1	2002	Aggregates of green fluorescent protein (GFP)-fused truncated N-terminal huntingtin containing abnormally long polyglutamine tracts (150 repeats of glutamine residue) were purified from an ecdysone-inducible mutant neuro2A cell line (HD150Q-28) by using a fluorescence-activated cell sorter.	Glutamine	115-124	huntingtin	Mus musculus	73-83
12217951-1	2002	The hallmark striatal neurodegeneration of Huntington"s disease (HD) is first triggered by a dominant property of the expanded glutamine tract in mutant huntingtin that increases in severity with glutamine size.	Glutamine	127-136	huntingtin	Mus musculus	153-163
12217951-1	2002	The hallmark striatal neurodegeneration of Huntington"s disease (HD) is first triggered by a dominant property of the expanded glutamine tract in mutant huntingtin that increases in severity with glutamine size.	Glutamine	196-205	huntingtin	Mus musculus	153-163
12217951-2	2002	Indeed 111-glutamine murine huntingtin leads to a dominant cascade of phenotypes in Hdh(Q111) mice, although these abnormalities are not manifest in Hdh(Q50) mice, with 50-glutamine mutant protein.	Glutamine	11-20	huntingtin	Mus musculus	28-38
12217951-2	2002	Indeed 111-glutamine murine huntingtin leads to a dominant cascade of phenotypes in Hdh(Q111) mice, although these abnormalities are not manifest in Hdh(Q50) mice, with 50-glutamine mutant protein.	Glutamine	11-20	huntingtin	Mus musculus	84-87
12217951-2	2002	Indeed 111-glutamine murine huntingtin leads to a dominant cascade of phenotypes in Hdh(Q111) mice, although these abnormalities are not manifest in Hdh(Q50) mice, with 50-glutamine mutant protein.	Glutamine	172-181	huntingtin	Mus musculus	28-38
12223539-8	2002	However, in HD, cleavage of mutant htt would release N-terminal fragments with the potential for increased toxicity and accumulation caused by the presence of the expanded polyglutamine tract.	polyglutamine	172-185	huntingtin	Mus musculus	35-38
12193654-15	2002	Here we show that structural analyses of soluble huntingtin exon 1 fusion proteins with 16 to 46 glutamine residues reveal extended structures with random coil characteristics and no evidence for a global conformational change above 36 glutamines.	Glutamine	97-106	huntingtin	Mus musculus	49-59
12193654-16	2002	An antibody (MW1) Fab fragment, which recognizes full-length huntingtin in mouse brain sections, binds specifically to exon 1 constructs containing normal and expanded poly(Gln) tracts, with affinity and stoichiometry that increase with poly(Gln) length.	poly(gln)	168-177	huntingtin	Mus musculus	61-71
12193654-16	2002	An antibody (MW1) Fab fragment, which recognizes full-length huntingtin in mouse brain sections, binds specifically to exon 1 constructs containing normal and expanded poly(Gln) tracts, with affinity and stoichiometry that increase with poly(Gln) length.	poly(gln)	237-246	huntingtin	Mus musculus	61-71
12165554-1	2002	Previous analyses of gene expression in a mouse model of Huntington"s disease (R6/2) indicated that an N-terminal fragment of mutant huntingtin causes downregulation of striatal signaling genes and particularly those normally induced by cAMP and retinoic acid.	Cyclic AMP	237-241	huntingtin	Mus musculus	133-143
12165554-1	2002	Previous analyses of gene expression in a mouse model of Huntington"s disease (R6/2) indicated that an N-terminal fragment of mutant huntingtin causes downregulation of striatal signaling genes and particularly those normally induced by cAMP and retinoic acid.	Tretinoin	246-259	huntingtin	Mus musculus	133-143
12165556-0	2002	Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington"s disease.	polyglutamine	58-71	huntingtin	Mus musculus	10-20
12165556-4	2002	Oligonucleotide microarray analyses of HD46 and YAC72 mice identified fewer differentially expressed mRNAs than were seen in transgenic mice expressing short N-terminal mutant htt fragments.	Oligonucleotides	0-15	huntingtin	Mus musculus	176-179
12149470-7	2002	Specifically, R6/2 mice began receiving TUDCA at 6 weeks of age and exhibited reduced striatal atrophy, decreased striatal apoptosis, as well as fewer and smaller size ubiquitinated neuronal intranuclear huntingtin inclusions.	ursodoxicoltaurine	40-45	huntingtin	Mus musculus	204-214
12490527-0	2003	Cell death triggered by polyglutamine-expanded huntingtin in a neuronal cell line is associated with degradation of CREB-binding protein.	polyglutamine	24-37	huntingtin	Mus musculus	47-57
12490527-1	2003	Huntington"s Disease belongs to the CAG repeat family of neurodegenerative diseases and is characterized by the presence of an expanded polyglutamine (polyQ) repeat in the huntingtin (htt) gene product.	polyglutamine	136-149	huntingtin	Mus musculus	172-182
12490527-1	2003	Huntington"s Disease belongs to the CAG repeat family of neurodegenerative diseases and is characterized by the presence of an expanded polyglutamine (polyQ) repeat in the huntingtin (htt) gene product.	polyglutamine	136-149	huntingtin	Mus musculus	184-187
12490527-1	2003	Huntington"s Disease belongs to the CAG repeat family of neurodegenerative diseases and is characterized by the presence of an expanded polyglutamine (polyQ) repeat in the huntingtin (htt) gene product.	polyglutamine	151-156	huntingtin	Mus musculus	172-182
12490527-1	2003	Huntington"s Disease belongs to the CAG repeat family of neurodegenerative diseases and is characterized by the presence of an expanded polyglutamine (polyQ) repeat in the huntingtin (htt) gene product.	polyglutamine	151-156	huntingtin	Mus musculus	184-187
12490527-2	2003	PolyQ-expanded htt accumulates within large aggregates that are found in various subcellular compartments, but are more often localized within the nucleus.	polyglutamine	0-5	huntingtin	Mus musculus	15-18
12490527-4	2003	Nuclear inclusions containing polyQ-expanded htt recruit the transcriptional cofactor, CREB-binding protein (CBP).	polyglutamine	30-35	huntingtin	Mus musculus	45-48
12490527-6	2003	In the HT22 hippocampal cell line, we find that toxicity within individual cells induced by polyQ-expanded htt, as revealed by a TUNEL assay, is associated with the localization of the mutant htt within either nuclear or perinuclear aggregates.	polyglutamine	92-97	huntingtin	Mus musculus	107-110
12490527-6	2003	In the HT22 hippocampal cell line, we find that toxicity within individual cells induced by polyQ-expanded htt, as revealed by a TUNEL assay, is associated with the localization of the mutant htt within either nuclear or perinuclear aggregates.	polyglutamine	92-97	huntingtin	Mus musculus	192-195
12490527-7	2003	However, in addition to CBP recruitment, we show here that CBP ubiquitylation and degradation can be selectively enhanced by polyQ-expanded htt.	polyglutamine	125-130	huntingtin	Mus musculus	140-143
12490527-8	2003	Thus, selected substrates may be directed to the ubiquitin/proteasome-dependent protein degradation pathway in response to polyQ-expanded htt within the nucleus.	polyglutamine	123-128	huntingtin	Mus musculus	138-141
11960015-1	2002	The exon-1 peptide of huntingtin has 51 Gln repeats and produces the symptoms of Huntington"s disease in transgenic mice.	Glutamine	40-43	huntingtin	Mus musculus	22-32
12097468-2	2002	The current studies describe the production of 16-mer peptide nucleic acid (PNA) that is antisense around the methionine initiation codon of the huntingtin gene of Huntington"s disease (HD).	Methionine	110-120	huntingtin	Mus musculus	145-155
11698589-8	2001	Furthermore, the proteasome inhibitor lactacystin inhibited the aggregate clearance observed in culture, thus indicating that aggregate formation is a balance between the rate of huntingtin synthesis and its degradation by the proteasome.	lactacystin	38-49	huntingtin	Mus musculus	179-189
11912178-3	2002	In young Hdh knock-in mice, CAGs that expand the glutamine tract in mouse huntingtin to childhood-onset HD lengths lead to nuclear accumulation of full-length mutant huntingtin and later accumulation of insoluble fragment.	Glutamine	49-58	huntingtin	Mus musculus	9-12
11912178-3	2002	In young Hdh knock-in mice, CAGs that expand the glutamine tract in mouse huntingtin to childhood-onset HD lengths lead to nuclear accumulation of full-length mutant huntingtin and later accumulation of insoluble fragment.	Glutamine	49-58	huntingtin	Mus musculus	74-84
11912178-3	2002	In young Hdh knock-in mice, CAGs that expand the glutamine tract in mouse huntingtin to childhood-onset HD lengths lead to nuclear accumulation of full-length mutant huntingtin and later accumulation of insoluble fragment.	Glutamine	49-58	huntingtin	Mus musculus	166-176
11839795-2	2002	In HD, N-terminal fragments of huntingtin with an expanded glutamine tract are able to aggregate and accumulate in the nucleus.	Glutamine	59-68	huntingtin	Mus musculus	31-41
11839795-5	2002	In vitro binding and immunoprecipitation assays show that polyglutamine expansion enhances the interaction of N-terminal huntingtin with Sp1.	polyglutamine	58-71	huntingtin	Mus musculus	121-131
11854752-3	2002	Endogenous arfaptin 2 localizes to aggregates induced by expression of an abnormal amino-terminal fragment of huntingtin that contains polyglutamine (polyQ) expansions.	polyglutamine	135-148	huntingtin	Mus musculus	110-120
11854752-3	2002	Endogenous arfaptin 2 localizes to aggregates induced by expression of an abnormal amino-terminal fragment of huntingtin that contains polyglutamine (polyQ) expansions.	polyglutamine	150-155	huntingtin	Mus musculus	110-120
11784701-6	2002	R6/1 transgenics also showed reductions in body weight and in brain dopamine D(1)-like and D(2)-like quantitative receptor autoradiography which were unaltered by essential fatty acids.These findings indicate that early and sustained treatment with essential fatty acids are able to protect against motor deficits in R6/1 transgenic mice expressing exon 1 and a portion of intron 2 of the Huntingtin gene, and suggest that essential fatty acids may have therapeutic potential in Huntington"s disease.	Fatty Acids, Essential	249-270	huntingtin	Mus musculus	389-399
11751688-4	2001	A previous study reported that activation of the wild-type glucocorticoid receptor (wtGR) suppressed the aggregation of expanded polyglutamine proteins derived from AR and huntingtin, whereas a mutant receptor containing an internal deletion, GRDelta108-317, increased polyglutamine protein aggregation, in this case primarily within the nucleus.	polyglutamine	129-142	huntingtin	Mus musculus	172-182
11864629-4	2002	These mice express huntingtin exon 1 with a polyglutamine tract of 94 repeats in a tissue-specific and conditional manner using the tet regulatable system.	polyglutamine	44-57	huntingtin	Mus musculus	19-29
11895367-4	2002	In the present study, we have employed a technique used in detecting and quantifying aggregates of mutant huntingtin (cellulose acetate filtration) to examine the molecular characteristics of mutant SOD1 in three previously characterized transgenic mouse models of FALS.	acetylcellulose	118-135	huntingtin	Mus musculus	106-116
11821898-1	2002	An expanded polyglutamine domain in huntingtin underlies the pathogenic events in Huntington disease (HD), characterized by chorea, dementia and severe weight loss, culminating in death.	polyglutamine	12-25	huntingtin	Mus musculus	36-46
11821898-3	2002	Administration of the TGase competitive inhibitor, cystamine, to transgenic mice expressing exon 1 of huntingtin containing an expanded polyglutamine repeat, altered the course of their HD-like disease.	Cystamine	51-60	huntingtin	Mus musculus	102-112
11821898-3	2002	Administration of the TGase competitive inhibitor, cystamine, to transgenic mice expressing exon 1 of huntingtin containing an expanded polyglutamine repeat, altered the course of their HD-like disease.	polyglutamine	136-149	huntingtin	Mus musculus	102-112
11784701-6	2002	R6/1 transgenics also showed reductions in body weight and in brain dopamine D(1)-like and D(2)-like quantitative receptor autoradiography which were unaltered by essential fatty acids.These findings indicate that early and sustained treatment with essential fatty acids are able to protect against motor deficits in R6/1 transgenic mice expressing exon 1 and a portion of intron 2 of the Huntingtin gene, and suggest that essential fatty acids may have therapeutic potential in Huntington"s disease.	Fatty Acids, Essential	249-270	huntingtin	Mus musculus	389-399
11161468-2	2001	Here we determined whether expression of huntingtin containing the polyglutamine expansion augments NMDAR-mediated excitotoxicity.	polyglutamine	67-80	huntingtin	Mus musculus	41-51
11567051-4	2001	By contrast, Hdh (-/-) ES cells injected into blastocysts yielded offspring that were born and in adulthood were found to have Hdh (-/-) neurons throughout brain.	Einsteinium	23-25	huntingtin	Mus musculus	13-16
11567051-4	2001	By contrast, Hdh (-/-) ES cells injected into blastocysts yielded offspring that were born and in adulthood were found to have Hdh (-/-) neurons throughout brain.	Einsteinium	23-25	huntingtin	Mus musculus	127-130
11447996-3	2001	We examined the effects of creatine administration in a transgenic mouse model of HD produced by 82 polyglutamine repeats in a 171 amino acid N-terminal fragment of huntingtin (N171-82Q).	Creatine	27-35	huntingtin	Mus musculus	165-175
11709539-1	2001	Huntingtin is an essential protein that with mutant polyglutamine tracts initiates dominant striatal neurodegeneration in Huntington"s disease (HD).	polyglutamine	52-65	huntingtin	Mus musculus	0-10
11719267-2	2001	Peptide array epitope mapping shows that mAbs MW1-6 specifically bind the polyQ domain of Htt exon 1.	polyglutamine	74-79	huntingtin	Mus musculus	90-93
11719267-10	2001	This suggests that in its various subcellular locations, the polyQ domain of Htt either takes on different conformations and/or is differentially occluded by Htt binding proteins.	polyglutamine	61-66	huntingtin	Mus musculus	77-80
11719267-10	2001	This suggests that in its various subcellular locations, the polyQ domain of Htt either takes on different conformations and/or is differentially occluded by Htt binding proteins.	polyglutamine	61-66	huntingtin	Mus musculus	158-161
11331615-0	2001	Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release.	polyglutamine	54-67	huntingtin	Mus musculus	98-108
11331615-2	2001	A 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	96-109	huntingtin	Mus musculus	74-84
11181933-7	2001	The selective 5-HT reuptake inhibitor paroxetine significantly prolonged the RT(50) in 5-HTT +/+ and 5-HTT +/- mice, without altering the maximal inhibitory effect of 5-HT.	Paroxetine	38-48	huntingtin	Mus musculus	89-92
11092762-1	2000	Expansion of a polyglutamine repeat in huntingtin causes Huntington"s disease (HD).	polyglutamine	15-28	huntingtin	Mus musculus	39-49
11092762-2	2000	Although full-length huntingtin is predominantly distributed in the cytoplasm, N-terminal fragments of huntingtin with expanded polyglutamine tracts are able to accumulate in the nucleus and kill neurons through apoptotic pathways.	polyglutamine	128-141	huntingtin	Mus musculus	103-113
11040449-0	2000	DMSO and glycerol reduce bacterial death induced by expression of truncated N-terminal huntingtin with expanded polyglutamine tracts.	Dimethyl Sulfoxide	0-4	huntingtin	Mus musculus	87-97
11040449-0	2000	DMSO and glycerol reduce bacterial death induced by expression of truncated N-terminal huntingtin with expanded polyglutamine tracts.	Glycerol	9-17	huntingtin	Mus musculus	87-97
11040449-0	2000	DMSO and glycerol reduce bacterial death induced by expression of truncated N-terminal huntingtin with expanded polyglutamine tracts.	polyglutamine	112-125	huntingtin	Mus musculus	87-97
11040449-6	2000	These results suggest that DMSO and glycerol may decrease the toxicity of huntingtin with expanded polyglutamine tracts by acting as chemical chaperones.	Dimethyl Sulfoxide	27-31	huntingtin	Mus musculus	74-84
11040449-6	2000	These results suggest that DMSO and glycerol may decrease the toxicity of huntingtin with expanded polyglutamine tracts by acting as chemical chaperones.	Glycerol	36-44	huntingtin	Mus musculus	74-84
11040449-6	2000	These results suggest that DMSO and glycerol may decrease the toxicity of huntingtin with expanded polyglutamine tracts by acting as chemical chaperones.	polyglutamine	99-112	huntingtin	Mus musculus	74-84
11030759-1	2000	An unstable CAG triplet repeat expansion encoding a polyglutamine stretch within the ubiquitously expressed protein huntingtin is responsible for causing Huntington"s disease (HD).	polyglutamine	52-65	huntingtin	Mus musculus	116-126
10932179-1	2000	Huntington disease (HD) is caused by expansion of a glutamine repeat in the amino-terminal region of huntingtin.	Glutamine	52-61	huntingtin	Mus musculus	101-111
10942430-1	2000	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by polyglutamine expansion in the disease protein, huntingtin.	polyglutamine	88-101	huntingtin	Mus musculus	136-146
10942430-4	2000	Here we demonstrate that newly synthesized polyglutamine-expanded truncated huntingtin interacts with members of Hsp40 and Hsp70 families of chaperones in a polyglutamine length-dependent manner.	polyglutamine	43-56	huntingtin	Mus musculus	76-86
10942430-4	2000	Here we demonstrate that newly synthesized polyglutamine-expanded truncated huntingtin interacts with members of Hsp40 and Hsp70 families of chaperones in a polyglutamine length-dependent manner.	polyglutamine	157-170	huntingtin	Mus musculus	76-86
10932179-5	2000	N-terminal mutant huntingtin also binds to synaptic vesicles and inhibits their glutamate uptake in vitro.	Glutamic Acid	80-89	huntingtin	Mus musculus	18-28
10699173-0	2000	Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knock-in mice.	Glutamine	5-14	huntingtin	Mus musculus	68-78
10844007-3	2000	Dietary creatine supplementation significantly improved survival, slowed the development of brain atrophy, and delayed atrophy of striatal neurons and the formation of huntingtin-positive aggregates in R6/2 mice.	Creatine	8-16	huntingtin	Mus musculus	168-178
10754231-2	2000	Here we demonstrate that the levels of two of these metabolites, the free radical generator 3-hydroxykynurenine (3HK) and the neuroprotectant kynurenate (KYNA), are increased in the neostriatum of stage 1 HD patients and in the brain of mice transgenic for full-length mutant huntingtin.	3-hydroxykynurenine	92-111	huntingtin	Mus musculus	276-286
10754231-2	2000	Here we demonstrate that the levels of two of these metabolites, the free radical generator 3-hydroxykynurenine (3HK) and the neuroprotectant kynurenate (KYNA), are increased in the neostriatum of stage 1 HD patients and in the brain of mice transgenic for full-length mutant huntingtin.	3-hydroxykynurenine	113-116	huntingtin	Mus musculus	276-286
10754231-2	2000	Here we demonstrate that the levels of two of these metabolites, the free radical generator 3-hydroxykynurenine (3HK) and the neuroprotectant kynurenate (KYNA), are increased in the neostriatum of stage 1 HD patients and in the brain of mice transgenic for full-length mutant huntingtin.	Kynurenic Acid	142-152	huntingtin	Mus musculus	276-286
10754231-2	2000	Here we demonstrate that the levels of two of these metabolites, the free radical generator 3-hydroxykynurenine (3HK) and the neuroprotectant kynurenate (KYNA), are increased in the neostriatum of stage 1 HD patients and in the brain of mice transgenic for full-length mutant huntingtin.	Kynurenic Acid	154-158	huntingtin	Mus musculus	276-286
10699173-1	2000	Huntington"s disease (HD) is caused by an expanded N-terminal glutamine tract that endows huntingtin with a striatal-selective structural property ultimately toxic to medium spiny neurons.	Glutamine	62-71	huntingtin	Mus musculus	90-100
10699173-2	2000	In precise genetic models of juvenile HD, HdhQ92 and HdhQ111 knock-in mice, long polyglutamine segments change huntingtin"s physical properties, producing HD-like in vivo correlates in the striatum, including nuclear localization of a version of the full-length protein predominant in medium spiny neurons, and subsequent formation of N-terminal inclusions and insoluble aggregate.	polyglutamine	81-94	huntingtin	Mus musculus	111-121
10699173-3	2000	These changes show glutamine length dependence and dominant inheritance with recruitment of wild-type protein, critical features of the altered HD property that strongly implicate them in the HD disease process and that suggest alternative pathogenic scenarios: the effect of the glutamine tract may act by altering interaction with a critical cellular constituent or by depleting a form of huntingtin essential to medium spiny striatal neurons.	Glutamine	19-28	huntingtin	Mus musculus	391-401
10699173-3	2000	These changes show glutamine length dependence and dominant inheritance with recruitment of wild-type protein, critical features of the altered HD property that strongly implicate them in the HD disease process and that suggest alternative pathogenic scenarios: the effect of the glutamine tract may act by altering interaction with a critical cellular constituent or by depleting a form of huntingtin essential to medium spiny striatal neurons.	Glutamine	280-289	huntingtin	Mus musculus	391-401
9949199-1	1999	Huntington"s disease (HD) is an inherited, neurodegenerative disorder caused by the expansion of a glutamine repeat in the N-terminus of the huntingtin protein.	Glutamine	99-108	huntingtin	Mus musculus	141-151
10655548-1	2000	Huntington"s disease (HD) is a neurodegenerative disease associated with polyglutamine expansion in huntingtin, a widely expressed protein.	polyglutamine	73-86	huntingtin	Mus musculus	100-110
10434303-4	1999	The transgene encoding normal huntingtin consists of 9417 bp of the huntingtin coding sequences including 16 tandem CAGs coding for polyglutamines as part of exon 1.	polyglutamine	132-146	huntingtin	Mus musculus	30-40
10217265-2	1999	The gene mutation that causes HD encodes an expanded polyglutamine tract of &gt;35 in huntingtin, a protein of unknown function.	polyglutamine	53-66	huntingtin	Mus musculus	86-96
11128600-1	2000	Huntington Disease (HD) results from polyglutamine expansion within the N-terminus of huntingtin.	polyglutamine	37-50	huntingtin	Mus musculus	86-96
9949199-2	1999	To gain insight into the pathogenesis of HD, we generated transgenic mice that express a cDNA encoding an N-terminal fragment (171 amino acids) of huntingtin with 82, 44 or 18 glutamines.	Glutamine	176-186	huntingtin	Mus musculus	147-157
10037472-1	1999	Huntington disease (HD) is a neurodegenerative disorder associated with polyglutamine expansion in a recently identified protein, huntingtin.	polyglutamine	72-85	huntingtin	Mus musculus	130-140
9725082-1	1998	The gene mutation causing Huntington"s disease was identified in 1993 as an expanded trinucleotide repeat within the coding region for a 348-kd protein called huntingtin.	trinucleotide	85-98	huntingtin	Mus musculus	159-169
9819135-4	1998	The CAG repeats are translated to polyglutamine repeats in the expressed protein, huntingtin.	polyglutamine	34-47	huntingtin	Mus musculus	82-92
9819135-7	1998	Polyglutamine expansion alters many of these interactions and leads to huntingtin aggregation and the formation of neuronal nuclear inclusions, ultimately culminating in cell death.	polyglutamine	0-13	huntingtin	Mus musculus	71-81
9878254-3	1998	In a yeast two-hybrid system, association with a huntingtin fragment containing an elongated stretch of polyglutamines was observed recently.	polyglutamine	104-118	huntingtin	Mus musculus	49-59
8009370-6	1994	Despite the overall high level of conservation, Hdh possesses an imperfect CAG repeat encoding only seven consecutive glutamines, compared to the 13-36 residues that are normal in man.	Glutamine	118-128	huntingtin	Mus musculus	48-51
9462744-3	1998	In vitro these huntingtin-containing aggregates disrupt normal cellular architecture and increase in frequency with polyglutamine length.	polyglutamine	116-129	huntingtin	Mus musculus	15-25
9462744-7	1998	Asymptomatic transgenic mice expressing full-length huntingtin with 138 polyglutamines form exclusively perinuclear aggregates in neurons.	polyglutamine	72-86	huntingtin	Mus musculus	52-62
9599014-1	1998	HAP1 (huntingtin associated protein) has previously been found to interact with huntingtin (htt) in a glutamine length dependent manner and has been proposed to play a role in the cell specific neurodegeneration observed in Huntington"s disease (HD).	Glutamine	102-111	huntingtin	Mus musculus	6-16
9599014-1	1998	HAP1 (huntingtin associated protein) has previously been found to interact with huntingtin (htt) in a glutamine length dependent manner and has been proposed to play a role in the cell specific neurodegeneration observed in Huntington"s disease (HD).	Glutamine	102-111	huntingtin	Mus musculus	92-95
9502734-6	1998	Consistent with preliminary histochemical analysis indicating that at least the transport of ferric ions is defective in Hdh mutants and in conjunction with the known localization of huntingtin in the membranes of vesicles associated with microtubules, we hypothesize that this protein is involved in the intracellular trafficking of nutrients in early embryos.	Ferric enterobactin ion	93-99	huntingtin	Mus musculus	121-124
9267034-0	1997	Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo.	polyglutamine	19-32	huntingtin	Mus musculus	0-10
9267034-2	1997	In this study, we show that the proteolytic cleavage of a GST-huntingtin fusion protein leads to the formation of insoluble high molecular weight protein aggregates only when the polyglutamine expansion is in the pathogenic range.	polyglutamine	179-192	huntingtin	Mus musculus	62-72
7759106-4	1995	Two dinucleotide (CT) and one trinucleotide intronic polymorphism in Hdh and an intronic CA polymorphism in the HD gene were identified.	Dinucleoside Phosphates	4-16	huntingtin	Mus musculus	69-72
7759106-4	1995	Two dinucleotide (CT) and one trinucleotide intronic polymorphism in Hdh and an intronic CA polymorphism in the HD gene were identified.	trinucleotide	30-43	huntingtin	Mus musculus	69-72
34884469-6	2021	Here, we tested the relevance of strain background for mutant huntingtin (mHTT) toxicity on the cellular level by investigating HD pathologies in YAC128 mice in the C57BL/6 background (YAC128/BL6).	mhtt	74-78	huntingtin	Mus musculus	62-72
26362846-0	2015	Rosiglitazone activation of PPARgamma-dependent signaling is neuroprotective in mutant huntingtin expressing cells.	Rosiglitazone	0-13	huntingtin	Mus musculus	87-97
26362846-2	2015	Using a mouse model of Huntington"s Disease (HD), we recently showed that PPARgamma not only played a major function in preventing HD, but also oral intake of a PPARgamma agonist (thiazolidinedione, TZD) significantly reduced the formation of mutant Huntingtin (mHtt) aggregates in the brain (e.g., cortex and striatum).	2,4-thiazolidinedione	180-197	huntingtin	Mus musculus	250-260
26362846-2	2015	Using a mouse model of Huntington"s Disease (HD), we recently showed that PPARgamma not only played a major function in preventing HD, but also oral intake of a PPARgamma agonist (thiazolidinedione, TZD) significantly reduced the formation of mutant Huntingtin (mHtt) aggregates in the brain (e.g., cortex and striatum).	tzd	199-202	huntingtin	Mus musculus	250-260
34962383-1	2022	Aggregation of mutant huntingtin, because of an expanded polyglutamine track, underlies the cause of neurodegeneration in Huntington disease (HD).	polyglutamine	57-70	huntingtin	Mus musculus	22-32
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	Mus musculus	25-29
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	Mus musculus	229-233
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	Mus musculus	25-29
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	Mus musculus	229-233
34331233-4	2021	Here, we demonstrated that the mouse pancreatic insulinoma cell line NIT-1 expressing N-terminal mutant huntingtin (mHTT) containing 160 polyglutamine (160Q cells) displayed lower cell proliferative ability than the cells expressing N-terminal wild-type HTT containing 20 polyglutamine (20Q cells).	polyglutamine	137-150	huntingtin	Mus musculus	104-114
34663519-2	2021	Here, we examined the effects of antioxidants on 3-nitropropionic acid (3-NP; a mitochondrial complex II inhibitor)-induced mitochondrial dysfunction and cell death in STHdhQ111 striatal cells carrying homozygous mutant HTT with extended CAG repeats compared with those in STHdhQ7 striatal cells.	3-nitropropionic acid	49-70	huntingtin	Mus musculus	220-223
34663519-2	2021	Here, we examined the effects of antioxidants on 3-nitropropionic acid (3-NP; a mitochondrial complex II inhibitor)-induced mitochondrial dysfunction and cell death in STHdhQ111 striatal cells carrying homozygous mutant HTT with extended CAG repeats compared with those in STHdhQ7 striatal cells.	3-nitropropionic acid	72-76	huntingtin	Mus musculus	220-223
34663519-7	2021	These results suggest that reduced mitochondrial complex II activity enhances cell death via intracellular ROS production and Drp1 oligomerization in striatal cells with mutant HTT and antioxidants may reduce striatal cell death.	Reactive Oxygen Species	107-110	huntingtin	Mus musculus	177-180
34648564-3	2021	Rhes is a Ras-related small GTP-binding protein highly expressed in the striatum that has been reported to modulate mTOR and sumoylation of mutant huntingtin to alter HD mouse model pathogenesis.	Guanosine Triphosphate	28-31	huntingtin	Mus musculus	147-157
34755099-1	2021	Huntington disease (HD) is a devastating neurodegenerative disorder characterized by aggregation of huntingtin (HTT) protein containing expanded polyglutamine (polyQ) tracts.	polyglutamine	145-158	huntingtin	Mus musculus	100-110
34755099-1	2021	Huntington disease (HD) is a devastating neurodegenerative disorder characterized by aggregation of huntingtin (HTT) protein containing expanded polyglutamine (polyQ) tracts.	polyglutamine	145-158	huntingtin	Mus musculus	112-115
34755099-1	2021	Huntington disease (HD) is a devastating neurodegenerative disorder characterized by aggregation of huntingtin (HTT) protein containing expanded polyglutamine (polyQ) tracts.	polyglutamine	160-165	huntingtin	Mus musculus	100-110
34755099-1	2021	Huntington disease (HD) is a devastating neurodegenerative disorder characterized by aggregation of huntingtin (HTT) protein containing expanded polyglutamine (polyQ) tracts.	polyglutamine	160-165	huntingtin	Mus musculus	112-115
34755099-5	2021	Administration of sEVs isolated from DNAJB6-overexpressing cells to cells expressing expanded polyQ tracts suppressed HTT aggregation.	polyglutamine	94-99	huntingtin	Mus musculus	118-121
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	Mus musculus	154-158
34330748-6	2021	LY379268 also reduces mutant huntingtin aggregate formation, neuronal cell death, and microglia activation in the striatum of both male and female zQ175 mice.	LY 379268	0-8	huntingtin	Mus musculus	29-39
34651228-0	2022	Longitudinal preclinical evaluation of the novel radioligand (11C)CHDI-626 for PET imaging of mutant huntingtin aggregates in Huntington"s disease.	(11c)chdi-626	61-74	huntingtin	Mus musculus	101-111
34651228-2	2022	Here we characterized and longitudinally assessed the novel radioligand (11C)CHDI-626 for mHTT PET imaging in the zQ175DN mouse model of HD.	(11c)chdi-626	72-85	huntingtin	Mus musculus	90-94
34250577-4	2021	We performed stereotaxic injection of AAV to selectively express HspBP1 in astrocytes in the brains of HD140Q knock-in (KI) mice that express mutant HTT ubiquitously but do not display obvious neurodegeneration.	CHEMBL2031461	38-41	huntingtin	Mus musculus	149-152
34390831-6	2021	HTT is palmitoylated at cysteine 214 by the huntingtin-interacting protein 14 (HIP14 or ZDHHC17) and 14-like (HIP14L or ZDHHC13) acyltransferases.	Cysteine	24-32	huntingtin	Mus musculus	0-3
34351166-0	2021	(11C)CHDI-626, a PET Tracer Candidate for Imaging Mutant Huntingtin Aggregates with Reduced Binding to AD Pathological Proteins.	Carbon-11	1-4	huntingtin	Mus musculus	57-67
34351166-0	2021	(11C)CHDI-626, a PET Tracer Candidate for Imaging Mutant Huntingtin Aggregates with Reduced Binding to AD Pathological Proteins.	chdi-626	5-13	huntingtin	Mus musculus	57-67
34351166-1	2021	The expanded polyglutamine-containing mutant huntingtin (mHTT) protein is implicated in neuronal degeneration of medium spiny neurons in Huntington"s disease (HD) for which multiple therapeutic approaches are currently being evaluated to eliminate or reduce mHTT.	polyglutamine	13-26	huntingtin	Mus musculus	45-55
34351166-1	2021	The expanded polyglutamine-containing mutant huntingtin (mHTT) protein is implicated in neuronal degeneration of medium spiny neurons in Huntington"s disease (HD) for which multiple therapeutic approaches are currently being evaluated to eliminate or reduce mHTT.	polyglutamine	13-26	huntingtin	Mus musculus	57-61
34351166-5	2021	We describe here the optimization of the benzo(4,5)imidazo(1,2-a)pyrimidine series that show selective binding to mHTT aggregates over Abeta- and/or tau-aggregates associated with Alzheimer"s disease pathology.	benzo(4,5)imidazo(1,2-a)pyrimidine	41-75	huntingtin	Mus musculus	114-118
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	Mus musculus	154-158
34239412-2	2021	Previous investigations in cell-free and cell-based disease models showed mHTT exon-1 (mHTTex1) fragments with pathogenic polyglutamine (polyQ) tracts (>40 glutamines) to self-assemble into highly stable, beta-sheet-rich protein aggregates with a fibrillar morphology.	polyglutamine	122-135	huntingtin	Mus musculus	74-78
34339019-7	2021	Furthermore, in striatal cells bearing a mutated form of the huntingtin protein, BAH stabilized HIF-1alpha protein, induced Vegf and Bnip3 gene expression and protected against mitochondrial toxin-induced cytotoxicity.	bis(5-amidino-2-benzimidazolyl)methane ketone hydrate	81-84	huntingtin	Mus musculus	61-71
34239412-2	2021	Previous investigations in cell-free and cell-based disease models showed mHTT exon-1 (mHTTex1) fragments with pathogenic polyglutamine (polyQ) tracts (>40 glutamines) to self-assemble into highly stable, beta-sheet-rich protein aggregates with a fibrillar morphology.	polyglutamine	137-142	huntingtin	Mus musculus	74-78
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	119-132	huntingtin	Mus musculus	16-26
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	119-132	huntingtin	Mus musculus	28-31
34151850-1	2021	BACKGROUND: Huntington"s disease is a neurodegenerative disorder caused by a CAG expansion in the huntingtin gene, resulting in a polyglutamine expansion in the ubiquitously expressed mutant huntingtin protein.	polyglutamine	130-143	huntingtin	Mus musculus	98-108
34151850-1	2021	BACKGROUND: Huntington"s disease is a neurodegenerative disorder caused by a CAG expansion in the huntingtin gene, resulting in a polyglutamine expansion in the ubiquitously expressed mutant huntingtin protein.	polyglutamine	130-143	huntingtin	Mus musculus	191-201
34151850-3	2021	METHODS: Full-length huntingtin with 20 and 140 polyQ repeats were formaldehyde-crosslinked and isolated via their N-terminal Flag-tag from 2-month-old mice brain cortex.	polyglutamine	48-53	huntingtin	Mus musculus	21-31
34151850-3	2021	METHODS: Full-length huntingtin with 20 and 140 polyQ repeats were formaldehyde-crosslinked and isolated via their N-terminal Flag-tag from 2-month-old mice brain cortex.	Formaldehyde	67-79	huntingtin	Mus musculus	21-31
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	119-132	huntingtin	Mus musculus	63-73
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	119-132	huntingtin	Mus musculus	77-80
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	134-139	huntingtin	Mus musculus	16-26
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	134-139	huntingtin	Mus musculus	28-31
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	134-139	huntingtin	Mus musculus	63-73
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	polyglutamine	134-139	huntingtin	Mus musculus	77-80
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	16-26
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	28-31
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	63-73
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	77-80
35626712-2	2022	Huntington"s disease (HD) is just such an example of a fatal neurological disorder, where mutated genes (CAG trinucleotide expansions in the Huntingtin gene) have widespread expression, leading to the production of mutant Huntingtin (mHTT) protein.	trinucleotide	109-122	huntingtin	Mus musculus	141-151
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	Mus musculus	145-149
35626712-2	2022	Huntington"s disease (HD) is just such an example of a fatal neurological disorder, where mutated genes (CAG trinucleotide expansions in the Huntingtin gene) have widespread expression, leading to the production of mutant Huntingtin (mHTT) protein.	trinucleotide	109-122	huntingtin	Mus musculus	222-232
35626712-2	2022	Huntington"s disease (HD) is just such an example of a fatal neurological disorder, where mutated genes (CAG trinucleotide expansions in the Huntingtin gene) have widespread expression, leading to the production of mutant Huntingtin (mHTT) protein.	trinucleotide	109-122	huntingtin	Mus musculus	234-238
35129568-1	2022	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder that occurs with the increase of CAG trinucleotide repeats in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	111-114	huntingtin	Mus musculus	144-154
35628260-1	2022	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin protein.	polyglutamine	76-89	huntingtin	Mus musculus	107-117
35129568-1	2022	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder that occurs with the increase of CAG trinucleotide repeats in the huntingtin gene.	trinucleotide	115-128	huntingtin	Mus musculus	144-154
35143966-1	2022	Huntington disease (HD) is a neurodegenerative disease caused by a trinucleotide repeat expansion in the HTT gene encoding an elongated polyglutamine tract in the huntingtin (HTT) protein.	trinucleotide	67-80	huntingtin	Mus musculus	105-108
35143966-1	2022	Huntington disease (HD) is a neurodegenerative disease caused by a trinucleotide repeat expansion in the HTT gene encoding an elongated polyglutamine tract in the huntingtin (HTT) protein.	trinucleotide	67-80	huntingtin	Mus musculus	163-173
35143966-1	2022	Huntington disease (HD) is a neurodegenerative disease caused by a trinucleotide repeat expansion in the HTT gene encoding an elongated polyglutamine tract in the huntingtin (HTT) protein.	trinucleotide	67-80	huntingtin	Mus musculus	175-178
35143966-10	2022	We demonstrate that targeted lowering of mHTT selectively in the striatum using an antisense oligonucleotide leads to a significant reduction of mHTT in the CSF of HD mice.	Oligonucleotides	93-108	huntingtin	Mus musculus	41-45
35143966-10	2022	We demonstrate that targeted lowering of mHTT selectively in the striatum using an antisense oligonucleotide leads to a significant reduction of mHTT in the CSF of HD mice.	Oligonucleotides	93-108	huntingtin	Mus musculus	145-149
35262396-1	2022	Huntington"s disease (HD) is a neurodegenerative disorder caused by a trinucleotide expansion in the HTT gene, which is expressed throughout the brain and body, including the gut epithelium and enteric nervous system.	trinucleotide	70-83	huntingtin	Mus musculus	101-104
35148841-3	2022	Here, we define HTT protein-protein interactions (PPIs) perturbed by the mutant protein with expanded polyglutamine in the mouse striatum, a brain region with selective HD vulnerability.	polyglutamine	102-115	huntingtin	Mus musculus	16-19
35148841-4	2022	Using metabolically labeled tissues and immunoaffinity purification-mass spectrometry, we establish that polyglutamine-dependent modulation of HTT PPI abundances and relative stability starts at an early stage of pathogenesis in a Q140 HD mouse model.	polyglutamine	105-118	huntingtin	Mus musculus	143-146
35083661-10	2022	Furthermore, huntingtin protein appeared as an upstream regulator for the changes observed at the fully symptomatic stage, suggesting impacts on kinases and phosphatases that extend beyond the mutated polyglutamine tract.	polyglutamine	201-214	huntingtin	Mus musculus	13-23
35305696-1	2022	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder whereby mutated huntingtin protein (mHTT) aggregates when polyglutamine repeats in the N-terminal of mHTT exceeds 36 glutamines (Q).	polyglutamine	128-141	huntingtin	Mus musculus	86-96
35305696-1	2022	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder whereby mutated huntingtin protein (mHTT) aggregates when polyglutamine repeats in the N-terminal of mHTT exceeds 36 glutamines (Q).	Glutamine	187-197	huntingtin	Mus musculus	86-96
35185467-8	2022	However, CTEP reduced the number of huntingtin aggregates, improved neuronal survival and decreased microglia activation in the striatum of both male and female zQ175 mice.	2-chloro-4-((2,5-dimethyl-1-(4-(trifluoromethoxy)phenyl)-1H-imidazol-4-yl)ethynyl)pyridine	9-13	huntingtin	Mus musculus	36-46
35165396-7	2022	Pharmacologically augmenting Bdnf transport by chronic lithium administration, partly via phosphorylation of Huntingtin (Htt) serine-421 and its integration into the motor machinery, restored striatal Bdnf levels and rescued PPI deficits in Disc1-LI mice.	Lithium	55-62	huntingtin	Mus musculus	109-119
35165396-7	2022	Pharmacologically augmenting Bdnf transport by chronic lithium administration, partly via phosphorylation of Huntingtin (Htt) serine-421 and its integration into the motor machinery, restored striatal Bdnf levels and rescued PPI deficits in Disc1-LI mice.	Lithium	55-62	huntingtin	Mus musculus	121-124
35165396-7	2022	Pharmacologically augmenting Bdnf transport by chronic lithium administration, partly via phosphorylation of Huntingtin (Htt) serine-421 and its integration into the motor machinery, restored striatal Bdnf levels and rescued PPI deficits in Disc1-LI mice.	Serine	126-132	huntingtin	Mus musculus	109-119
35165396-7	2022	Pharmacologically augmenting Bdnf transport by chronic lithium administration, partly via phosphorylation of Huntingtin (Htt) serine-421 and its integration into the motor machinery, restored striatal Bdnf levels and rescued PPI deficits in Disc1-LI mice.	Serine	126-132	huntingtin	Mus musculus	121-124
35246273-4	2022	Although the sequence with expanded polyglutamine could not be identified by liquid-chromatography mass spectrometry, amino acid analysis revealed that glutamine of the huntingtin inclusion-rich fraction increased significantly.	Glutamine	152-161	huntingtin	Mus musculus	169-179
35219323-2	2022	When the number of CAG repeats exceeds 36, the translated expanded polyglutamine-containing HTT protein (mutant HTT (mHTT)) interferes with the normal functions of many cellular proteins and subsequently jeopardizes important cellular machineries in major types of brain cells, including neurons, astrocytes, and microglia.	polyglutamine	67-80	huntingtin	Mus musculus	92-95
35219323-2	2022	When the number of CAG repeats exceeds 36, the translated expanded polyglutamine-containing HTT protein (mutant HTT (mHTT)) interferes with the normal functions of many cellular proteins and subsequently jeopardizes important cellular machineries in major types of brain cells, including neurons, astrocytes, and microglia.	polyglutamine	67-80	huntingtin	Mus musculus	112-115
35219323-2	2022	When the number of CAG repeats exceeds 36, the translated expanded polyglutamine-containing HTT protein (mutant HTT (mHTT)) interferes with the normal functions of many cellular proteins and subsequently jeopardizes important cellular machineries in major types of brain cells, including neurons, astrocytes, and microglia.	polyglutamine	67-80	huntingtin	Mus musculus	117-121
34974533-4	2022	We show that the poly-glutamine (polyQ) tract encoded by CAGs in the huntingtin protein (HTT) is under purifying selection and subjected to stronger selective pressures than CAG-encoded polyQ tracts in other proteins.	polyglutamine	17-31	huntingtin	Mus musculus	69-79
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	Mus musculus	188-192
35108063-4	2022	This small molecule radiolabeled with 11C ((11C)CHDI-180R) allowed noninvasive monitoring of mHTT pathology in the brain and could track region- and time-dependent suppression of mHTT in response to therapeutic interventions targeting mHTT expression in a rodent model.	Carbon-11	38-41	huntingtin	Mus musculus	93-97
35108063-4	2022	This small molecule radiolabeled with 11C ((11C)CHDI-180R) allowed noninvasive monitoring of mHTT pathology in the brain and could track region- and time-dependent suppression of mHTT in response to therapeutic interventions targeting mHTT expression in a rodent model.	Carbon-11	38-41	huntingtin	Mus musculus	179-183
35108063-4	2022	This small molecule radiolabeled with 11C ((11C)CHDI-180R) allowed noninvasive monitoring of mHTT pathology in the brain and could track region- and time-dependent suppression of mHTT in response to therapeutic interventions targeting mHTT expression in a rodent model.	Carbon-11	38-41	huntingtin	Mus musculus	235-239
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	Mus musculus	188-192
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	Mus musculus	188-192
34974533-4	2022	We show that the poly-glutamine (polyQ) tract encoded by CAGs in the huntingtin protein (HTT) is under purifying selection and subjected to stronger selective pressures than CAG-encoded polyQ tracts in other proteins.	polyglutamine	17-31	huntingtin	Mus musculus	89-92
34974533-4	2022	We show that the poly-glutamine (polyQ) tract encoded by CAGs in the huntingtin protein (HTT) is under purifying selection and subjected to stronger selective pressures than CAG-encoded polyQ tracts in other proteins.	polyglutamine	33-38	huntingtin	Mus musculus	69-79
34974533-4	2022	We show that the poly-glutamine (polyQ) tract encoded by CAGs in the huntingtin protein (HTT) is under purifying selection and subjected to stronger selective pressures than CAG-encoded polyQ tracts in other proteins.	polyglutamine	33-38	huntingtin	Mus musculus	89-92
34974533-6	2022	By combining genome-edited mouse embryonic stem cells and cell assays, we show that small variations in HTT polyQ lengths significantly correlate with cells" neurogenic potential and with changes in the gene transcription network governing neuronal function.	polyglutamine	108-113	huntingtin	Mus musculus	104-107
33492644-1	2021	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an expansion of polyglutamine stretch (polyQ) at the N-terminus of huntingtin (Htt) protein.	polyglutamine	96-109	huntingtin	Mus musculus	147-157
34376056-1	2022	Huntington"s disease (HD) is a devasting, autosomal dominant neurodegenerative disease caused by a trinucleotide repeat expansion in the HTT gene.	trinucleotide	99-112	huntingtin	Mus musculus	137-140
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	cytosine-adenine-guanine	143-167	huntingtin	Mus musculus	98-108
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	cytosine-adenine-guanine	143-167	huntingtin	Mus musculus	115-118
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	cytosine-adenine-guanine	143-167	huntingtin	Mus musculus	233-243
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	169-172	huntingtin	Mus musculus	98-108
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	169-172	huntingtin	Mus musculus	115-118
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	169-172	huntingtin	Mus musculus	233-243
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	trinucleotide	174-187	huntingtin	Mus musculus	98-108
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	trinucleotide	174-187	huntingtin	Mus musculus	115-118
34806402-1	2022	Huntington"s Disease is a fatal neurodegenerative disorder caused by an inherited mutation in the huntingtin gene (HTT) comprising an expanded cytosine-adenine-guanine (CAG) trinucleotide repeat sequence that results in a pathogenic huntingtin protein.	trinucleotide	174-187	huntingtin	Mus musculus	233-243
34806402-9	2022	The optimized pri-amiRNA was selected with this focus on efficiency and precision of pri-amiRNA processing in addition to its pharmacological activity on HTT lowering, and general tolerability in vivo.	pri-amirna	14-24	huntingtin	Mus musculus	154-157
33684424-1	2021	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by an abnormal CAG repeat expansion in the huntingtin gene coding for a protein with an elongated polyglutamine sequence.	polyglutamine	174-187	huntingtin	Mus musculus	119-129
33492644-1	2021	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an expansion of polyglutamine stretch (polyQ) at the N-terminus of huntingtin (Htt) protein.	polyglutamine	96-109	huntingtin	Mus musculus	159-162
33492644-2	2021	The abnormally expanded polyQ stretch of mutant Htt makes it prone to aggregate, leading to neuropathology.	polyglutamine	24-29	huntingtin	Mus musculus	48-51
33492644-9	2021	Importantly, inhibition of p38 MAPK pathway by PD169316 increased chymotrypsin-like activity and reduced accumulation of aggregated and soluble forms of mutant Htt in HAP40-depleted cells to alleviate HAP40-depletion induced cytotoxicity.	2-(4-nitrophenyl)-4-(4-fluorophenyl)-5-(4-pyridinyl)-1H-imidazole	47-55	huntingtin	Mus musculus	160-163
34043007-9	2021	CRISPR/Cas9-mediated nonallele-specific HTT silencing in striatal neurons restored altered CBVa in premanifest zQ175 mice, delayed onset of striatal atrophy, and slowed the progression of motor phenotype and brain pathology.	cbva	91-95	huntingtin	Mus musculus	40-43
33516737-3	2021	We previously described the 23aa Htt fragment P42, that attenuated the pathological phenotypes induced by mHtt.	mhtt	106-110	huntingtin	Mus musculus	33-36
33920936-1	2021	Huntington"s disease (HD) is a rare hereditary autosomal dominant neurodegenerative disorder, which is caused by expression of mutant huntingtin protein (mHTT) with an abnormal number of glutamine repeats in its N terminus, and characterized by intracellular mHTT aggregates (inclusions) in the brain.	Glutamine	187-196	huntingtin	Mus musculus	154-158
32941796-2	2021	The impact of phosphorylating serine 13/16 of mutant HTT (mHTT) on HD has been documented in cell culture and murine models.	Serine	30-36	huntingtin	Mus musculus	53-56
32941796-2	2021	The impact of phosphorylating serine 13/16 of mutant HTT (mHTT) on HD has been documented in cell culture and murine models.	Serine	30-36	huntingtin	Mus musculus	58-62
32941796-6	2021	Phosphomimetic mHTT aggravates and the phosphoresistant mutation ameliorates mHTT-induced toxicity in the context of both FL- and exon1- mHTT in Drosophila although in all cases FL appears less toxic than exon1.	fl	122-124	huntingtin	Mus musculus	77-81
32941796-6	2021	Phosphomimetic mHTT aggravates and the phosphoresistant mutation ameliorates mHTT-induced toxicity in the context of both FL- and exon1- mHTT in Drosophila although in all cases FL appears less toxic than exon1.	fl	122-124	huntingtin	Mus musculus	77-81
33636386-5	2021	Oral administration of GTB significantly reduced mutant huntingtin level in striatum, motor cortex as well as hippocampus and increased the integrity of viable neurons.	s-(p-nitrobenzyl)glutathione	23-26	huntingtin	Mus musculus	56-66
33636386-7	2021	Accordingly, NaB administration also markedly decreased huntingtin level in striatum and cortex.	nab	13-16	huntingtin	Mus musculus	56-66
34011527-1	2021	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a trinucleotide expansion in exon 1 of the huntingtin (HTT) gene.	trinucleotide	91-104	huntingtin	Mus musculus	132-142
34011527-1	2021	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a trinucleotide expansion in exon 1 of the huntingtin (HTT) gene.	trinucleotide	91-104	huntingtin	Mus musculus	144-147
33904021-2	2021	In HD, N-terminal portion of mutant huntingtin protein containing expanded polyglutamine repeats accumulates as inclusion bodies and leads to progressive deterioration of various cellular functioning including proteostasis network.	polyglutamine	75-88	huntingtin	Mus musculus	36-46
33904021-4	2021	Exposure of Withaferin A activates HSF1 and induces the expression of HSP70 chaperones in an in vitro cell culture system and also suppresses mutant huntingtin aggregation in a cellular model of HD.	withaferin A	12-24	huntingtin	Mus musculus	149-159
33904021-6	2021	Biochemical studies confirmed the activation of HSR and global decrease in mutant huntingtin aggregates load accompanied with improvement of striatal function in Withaferin A-treated HD mouse brain.	withaferin A	162-174	huntingtin	Mus musculus	82-92
33710799-1	2021	Huntington"s disease (HD) is a fatal autosomal-dominant neurodegenerative disease caused by a trinucleotide CAG repeat expansion of the huntingtin gene (HTT) that affects 1 in every 10 000 individuals in the United States.	trinucleotide	94-107	huntingtin	Mus musculus	136-146
33710799-1	2021	Huntington"s disease (HD) is a fatal autosomal-dominant neurodegenerative disease caused by a trinucleotide CAG repeat expansion of the huntingtin gene (HTT) that affects 1 in every 10 000 individuals in the United States.	trinucleotide	94-107	huntingtin	Mus musculus	153-156
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	Mus musculus	19-23
33675499-1	2021	Huntington"s disease (HD) is a neurodegenerative disorder caused by a trinucleotide repeat expansion in the huntingtin gene.	trinucleotide	70-83	huntingtin	Mus musculus	108-118
33674575-1	2021	The polyglutamine expansion of huntingtin (mHTT) causes Huntington disease (HD) and neurodegeneration, but the mechanisms remain unclear.	polyglutamine	4-17	huntingtin	Mus musculus	31-41
33674575-1	2021	The polyglutamine expansion of huntingtin (mHTT) causes Huntington disease (HD) and neurodegeneration, but the mechanisms remain unclear.	polyglutamine	4-17	huntingtin	Mus musculus	43-47
33517535-2	2021	Whether the pathogenic trinucleotide repeat expansion of the HTT gene causes neurodevelopmental abnormalities has garnered attention in both murine and human studies; however, documentation of discrete malformations in autopsy brains of HD individuals has yet to be described.	trinucleotide	23-36	huntingtin	Mus musculus	61-64
33310753-1	2021	Huntington disease (HD) is a neurodegenerative disease caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene.	trinucleotide	71-84	huntingtin	Mus musculus	109-119
33310753-1	2021	Huntington disease (HD) is a neurodegenerative disease caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene.	trinucleotide	71-84	huntingtin	Mus musculus	121-124
33310753-5	2021	We have also shown that lowering HTT in the brains of HD mice results in correlative reduction of mHTT in the CSF, prompting the use of this measure as an exploratory marker of target engagement in clinical trials.	mhtt	98-102	huntingtin	Mus musculus	33-36
33310753-10	2021	Overall, our data supports both passive release and active clearance of mHTT into CSF, suggesting that its treatment-induced changes may represent a combination of target engagement and preservation of neurons.SIGNIFICANCE STATEMENTChanges in cerebrospinal fluid (CSF) mutant huntingtin (mHTT) are being used as an exploratory endpoint in HTT lowering clinical trials for the treatment of Huntington disease (HD).	mhtt	72-76	huntingtin	Mus musculus	276-286
33239172-1	2021	Huntington"s disease (HD) is caused by a mutant huntingtin (mHtt) protein that contains abnormally extended polyglutamine (polyQ) repeats.	polyglutamine	108-121	huntingtin	Mus musculus	48-58
33239172-1	2021	Huntington"s disease (HD) is caused by a mutant huntingtin (mHtt) protein that contains abnormally extended polyglutamine (polyQ) repeats.	polyglutamine	123-128	huntingtin	Mus musculus	48-58
33579860-3	2021	In the case of HD, the expanded repeat unit is a CAG trinucleotide located in exon 1 of the huntingtin (HTT) gene, resulting in an expanded polyglutamine tract in the huntingtin protein.	trinucleotide	53-66	huntingtin	Mus musculus	92-102
33579860-3	2021	In the case of HD, the expanded repeat unit is a CAG trinucleotide located in exon 1 of the huntingtin (HTT) gene, resulting in an expanded polyglutamine tract in the huntingtin protein.	trinucleotide	53-66	huntingtin	Mus musculus	104-107
33579860-3	2021	In the case of HD, the expanded repeat unit is a CAG trinucleotide located in exon 1 of the huntingtin (HTT) gene, resulting in an expanded polyglutamine tract in the huntingtin protein.	trinucleotide	53-66	huntingtin	Mus musculus	167-177
33579860-3	2021	In the case of HD, the expanded repeat unit is a CAG trinucleotide located in exon 1 of the huntingtin (HTT) gene, resulting in an expanded polyglutamine tract in the huntingtin protein.	polyglutamine	140-153	huntingtin	Mus musculus	92-102
33579860-3	2021	In the case of HD, the expanded repeat unit is a CAG trinucleotide located in exon 1 of the huntingtin (HTT) gene, resulting in an expanded polyglutamine tract in the huntingtin protein.	polyglutamine	140-153	huntingtin	Mus musculus	104-107
33579860-3	2021	In the case of HD, the expanded repeat unit is a CAG trinucleotide located in exon 1 of the huntingtin (HTT) gene, resulting in an expanded polyglutamine tract in the huntingtin protein.	polyglutamine	140-153	huntingtin	Mus musculus	167-177
33335120-1	2020	Huntington"s disease (HD) is a monogenetic neurodegenerative disorder that is caused by the expansion of a polyglutamine region within the huntingtin (HTT) protein, but there is still an incomplete understanding of the molecular mechanisms that drive pathology.	polyglutamine	107-120	huntingtin	Mus musculus	139-149
32754987-1	2021	Huntington"s disease (HD) is a neurodegenerative disorder caused by a glutamine expansion at the first exon of the huntingtin gene.	Glutamine	70-79	huntingtin	Mus musculus	115-125
33335120-1	2020	Huntington"s disease (HD) is a monogenetic neurodegenerative disorder that is caused by the expansion of a polyglutamine region within the huntingtin (HTT) protein, but there is still an incomplete understanding of the molecular mechanisms that drive pathology.	polyglutamine	107-120	huntingtin	Mus musculus	151-154
32702387-1	2020	Huntington"s disease (HD) is an incurable neurodegenerative disorder caused by a trinucleotide (CAG) repeat expansion in the huntingtin gene (HTT).	trinucleotide	81-94	huntingtin	Mus musculus	125-135
32959531-7	2020	The treatment also enhanced endogenous cholesterol biosynthesis and clearance of mutant Huntingtin aggregates.	Cholesterol	39-50	huntingtin	Mus musculus	88-98
32865873-1	2020	OBJECTIVES: Huntington"s disease (HD) is a devastating neurodegenerative disease caused by polyglutamine (polyQ) expansion in the huntingtin (HTT) gene.	polyglutamine	91-104	huntingtin	Mus musculus	130-140
32865873-1	2020	OBJECTIVES: Huntington"s disease (HD) is a devastating neurodegenerative disease caused by polyglutamine (polyQ) expansion in the huntingtin (HTT) gene.	polyglutamine	91-104	huntingtin	Mus musculus	142-145
32865873-1	2020	OBJECTIVES: Huntington"s disease (HD) is a devastating neurodegenerative disease caused by polyglutamine (polyQ) expansion in the huntingtin (HTT) gene.	polyglutamine	106-111	huntingtin	Mus musculus	130-140
32865873-1	2020	OBJECTIVES: Huntington"s disease (HD) is a devastating neurodegenerative disease caused by polyglutamine (polyQ) expansion in the huntingtin (HTT) gene.	polyglutamine	106-111	huntingtin	Mus musculus	142-145
32622701-1	2020	Huntington disease (HD) is an autosomal dominant neurodegenerative disorder caused by an expansion of a polyglutamine repeat in the huntingtin (HTT) protein.	polyglutamine	104-117	huntingtin	Mus musculus	132-142
32622701-1	2020	Huntington disease (HD) is an autosomal dominant neurodegenerative disorder caused by an expansion of a polyglutamine repeat in the huntingtin (HTT) protein.	polyglutamine	104-117	huntingtin	Mus musculus	144-147
32702387-1	2020	Huntington"s disease (HD) is an incurable neurodegenerative disorder caused by a trinucleotide (CAG) repeat expansion in the huntingtin gene (HTT).	trinucleotide	81-94	huntingtin	Mus musculus	142-145
32702387-1	2020	Huntington"s disease (HD) is an incurable neurodegenerative disorder caused by a trinucleotide (CAG) repeat expansion in the huntingtin gene (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	96-99	huntingtin	Mus musculus	125-135
32702387-1	2020	Huntington"s disease (HD) is an incurable neurodegenerative disorder caused by a trinucleotide (CAG) repeat expansion in the huntingtin gene (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	96-99	huntingtin	Mus musculus	142-145
32978366-2	2020	Phosphorylation at serine-421 (pS421) of mHTT has been shown to be neuroprotective in cellular and rodent models.	Serine	19-25	huntingtin	Mus musculus	41-45
32574176-1	2020	In the BACHD mouse model of Huntington"s disease (HD), deletion of the N17 domain of the Huntingtin gene (BACHDDeltaN17, Q97) has been reported to lead to nuclear accumulation of mHTT and exacerbation of motor deficits, neuroinflammation and striatal atrophy (Gu et al., 2015).	mhtt	179-183	huntingtin	Mus musculus	89-99
32968182-8	2020	Our results show that stabilizing polyol osmolytes promote mHtt aggregation, alleviate CREB dysfunction, and promote survival under stress to support the hypothesis that lower molecular weight entities of disease protein are relevant pathogenic species in neurodegeneration.	polyol	34-40	huntingtin	Mus musculus	59-63
32933349-7	2022	We noted that HTT null cardiomyocytes showed diminished intracellular ATP (4.9 +- 0.5; 6.7 +- 0.4 nmol/mg protein HTT KO vs. SCR) and NAD+ (0.9 +- 0.1; 1.6 +- 0.1 nmol/mg HTT KO vs. SCR).	Adenosine Triphosphate	70-73	huntingtin	Mus musculus	14-17
32933349-7	2022	We noted that HTT null cardiomyocytes showed diminished intracellular ATP (4.9 +- 0.5; 6.7 +- 0.4 nmol/mg protein HTT KO vs. SCR) and NAD+ (0.9 +- 0.1; 1.6 +- 0.1 nmol/mg HTT KO vs. SCR).	NAD	134-138	huntingtin	Mus musculus	14-17
32933349-8	2022	We noted also reduced cellular medium concentration of total purines pool (17.1 +- 1.7; 24.7 +- 2.7 nmol/ml HTT KO vs. SCR) as well as IMP concentration (7.7 +- 0.6; 10.2 +- 0.4 nmol/ml HTT KO vs. SCR).	Purines	61-68	huntingtin	Mus musculus	108-111
32387649-1	2020	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine expansion in the widely expressed huntingtin protein.	polyglutamine	90-103	huntingtin	Mus musculus	138-148
32640230-0	2020	Chronic Corticosterone Elevation Suppresses Adult Hippocampal Neurogenesis by Hyperphosphorylating Huntingtin.	Corticosterone	8-22	huntingtin	Mus musculus	99-109
32533168-2	2020	Huntington"s disease is caused by a polyglutamine-encoding CAG repeat expansion in the Huntingtin (HTT) gene leading to several toxic interactions of both the expanded CAG-containing mRNA and the polyglutamine-containing protein, while X-linked dystonia parkinsonism is caused by a retrotransposon insertion in the TAF1 gene, which decreases expression of this core scaffold of the basal transcription factor complex TFIID.	polyglutamine	36-49	huntingtin	Mus musculus	87-97
32533168-2	2020	Huntington"s disease is caused by a polyglutamine-encoding CAG repeat expansion in the Huntingtin (HTT) gene leading to several toxic interactions of both the expanded CAG-containing mRNA and the polyglutamine-containing protein, while X-linked dystonia parkinsonism is caused by a retrotransposon insertion in the TAF1 gene, which decreases expression of this core scaffold of the basal transcription factor complex TFIID.	polyglutamine	36-49	huntingtin	Mus musculus	99-102
32439598-5	2020	Moreover, SDS-soluble total HTT (WT plus mutant HTT) and pThr3 HTT were reduced with increasing CAG repeat length, and there was no pSer421 mutant HTT detected in any HD mice.	Sodium Dodecyl Sulfate	10-13	huntingtin	Mus musculus	28-31
32439598-5	2020	Moreover, SDS-soluble total HTT (WT plus mutant HTT) and pThr3 HTT were reduced with increasing CAG repeat length, and there was no pSer421 mutant HTT detected in any HD mice.	Sodium Dodecyl Sulfate	10-13	huntingtin	Mus musculus	48-51
32439598-5	2020	Moreover, SDS-soluble total HTT (WT plus mutant HTT) and pThr3 HTT were reduced with increasing CAG repeat length, and there was no pSer421 mutant HTT detected in any HD mice.	Sodium Dodecyl Sulfate	10-13	huntingtin	Mus musculus	48-51
32439598-8	2020	SDS-insoluble mutant HTT was detected in HD striatal synaptosomes consistent with the presence of aggregates.	Sodium Dodecyl Sulfate	0-3	huntingtin	Mus musculus	21-24
32675242-5	2020	We identified two lysine residues, 6 and 9, in the first exon of mHtt that are specifically ubiquitinated in striatal and cortical brain tissues of mHtt-transgenic animals.	Lysine	18-24	huntingtin	Mus musculus	65-69
32675242-5	2020	We identified two lysine residues, 6 and 9, in the first exon of mHtt that are specifically ubiquitinated in striatal and cortical brain tissues of mHtt-transgenic animals.	Lysine	18-24	huntingtin	Mus musculus	148-152
32640230-3	2020	Using a cortico-hippocampal network-on-a-chip, we find that the glucocorticoid receptor agonist dexamethasone (DXM) stimulates the cyclin-dependent kinase 5 (CDK5) to phosphorylate huntingtin (HTT) at serines 1181 and 1201 (S1181/1201), which retards BDNF vesicular transport in cortical axons.	Dexamethasone	96-109	huntingtin	Mus musculus	181-191
32640230-3	2020	Using a cortico-hippocampal network-on-a-chip, we find that the glucocorticoid receptor agonist dexamethasone (DXM) stimulates the cyclin-dependent kinase 5 (CDK5) to phosphorylate huntingtin (HTT) at serines 1181 and 1201 (S1181/1201), which retards BDNF vesicular transport in cortical axons.	Dexamethasone	96-109	huntingtin	Mus musculus	193-196
32640230-3	2020	Using a cortico-hippocampal network-on-a-chip, we find that the glucocorticoid receptor agonist dexamethasone (DXM) stimulates the cyclin-dependent kinase 5 (CDK5) to phosphorylate huntingtin (HTT) at serines 1181 and 1201 (S1181/1201), which retards BDNF vesicular transport in cortical axons.	Dexamethasone	111-114	huntingtin	Mus musculus	181-191
32640230-3	2020	Using a cortico-hippocampal network-on-a-chip, we find that the glucocorticoid receptor agonist dexamethasone (DXM) stimulates the cyclin-dependent kinase 5 (CDK5) to phosphorylate huntingtin (HTT) at serines 1181 and 1201 (S1181/1201), which retards BDNF vesicular transport in cortical axons.	Dexamethasone	111-114	huntingtin	Mus musculus	193-196
32514103-6	2021	The presence of mHTT in the brain was accompanied by vascular abnormalities, such as a reduction of Collagen IV signal intensity and altered vessel diameter in the striatum, and changes in expression of Glutamic acid decarboxylase 65/67 (GAD65-67) in the cortex.	Glutamic Acid	203-216	huntingtin	Mus musculus	16-20
32242231-8	2020	Phosphorylation defective mutation of Serine at amino acid 120 (S120) abolishes the mHTT-lowering effect of NLK, suggesting that S120 phosphorylation is an important step in the NLK-mediated lowering of mHTT.	Serine	38-44	huntingtin	Mus musculus	84-88
32242231-8	2020	Phosphorylation defective mutation of Serine at amino acid 120 (S120) abolishes the mHTT-lowering effect of NLK, suggesting that S120 phosphorylation is an important step in the NLK-mediated lowering of mHTT.	Serine	38-44	huntingtin	Mus musculus	203-207
32547392-7	2020	Our results showed that 6-ohda increased mHTT expression and reduced HTT phosphorylation at Ser421, a post-translational modification, which protects against mHTT accumulation.	Oxidopamine	24-30	huntingtin	Mus musculus	41-45
32547392-7	2020	Our results showed that 6-ohda increased mHTT expression and reduced HTT phosphorylation at Ser421, a post-translational modification, which protects against mHTT accumulation.	Oxidopamine	24-30	huntingtin	Mus musculus	42-45
32547392-7	2020	Our results showed that 6-ohda increased mHTT expression and reduced HTT phosphorylation at Ser421, a post-translational modification, which protects against mHTT accumulation.	Oxidopamine	24-30	huntingtin	Mus musculus	158-162
32448329-1	2020	Huntington"s disease (HD) is an incurable neurodegenerative disorder caused by CAG trinucleotide expansions in the huntingtin gene.	trinucleotide	83-96	huntingtin	Mus musculus	115-125
32341997-5	2020	First, through the enrichment of deuterated glutamine in the polyQ sequence of mutant Huntingtin (mHtt) exon1 proteins for Huntington"s disease, we achieved sensitive and specific stimulated Raman scattering (SRS) imaging of carbon-deuterium bonds (C-D) from aggregates without GFP labeling, which is commonly employed in fluorescence microscopy.	deuterated	33-43	huntingtin	Mus musculus	98-102
32341997-5	2020	First, through the enrichment of deuterated glutamine in the polyQ sequence of mutant Huntingtin (mHtt) exon1 proteins for Huntington"s disease, we achieved sensitive and specific stimulated Raman scattering (SRS) imaging of carbon-deuterium bonds (C-D) from aggregates without GFP labeling, which is commonly employed in fluorescence microscopy.	Glutamine	44-53	huntingtin	Mus musculus	98-102
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	Mus musculus	98-102
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	Mus musculus	98-102
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	Mus musculus	98-102
31599037-1	2019	Huntington"s disease (HD) is an inherited neurodegenerative disease caused by a polyglutamine repeat expansion in the huntingtin protein.	polyglutamine	80-93	huntingtin	Mus musculus	118-128
32029588-3	2020	Via CRISPR/Cas9-mediated genome editing, we established knock-in mouse models that harbor expanded CAG repeats in the mouse huntingtin gene to express RAN-translated products with or without polyglutamine peptides.	polyglutamine peptides	191-213	huntingtin	Mus musculus	124-134
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	Mus musculus	145-149
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	Mus musculus	145-149
30194046-1	2020	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a trinucleotide repeat expansion in the huntingtin (HTT) gene, which is expressed ubiquitously throughout the brain and peripheral tissues.	trinucleotide	82-95	huntingtin	Mus musculus	120-130
30194046-1	2020	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a trinucleotide repeat expansion in the huntingtin (HTT) gene, which is expressed ubiquitously throughout the brain and peripheral tissues.	trinucleotide	82-95	huntingtin	Mus musculus	132-135
31648394-2	2020	Suppressing HTT production with antisense oligonucleotides (ASOs) is a promising treatment strategy for HD; however, the difficulty of delivering ASOs to deep brain structures is a major barrier for its clinical application.	Oligonucleotides	42-58	huntingtin	Mus musculus	12-15
31648394-2	2020	Suppressing HTT production with antisense oligonucleotides (ASOs) is a promising treatment strategy for HD; however, the difficulty of delivering ASOs to deep brain structures is a major barrier for its clinical application.	Oligonucleotides, Antisense	60-64	huntingtin	Mus musculus	12-15
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	Mus musculus	184-188
31778667-1	2020	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by polyglutamine (CAG) expansion in the Huntingtin (HTT) gene.	polyglutamine	100-113	huntingtin	Mus musculus	137-147
31778667-1	2020	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by polyglutamine (CAG) expansion in the Huntingtin (HTT) gene.	polyglutamine	100-113	huntingtin	Mus musculus	149-152
31778667-1	2020	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by polyglutamine (CAG) expansion in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	115-118	huntingtin	Mus musculus	137-147
31778667-1	2020	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by polyglutamine (CAG) expansion in the Huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	115-118	huntingtin	Mus musculus	149-152
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	Mus musculus	171-175
31695068-1	2019	Huntington"s disease (HD) is a fatal inherited autosomal dominant neurodegenerative disorder caused by an expansion in the number of CAG trinucleotide repeats in the huntingtin gene.	trinucleotide	137-150	huntingtin	Mus musculus	166-176
31381945-0	2019	Somatostatin and cannabinoid receptors crosstalk in protection of huntingtin knock-in striatal neuronal cells in response to quinolinic acid.	Quinolinic Acid	125-140	huntingtin	Mus musculus	66-76
32317916-1	2020	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by a polyglutamine expansion in the huntingtin protein, Striatum atrophy in HD leads to a progressive disturbance of psychiatric, motor, and cognitive function.	polyglutamine	80-93	huntingtin	Mus musculus	111-121
32043503-0	2020	Ellagic acid rescues motor and cognitive deficits in the R6/2 mouse model of Huntington"s disease by lowering mutant huntingtin protein.	Ellagic Acid	0-12	huntingtin	Mus musculus	117-127
32043503-1	2020	Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by a highly polymorphic CAG trinucleotide repeat expansion encoding an extended polyglutamine (polyQ) tract at the N-terminus of huntingtin protein (HTT).	polyglutamine	153-166	huntingtin	Mus musculus	202-212
32043503-1	2020	Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by a highly polymorphic CAG trinucleotide repeat expansion encoding an extended polyglutamine (polyQ) tract at the N-terminus of huntingtin protein (HTT).	polyglutamine	153-166	huntingtin	Mus musculus	222-225
32043503-1	2020	Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by a highly polymorphic CAG trinucleotide repeat expansion encoding an extended polyglutamine (polyQ) tract at the N-terminus of huntingtin protein (HTT).	polyglutamine	168-173	huntingtin	Mus musculus	202-212
32043503-1	2020	Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by a highly polymorphic CAG trinucleotide repeat expansion encoding an extended polyglutamine (polyQ) tract at the N-terminus of huntingtin protein (HTT).	polyglutamine	168-173	huntingtin	Mus musculus	222-225
32043503-1	2020	Huntington"s disease (HD) is a genetic neurodegenerative disorder caused by a highly polymorphic CAG trinucleotide repeat expansion encoding an extended polyglutamine (polyQ) tract at the N-terminus of huntingtin protein (HTT).	Nitrogen	188-189	huntingtin	Mus musculus	202-212
32043503-2	2020	The polyQ tract promotes the formation of toxic oligomers and aggregates of HTT, which leads to neuronal dysfunction and death.	polyglutamine	4-9	huntingtin	Mus musculus	76-79
31913581-4	2020	Here, we demonstrate that promoting HTT phosphorylation at Ser421, either by a phospho-mimetic mutation or inhibition of the phosphatase calcineurin, restores endogenous BDNF axonal transport in vitro in the corticostriatal pathway, increases striatal BDNF availability and synaptic connectivity in vivo, and improves the phenotype and the survival of Mecp2 knockout mice-even though treatments were initiated only after the mice had already developed symptoms.	seryl-seryl-seryl-arginine	59-62	huntingtin	Mus musculus	36-39
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	Mus musculus	137-141
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	Mus musculus	137-141
31757420-5	2020	These results signify the sporadic behavior of the polyQ inclusion that gives insight into the mechanism of protein dynamics as a consequence of secreted mHTT aggregates.	polyglutamine	51-56	huntingtin	Mus musculus	154-158
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	Mus musculus	184-188
31690177-4	2020	We tested this hypothesis in the scenario of Huntington disease (HD), a neurodegenerative disorder that is caused by the mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) stretch.	polyglutamine	164-177	huntingtin	Mus musculus	128-131
31690177-4	2020	We tested this hypothesis in the scenario of Huntington disease (HD), a neurodegenerative disorder that is caused by the mutant HTT (mHTT) protein with an expanded polyglutamine (polyQ) stretch.	polyglutamine	179-184	huntingtin	Mus musculus	128-131
32310183-8	2020	CONCLUSION: Mutant HTT expression impairs glutamate refill but not RRP size or replenishment in C-S synapses.	Glutamic Acid	42-51	huntingtin	Mus musculus	19-22
31282030-6	2019	While differences in the human and mouse exon 1 HTT proteins (e.g., proline rich sequences) could also contribute to the phenotypic differences, our data indicate that the incomplete splicing of HTT and approaches to lower the levels of the exon 1 HTT transcript should be pursued as therapeutic targets.	Proline	68-75	huntingtin	Mus musculus	48-51
31666698-3	2019	Mutant huntingtin protein (mHTT) contains an expanded polyglutamine (polyQ) tract and causes Huntington"s disease, an incurable neurodegenerative disorder2.	polyglutamine	54-67	huntingtin	Mus musculus	7-17
31666698-3	2019	Mutant huntingtin protein (mHTT) contains an expanded polyglutamine (polyQ) tract and causes Huntington"s disease, an incurable neurodegenerative disorder2.	polyglutamine	54-67	huntingtin	Mus musculus	27-31
31666698-3	2019	Mutant huntingtin protein (mHTT) contains an expanded polyglutamine (polyQ) tract and causes Huntington"s disease, an incurable neurodegenerative disorder2.	polyglutamine	69-74	huntingtin	Mus musculus	7-17
31666698-3	2019	Mutant huntingtin protein (mHTT) contains an expanded polyglutamine (polyQ) tract and causes Huntington"s disease, an incurable neurodegenerative disorder2.	polyglutamine	69-74	huntingtin	Mus musculus	27-31
31666698-7	2019	This study presents candidate compounds for lowering mHTT and potentially other disease-causing proteins with polyQ expansions, demonstrating the concept of lowering levels of disease-causing proteins using autophagosome-tethering compounds.	polyglutamine	110-115	huntingtin	Mus musculus	53-57
31681295-7	2019	In addition, mHTT expression in Drosophila macrophage-like S2 cells in vitro reduced ATP levels, phagocytic activity and the induction of antimicrobial peptides.	Adenosine Triphosphate	85-88	huntingtin	Mus musculus	13-17
31529216-1	2019	Huntington"s disease (HD) is an autosomal dominant disorder caused by an expansion in the trinucleotide CAG repeat in exon-1 in the huntingtin gene, located on chromosome 4.	trinucleotide	90-103	huntingtin	Mus musculus	132-142
31042572-1	2019	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disease caused by a CAG expansion, which translates into an elongated polyglutamine (polyQ) repeat near the amino-terminus of the huntingtin protein (HTT).	polyglutamine	144-157	huntingtin	Mus musculus	204-214
31488728-7	2019	Moreover, curcumin also increased the expression of the scaffolding proteins Rab7- interacting lysosomal protein (RILP) and huntingtin in N2a/APP695swe cells.	Curcumin	10-18	huntingtin	Mus musculus	124-134
31465962-1	2019	Huntington"s disease (HD) is a currently incurable and, ultimately, fatal neurodegenerative disorder caused by a CAG trinucleotide repeat expansion within exon 1 of the huntingtin (HTT) gene, which results in the production of a mutant protein that forms inclusions and selectively destroys neurons in the striatum and other adjacent structures.	trinucleotide	117-130	huntingtin	Mus musculus	169-179
31465962-1	2019	Huntington"s disease (HD) is a currently incurable and, ultimately, fatal neurodegenerative disorder caused by a CAG trinucleotide repeat expansion within exon 1 of the huntingtin (HTT) gene, which results in the production of a mutant protein that forms inclusions and selectively destroys neurons in the striatum and other adjacent structures.	trinucleotide	117-130	huntingtin	Mus musculus	181-184
31042572-1	2019	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disease caused by a CAG expansion, which translates into an elongated polyglutamine (polyQ) repeat near the amino-terminus of the huntingtin protein (HTT).	polyglutamine	144-157	huntingtin	Mus musculus	224-227
31042572-1	2019	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disease caused by a CAG expansion, which translates into an elongated polyglutamine (polyQ) repeat near the amino-terminus of the huntingtin protein (HTT).	polyglutamine	159-164	huntingtin	Mus musculus	204-214
31042572-1	2019	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disease caused by a CAG expansion, which translates into an elongated polyglutamine (polyQ) repeat near the amino-terminus of the huntingtin protein (HTT).	polyglutamine	159-164	huntingtin	Mus musculus	224-227
31108174-5	2019	Here we evaluate the neuroprotective effects of pridopidine against mutant Huntingtin toxicity in mouse and human derived in vitro cell models.	pridopidine	48-59	huntingtin	Mus musculus	75-85
31108174-7	2019	Pridopidine protects mutant Huntingtin transfected mouse primary striatal and cortical neurons, with an EC50 in the mid nanomolar range, as well as HD patient-derived induced pluripotent stem cells (iPSCs).	pridopidine	0-11	huntingtin	Mus musculus	28-38
31040226-1	2019	Huntington"s disease (HD) is a monogenic disorder, driven by the expansion of a trinucleotide (CAG) repeat within the huntingtin (Htt) gene and culminating in neuronal degeneration in the brain, predominantly in the striatum and cortex.	trinucleotide	80-93	huntingtin	Mus musculus	118-128
31138642-1	2019	Huntington"s disease is caused by a polyglutamine repeat expansion in the huntingtin protein which affects the function and folding of the protein, and results in intracellular protein aggregates.	polyglutamine	36-49	huntingtin	Mus musculus	74-84
31313908-7	2019	Reduced protein synthesis combined with PromISR-6-stimulated autophagic clearance made PromISR-6 the most efficacious GBZ analogue to reduce Huntingtin aggregates and promote survival in a cellular model of Huntington"s disease.	Guanabenz	118-121	huntingtin	Mus musculus	141-151
31040226-1	2019	Huntington"s disease (HD) is a monogenic disorder, driven by the expansion of a trinucleotide (CAG) repeat within the huntingtin (Htt) gene and culminating in neuronal degeneration in the brain, predominantly in the striatum and cortex.	trinucleotide	80-93	huntingtin	Mus musculus	130-133
31040226-1	2019	Huntington"s disease (HD) is a monogenic disorder, driven by the expansion of a trinucleotide (CAG) repeat within the huntingtin (Htt) gene and culminating in neuronal degeneration in the brain, predominantly in the striatum and cortex.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	95-98	huntingtin	Mus musculus	118-128
31040226-1	2019	Huntington"s disease (HD) is a monogenic disorder, driven by the expansion of a trinucleotide (CAG) repeat within the huntingtin (Htt) gene and culminating in neuronal degeneration in the brain, predominantly in the striatum and cortex.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	95-98	huntingtin	Mus musculus	130-133
30902619-1	2019	Huntington"s disease (HD) is a progressive ultimately fatal disorder caused by a glutamine-encoding CAG expansion in the huntingtin (HTT) gene that results in degeneration mainly in striatal and cerebro-cortical brain regions.	Glutamine	81-90	huntingtin	Mus musculus	121-131
30902619-1	2019	Huntington"s disease (HD) is a progressive ultimately fatal disorder caused by a glutamine-encoding CAG expansion in the huntingtin (HTT) gene that results in degeneration mainly in striatal and cerebro-cortical brain regions.	Glutamine	81-90	huntingtin	Mus musculus	133-136
31263285-1	2019	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin gene (HTT), which codes for the pathologic mutant HTT (mHTT) protein.	trinucleotide	95-108	huntingtin	Mus musculus	126-136
31165723-8	2019	Moreover, metformin intake reduces the number of nuclear aggregates of mutant huntingtin in the striatum.	Metformin	10-19	huntingtin	Mus musculus	78-88
30362565-3	2019	We found that meldonium was able to prevent cytotoxicity induced by serum deprivation, to reduce the accumulation of mutated huntingtin (mHtt) aggregates, and to upregulate the expression of peroxisome proliferator-activated receptor gamma coactivator 1alpha (PGC-1alpha) in mHTT-expressing cells.	3-(2,2,2-trimethylhydrazine)propionate	14-23	huntingtin	Mus musculus	137-141
30362565-3	2019	We found that meldonium was able to prevent cytotoxicity induced by serum deprivation, to reduce the accumulation of mutated huntingtin (mHtt) aggregates, and to upregulate the expression of peroxisome proliferator-activated receptor gamma coactivator 1alpha (PGC-1alpha) in mHTT-expressing cells.	3-(2,2,2-trimethylhydrazine)propionate	14-23	huntingtin	Mus musculus	275-279
30362565-5	2019	Meldonium-induced PGC-1alpha significantly alleviated motor dysfunction and prolonged the survival of a transgenic HD Drosophila model in which mHtt expression in the nervous system led to progressive motor performance deficits.	3-(2,2,2-trimethylhydrazine)propionate	0-9	huntingtin	Mus musculus	144-148
31263285-1	2019	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin gene (HTT), which codes for the pathologic mutant HTT (mHTT) protein.	trinucleotide	95-108	huntingtin	Mus musculus	143-146
31263285-1	2019	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG trinucleotide expansion in the huntingtin gene (HTT), which codes for the pathologic mutant HTT (mHTT) protein.	trinucleotide	95-108	huntingtin	Mus musculus	187-190
31076648-1	2019	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by the expansion of the CAG repeat in exon 1 of the huntingtin (HTT) gene, which results in a mutant protein with an extended polyglutamine tract.	polyglutamine	202-215	huntingtin	Mus musculus	128-138
30840784-8	2019	RESULTS: Expression of Na-K-2Cl cotransporter-1 was elevated in the striatum of R6/2 and Hdh150Q/7Q mouse models.	2,6-Dichlorophenylacetic acid	28-31	huntingtin	Mus musculus	89-92
30840784-11	2019	Expression of the mutant huntingtin in astrocytes and neuroinflammation were necessary for enhanced expression of Na-K-2Cl cotransporter-1 in HD mice.	2,6-Dichlorophenylacetic acid	119-122	huntingtin	Mus musculus	25-35
30994454-2	2019	We report that HTT forms a transcription-coupled DNA repair (TCR) complex with RNA polymerase II subunit A (POLR2A), ataxin-3, the DNA repair enzyme polynucleotide-kinase-3"-phosphatase (PNKP), and cyclic AMP-response element-binding (CREB) protein (CBP).	Cyclic AMP	198-208	huntingtin	Mus musculus	15-18
31088970-4	2019	In cell culture, IKKbeta phosphorylates HTT serine (S) 13 and activates HTT degradation, a process that becomes impaired with polyQ expansion.	Serine	44-50	huntingtin	Mus musculus	40-43
31088970-4	2019	In cell culture, IKKbeta phosphorylates HTT serine (S) 13 and activates HTT degradation, a process that becomes impaired with polyQ expansion.	Serine	52-53	huntingtin	Mus musculus	40-43
30914306-5	2019	Here, we show that JZL-184, a selective inhibitor of monoacylglycerol lipase (MGL), the key enzyme that deactivates the endocannabinoid 2-arachidonoylglycerol, prevented the mutant huntingtin-induced up-regulation of the pro-inflammatory cytokine tumor necrosis factor-alpha in primary mouse striatal astrocytes via CB1 receptors.	glyceryl 2-arachidonate	136-158	huntingtin	Mus musculus	181-191
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	Mus musculus	73-83
30961637-1	2019	Huntington"s disease (HD) is a neurodegenerative disorder caused by a genetic abnormality in the huntingtin gene that leads to a polyglutamine repeat expansion of the huntingtin protein.	polyglutamine	129-142	huntingtin	Mus musculus	97-107
30961637-1	2019	Huntington"s disease (HD) is a neurodegenerative disorder caused by a genetic abnormality in the huntingtin gene that leads to a polyglutamine repeat expansion of the huntingtin protein.	polyglutamine	129-142	huntingtin	Mus musculus	167-177
30961637-2	2019	The cleaved polyglutamine expansion of mutant huntingtin (mHTT) protein can form aggregates strongly correlated with HD progression.	polyglutamine	12-25	huntingtin	Mus musculus	46-56
31076648-1	2019	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by the expansion of the CAG repeat in exon 1 of the huntingtin (HTT) gene, which results in a mutant protein with an extended polyglutamine tract.	polyglutamine	202-215	huntingtin	Mus musculus	140-143
31049134-0	2019	Prevention of Huntington"s Disease-Like Behavioral Deficits in R6/1 Mouse by Tolfenamic Acid Is Associated with Decreases in Mutant Huntingtin and Oxidative Stress.	tolfenamic acid	77-92	huntingtin	Mus musculus	132-142
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	98-101	huntingtin	Mus musculus	137-147
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	98-101	huntingtin	Mus musculus	149-152
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	98-101	huntingtin	Mus musculus	221-224
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	trinucleotide	102-115	huntingtin	Mus musculus	137-147
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	trinucleotide	102-115	huntingtin	Mus musculus	149-152
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	trinucleotide	102-115	huntingtin	Mus musculus	221-224
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	polyglutamine	183-197	huntingtin	Mus musculus	137-147
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	polyglutamine	183-197	huntingtin	Mus musculus	149-152
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	polyglutamine	183-197	huntingtin	Mus musculus	221-224
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	polyglutamine	199-204	huntingtin	Mus musculus	137-147
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	polyglutamine	199-204	huntingtin	Mus musculus	149-152
30913220-1	2019	Huntington"s disease (HD) is a monogenic neurodegenerative disorder caused by an expansion of the CAG trinucleotide repeat domain in the huntingtin (HTT) gene, leading to an expanded poly-glutamine (polyQ) stretch in the HTT protein.	polyglutamine	199-204	huntingtin	Mus musculus	221-224
31049134-5	2019	Tolfenamic acid decreased the expression of mutant huntingtin in the striatum of 20-week-old R6/1 mice by inhibiting specificity protein 1 expression and enhancing autophagic function.	tolfenamic acid	0-15	huntingtin	Mus musculus	51-61
30897080-4	2019	Comparative molecular analysis of wild-type and Htt-null retinoic acid-differentiated cells revealed gene network dysregulation associated with organ development that nominate polycomb repressive complexes and miRNAs as molecular mediators.	retinoic	57-65	huntingtin	Mus musculus	48-51
30984798-2	2019	The translated expanded polyglutamine repeat in the HTT protein is known to cause toxic gain of function.	polyglutamine	24-37	huntingtin	Mus musculus	52-55
30899454-0	2019	Oral administration of the cannabigerol derivative VCE-003.2 promotes subventricular zone neurogenesis and protects against mutant huntingtin-induced neurodegeneration.	cannabigerol	27-39	huntingtin	Mus musculus	131-141
30899454-3	2019	Methods: We investigated the pro-neurogenic potential of the synthetic cannabigerol derivative, VCE-003.2, in striatal neurodegeneration by using adeno-associated viral expression of mutant huntingtin in vivo and mouse embryonic stem cell differentiation in vitro.	cannabigerol	71-83	huntingtin	Mus musculus	190-200
30626701-9	2019	Our findings have important implications for the establishment and deployment of neural circuitries and the integrity of network reserve in health and disease.SIGNIFICANCE STATEMENT Huntington"s disease (HD) is a progressive degenerative disorder caused by aberrant trinucleotide expansion in the huntingtin gene.	trinucleotide	266-279	huntingtin	Mus musculus	297-307
30423259-2	2019	It is caused by an expansion in the polyglutamine repeat at the N terminus of huntingtin (HTT) that leads to aggregation of mutant HTT.	polyglutamine	36-49	huntingtin	Mus musculus	78-88
30423259-2	2019	It is caused by an expansion in the polyglutamine repeat at the N terminus of huntingtin (HTT) that leads to aggregation of mutant HTT.	polyglutamine	36-49	huntingtin	Mus musculus	90-93
30423259-2	2019	It is caused by an expansion in the polyglutamine repeat at the N terminus of huntingtin (HTT) that leads to aggregation of mutant HTT.	polyglutamine	36-49	huntingtin	Mus musculus	131-134
30423259-5	2019	In particular, we have previously shown that caspase cleavage of mutant HTT at amino acid position aspartate 586 (D586) by caspase-6 is critical for the pathogenesis of the disease in an HD mouse model.	Aspartic Acid	99-108	huntingtin	Mus musculus	72-75
30618600-1	2018	Huntington"s disease (HD) is a neurodegenerative disorder caused by a tandem repeat mutation encoding an expanded polyglutamine tract in the huntingtin protein, which leads to cognitive, psychiatric and motor dysfunction.	polyglutamine	114-127	huntingtin	Mus musculus	141-151
30881980-1	2019	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease due to an expansion of a trinucleotide repeats in IT15 gene encoding for the protein huntingtin.	trinucleotide	102-115	huntingtin	Mus musculus	127-131
30881980-1	2019	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease due to an expansion of a trinucleotide repeats in IT15 gene encoding for the protein huntingtin.	trinucleotide	102-115	huntingtin	Mus musculus	162-172
29709465-13	2019	These data further suggest that specific changes in expression of cannabinoid receptors, preproenkephalin, and PDE10A, considered to be the hallmark of HD transcriptional dysregulation, may be produced by an abnormality of glutamate homeostasis under the regulation of neuronal GLT-1, or a synaptic disturbance caused by that abnormality, independently of mutation in huntingtin.	Glutamic Acid	223-232	huntingtin	Mus musculus	368-378
31079989-1	2019	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the huntingtin (Htt) protein, which results in a protein containing an abnormally expanded polyglutamine (polyQ) sequence.	trinucleotide	106-119	huntingtin	Mus musculus	162-172
31079989-1	2019	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the huntingtin (Htt) protein, which results in a protein containing an abnormally expanded polyglutamine (polyQ) sequence.	trinucleotide	106-119	huntingtin	Mus musculus	174-177
31079989-1	2019	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the huntingtin (Htt) protein, which results in a protein containing an abnormally expanded polyglutamine (polyQ) sequence.	polyglutamine	249-262	huntingtin	Mus musculus	162-172
31079989-1	2019	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the huntingtin (Htt) protein, which results in a protein containing an abnormally expanded polyglutamine (polyQ) sequence.	polyglutamine	249-262	huntingtin	Mus musculus	174-177
31079989-1	2019	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the huntingtin (Htt) protein, which results in a protein containing an abnormally expanded polyglutamine (polyQ) sequence.	polyglutamine	264-269	huntingtin	Mus musculus	162-172
31079989-1	2019	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene encoding the huntingtin (Htt) protein, which results in a protein containing an abnormally expanded polyglutamine (polyQ) sequence.	polyglutamine	264-269	huntingtin	Mus musculus	174-177
31079989-2	2019	The expanded polyQ in the Htt protein is toxic to brain cells.	polyglutamine	13-18	huntingtin	Mus musculus	26-29
30594931-9	2019	Affinity chromatography analysis of striatal lysates showed that Huntingtin is in a complex with Rac1, p85alpha subunit of PI 3-kinase, and the actin bundling protein alpha-actinin and interacts preferentially with the GTP bound form of Rac1.	Guanosine Triphosphate	219-222	huntingtin	Mus musculus	65-75
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	29-42	huntingtin	Mus musculus	101-111
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	29-42	huntingtin	Mus musculus	113-116
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	29-42	huntingtin	Mus musculus	124-128
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	29-42	huntingtin	Mus musculus	174-177
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	44-49	huntingtin	Mus musculus	101-111
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	44-49	huntingtin	Mus musculus	113-116
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	44-49	huntingtin	Mus musculus	124-128
30937182-2	2019	The disease is caused by the polyglutamine (polyQ) expansion at the 5" terminal of the exon 1 of the huntingtin (HTT) gene, IT15, which results in the accumulation of mutant HTT (mHTT) aggregates in neurons and cell death.	polyglutamine	44-49	huntingtin	Mus musculus	174-177
30292559-12	2019	Female R6/2 mice given WT-level corticosterone replacement also showed a reduction in HD neuropathological markers, including a reduction in mHTT inclusion burden in the striatum, cortex, and hippocampus (p < .05 for all).	Corticosterone	32-46	huntingtin	Mus musculus	141-145
30455632-0	2018	Huntingtin-Associated Protein 1A Regulates Store-Operated Calcium Entry in Medium Spiny Neurons From Transgenic YAC128 Mice, a Model of Huntington"s Disease.	Calcium	58-65	huntingtin	Mus musculus	0-10
30455632-1	2018	Huntington"s disease (HD) is a hereditary neurodegenerative disease that is caused by polyglutamine expansion within the huntingtin (HTT) gene.	polyglutamine	86-99	huntingtin	Mus musculus	121-131
30455632-1	2018	Huntington"s disease (HD) is a hereditary neurodegenerative disease that is caused by polyglutamine expansion within the huntingtin (HTT) gene.	polyglutamine	86-99	huntingtin	Mus musculus	133-136
30282695-3	2018	We previously identified HTT single-nucleotide polymorphisms (SNPs) tightly linked to the HD mutation and developed antisense oligonucleotides (ASOs) targeting HD-SNPs that selectively suppress mutant HTT.	Oligonucleotides	126-142	huntingtin	Mus musculus	201-204
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	Mus musculus	27-31
30143534-9	2018	CREB repression was reversed by heat shock coinciding with mHtt IB formation.	ib	64-66	huntingtin	Mus musculus	59-63
30143534-10	2018	In an embryonic striatal neuron-derived HD model, the chemical chaperone sorbitol similarly promoted the structuring of diffuse mHtt into IBs and supported cell survival under stress.	Sorbitol	73-81	huntingtin	Mus musculus	128-132
30282695-3	2018	We previously identified HTT single-nucleotide polymorphisms (SNPs) tightly linked to the HD mutation and developed antisense oligonucleotides (ASOs) targeting HD-SNPs that selectively suppress mutant HTT.	Oligonucleotides, Antisense	144-148	huntingtin	Mus musculus	25-28
30282695-3	2018	We previously identified HTT single-nucleotide polymorphisms (SNPs) tightly linked to the HD mutation and developed antisense oligonucleotides (ASOs) targeting HD-SNPs that selectively suppress mutant HTT.	Oligonucleotides, Antisense	144-148	huntingtin	Mus musculus	201-204
30282695-6	2018	To determine the translational potential of the treatment, we examined the effect of ASO administration on HTT brain expression in nonhuman primates.	Oligonucleotides, Antisense	85-88	huntingtin	Mus musculus	107-110
29294248-5	2018	Azadiradione-treated HD mice brain also exhibited considerable decrease in mutant huntingtin aggregates load and improvement of striatal pathology in comparison with age-matched saline-treated HD controls.	azadiradione	0-12	huntingtin	Mus musculus	82-92
30107216-1	2018	Huntington"s Disease (HD) is an autosomal dominant neurodegenerative disease caused by abnormal polyglutamine expansion in huntingtin (mHtt) protein leading to degeneration of striatal neurons.	polyglutamine	96-109	huntingtin	Mus musculus	123-133
30107216-1	2018	Huntington"s Disease (HD) is an autosomal dominant neurodegenerative disease caused by abnormal polyglutamine expansion in huntingtin (mHtt) protein leading to degeneration of striatal neurons.	polyglutamine	96-109	huntingtin	Mus musculus	135-139
30107216-3	2018	Mutant Htt causes enhanced NMDA sensitivity, alteration of NMDAR expression and localization in neurons.	N-Methylaspartate	27-31	huntingtin	Mus musculus	7-10
30107216-11	2018	Cholesterol as well as GluN2B level in lipid raft, are significantly increased by mHtt.	Cholesterol	0-11	huntingtin	Mus musculus	82-86
29713895-1	2018	Huntington"s disease (HD) is a neurodegenerative disease caused by a polyglutamine expansion in the huntingtin (Htt) protein.	polyglutamine	69-82	huntingtin	Mus musculus	100-110
29713895-1	2018	Huntington"s disease (HD) is a neurodegenerative disease caused by a polyglutamine expansion in the huntingtin (Htt) protein.	polyglutamine	69-82	huntingtin	Mus musculus	112-115
29713895-9	2018	Furthermore, we found that only SV2C expression was progressively inhibited in N2a cells expressing a mutant Htt containing 120 glutamine repeats.	Glutamine	128-137	huntingtin	Mus musculus	109-112
30179155-5	2018	We furthermore show that the antidiabetic drug metformin diminishes aberrant Huntingtin protein load and fully restores both early network activity patterns and behavioral aberrations.	Metformin	47-56	huntingtin	Mus musculus	77-87
30186318-1	2018	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a trinucleotide expansion in the HD gene, resulting in an extended polyglutamine tract in the protein huntingtin.	trinucleotide	90-103	huntingtin	Mus musculus	190-200
29294248-6	2018	Biochemical analysis further revealed upregulation and activation of not only HSF1 (master regulator of protein folding) but also Ube3a (an ubiquitin ligase involved in the clearance of mutant huntingtin) in azadiradione-treated mice.	azadiradione	208-220	huntingtin	Mus musculus	193-203
29294248-7	2018	Our results indicate that azadiradione-mediated enhanced folding and clearance of mutant huntingtin might underlie improved disease pathology in HD mice and suggests that it could be a potential therapeutic molecule to delay the progression of HD.	azadiradione	26-38	huntingtin	Mus musculus	89-99
30002810-0	2018	Mutant huntingtin induces iron overload via up-regulating IRP1 in Huntington"s disease.	Iron	26-30	huntingtin	Mus musculus	7-17
29914757-1	2018	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein.	polyglutamine	103-116	huntingtin	Mus musculus	130-140
29891550-1	2018	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an abnormal expansion of polyglutamine repeats in the huntingtin protein (Htt).	polyglutamine	99-112	huntingtin	Mus musculus	128-138
29891550-1	2018	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an abnormal expansion of polyglutamine repeats in the huntingtin protein (Htt).	polyglutamine	99-112	huntingtin	Mus musculus	148-151
29987005-0	2018	N6-Furfuryladenine is protective in Huntington"s disease models by signaling huntingtin phosphorylation.	Kinetin	0-18	huntingtin	Mus musculus	77-87
29987005-4	2018	N6FFA was protective in HD model neurons, and N6FFA treatment of an HD mouse model corrects HD phenotypes and eliminates cortical mutant huntingtin inclusions.	Kinetin	46-51	huntingtin	Mus musculus	137-147
29987005-8	2018	We present a model in which this natural product compound is salvaged to provide a triphosphate substrate to signal huntingtin phosphorylation via CK2 during low-ATP stress under conditions of DNA damage, with protective effects in HD model systems.	triphosphoric acid	83-95	huntingtin	Mus musculus	116-126
29987005-8	2018	We present a model in which this natural product compound is salvaged to provide a triphosphate substrate to signal huntingtin phosphorylation via CK2 during low-ATP stress under conditions of DNA damage, with protective effects in HD model systems.	Adenosine Triphosphate	162-165	huntingtin	Mus musculus	116-126
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	Mus musculus	12-16
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	Mus musculus	12-16
29510748-1	2018	Huntington disease (HD) is caused by the expression of mutant huntingtin (mHTT) bearing a polyglutamine expansion.	polyglutamine	90-103	huntingtin	Mus musculus	62-72
29608652-2	2018	Huntington"s disease is mainly caused by cytotoxicity of the mutant HTT protein with an expanded polyglutamine repeat tract.	polyglutamine	97-110	huntingtin	Mus musculus	68-71
29608652-7	2018	Importantly, a novel Gpr52 antagonist E7 reduces mutant HTT levels and rescues Huntington"s disease-associated phenotypes in cellular and mouse models.	WWGKKYRASKLGLAR	38-40	huntingtin	Mus musculus	56-59
29509900-1	2018	Polyglutamine expansions in the huntingtin gene cause Huntington"s disease (HD).	polyglutamine	0-13	huntingtin	Mus musculus	32-42
29462355-1	2018	Huntington"s disease (HD) is caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the huntingtin (HTT) gene encoding an elongated polyglutamine tract within the N-terminal of the huntingtin protein (Htt) and leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms.	cytosine-adenine-guanine (cag) trinucleotide	41-85	huntingtin	Mus musculus	110-120
29462355-1	2018	Huntington"s disease (HD) is caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the huntingtin (HTT) gene encoding an elongated polyglutamine tract within the N-terminal of the huntingtin protein (Htt) and leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms.	cytosine-adenine-guanine (cag) trinucleotide	41-85	huntingtin	Mus musculus	122-125
29462355-1	2018	Huntington"s disease (HD) is caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the huntingtin (HTT) gene encoding an elongated polyglutamine tract within the N-terminal of the huntingtin protein (Htt) and leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms.	cytosine-adenine-guanine (cag) trinucleotide	41-85	huntingtin	Mus musculus	203-213
29462355-1	2018	Huntington"s disease (HD) is caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the huntingtin (HTT) gene encoding an elongated polyglutamine tract within the N-terminal of the huntingtin protein (Htt) and leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms.	cytosine-adenine-guanine (cag) trinucleotide	41-85	huntingtin	Mus musculus	223-226
29462355-1	2018	Huntington"s disease (HD) is caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the huntingtin (HTT) gene encoding an elongated polyglutamine tract within the N-terminal of the huntingtin protein (Htt) and leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms.	cytosine-adenine-guanine (cag) trinucleotide	41-85	huntingtin	Mus musculus	241-244
30002810-9	2018	Conclusion: We conclude that mutant huntingtin may cause abnormal iron homeostatic pathways by increasing IRP1 expression in Huntington"s disease, suggesting potential therapeutic target.	Iron	66-70	huntingtin	Mus musculus	36-46
29510748-1	2018	Huntington disease (HD) is caused by the expression of mutant huntingtin (mHTT) bearing a polyglutamine expansion.	polyglutamine	90-103	huntingtin	Mus musculus	74-78
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	Mus musculus	124-128
28986324-1	2018	Huntington"s disease (HD) is caused by a CAG repeat expansion that encodes a polyglutamine (polyQ) expansion in the HD disease protein, huntingtin (HTT).	polyglutamine	77-90	huntingtin	Mus musculus	136-146
28858902-2	2018	Previous studies have shown that HD is caused by the exon 1 region of the huntingtin (HTT) gene having expanded CAG trinucleotide repeats.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	112-115	huntingtin	Mus musculus	74-84
28858902-2	2018	Previous studies have shown that HD is caused by the exon 1 region of the huntingtin (HTT) gene having expanded CAG trinucleotide repeats.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	112-115	huntingtin	Mus musculus	86-89
28858902-2	2018	Previous studies have shown that HD is caused by the exon 1 region of the huntingtin (HTT) gene having expanded CAG trinucleotide repeats.	trinucleotide	116-129	huntingtin	Mus musculus	74-84
28858902-2	2018	Previous studies have shown that HD is caused by the exon 1 region of the huntingtin (HTT) gene having expanded CAG trinucleotide repeats.	trinucleotide	116-129	huntingtin	Mus musculus	86-89
28858902-5	2018	METHODS: We used clinical similar transgenic HD mice carrying a mutant HTT exon 1 containing 84 CAG trinucleotide repeats to evaluate the relationship between HD and pain.	trinucleotide	100-113	huntingtin	Mus musculus	71-74
29056363-0	2018	Pramipexole reduces soluble mutant huntingtin and protects striatal neurons through dopamine D3 receptors in a genetic model of Huntington"s disease.	Pramipexole	0-11	huntingtin	Mus musculus	35-45
29056363-1	2018	Huntington"s disease (HD) is a neurodegenerative disorder caused by abnormal expansion of the polyglutamine tract in the huntingtin protein (HTT).	polyglutamine	94-107	huntingtin	Mus musculus	121-131
29056363-1	2018	Huntington"s disease (HD) is a neurodegenerative disorder caused by abnormal expansion of the polyglutamine tract in the huntingtin protein (HTT).	polyglutamine	94-107	huntingtin	Mus musculus	141-144
29056363-9	2018	Pramipexole reduced striatal levels of soluble mHTT and increased the size of intranuclear inclusions in R6/1 mice.	Pramipexole	0-11	huntingtin	Mus musculus	47-51
29056363-14	2018	The findings indicate that PPX protects striatal neurons by promoting the clearance of soluble mHTT through a D3R-mediated mechanism.	paclitaxel poliglumex	27-30	huntingtin	Mus musculus	95-99
29843246-1	2018	BACKGROUND: Huntington"s disease (HD) is a progressive neurodegenerative disorder associated with aging, caused by an expanded polyglutamine (polyQ) repeat within the Huntingtin (HTT) protein.	polyglutamine	127-140	huntingtin	Mus musculus	179-182
29843246-1	2018	BACKGROUND: Huntington"s disease (HD) is a progressive neurodegenerative disorder associated with aging, caused by an expanded polyglutamine (polyQ) repeat within the Huntingtin (HTT) protein.	polyglutamine	142-147	huntingtin	Mus musculus	167-177
29843246-1	2018	BACKGROUND: Huntington"s disease (HD) is a progressive neurodegenerative disorder associated with aging, caused by an expanded polyglutamine (polyQ) repeat within the Huntingtin (HTT) protein.	polyglutamine	142-147	huntingtin	Mus musculus	179-182
29843246-4	2018	METHODS: Using whole brain cell lysates, a unique method of SDS-PAGE and western analysis was used to quantitate HTT protein, which resolves as a monomer and as a high molecular weight species that is modulated by the presence of transglutaminase 2.	Sodium Dodecyl Sulfate	60-63	huntingtin	Mus musculus	113-116
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	Mus musculus	30-34
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	Mus musculus	30-34
29856017-1	2018	Motor deficits are a characteristic consequence of striatal damage, whether induced by experimental lesions, or in genetic models of Huntington"s disease involving polyglutamine expansion in the huntingtin protein.	polyglutamine	164-177	huntingtin	Mus musculus	195-205
29172480-5	2018	We have screened a set of small molecules to target this transcript and found Myricetin, a flavonoid, as a lead molecule that interacts with the CAG motif and thus prevents the translation of mutant huntingtin protein as well as sequestration of MBNL1.	myricetin	78-87	huntingtin	Mus musculus	199-209
29172480-5	2018	We have screened a set of small molecules to target this transcript and found Myricetin, a flavonoid, as a lead molecule that interacts with the CAG motif and thus prevents the translation of mutant huntingtin protein as well as sequestration of MBNL1.	Flavonoids	91-100	huntingtin	Mus musculus	199-209
29233555-2	2018	Expansion of the glutamine-encoding repeat in the Huntingtin (HTT) gene causes broad effects that are a challenge for single treatment strategies.	Glutamine	17-26	huntingtin	Mus musculus	50-60
29233555-2	2018	Expansion of the glutamine-encoding repeat in the Huntingtin (HTT) gene causes broad effects that are a challenge for single treatment strategies.	Glutamine	17-26	huntingtin	Mus musculus	62-65
28986324-1	2018	Huntington"s disease (HD) is caused by a CAG repeat expansion that encodes a polyglutamine (polyQ) expansion in the HD disease protein, huntingtin (HTT).	polyglutamine	77-90	huntingtin	Mus musculus	148-151
28986324-1	2018	Huntington"s disease (HD) is caused by a CAG repeat expansion that encodes a polyglutamine (polyQ) expansion in the HD disease protein, huntingtin (HTT).	polyglutamine	92-97	huntingtin	Mus musculus	136-146
28986324-1	2018	Huntington"s disease (HD) is caused by a CAG repeat expansion that encodes a polyglutamine (polyQ) expansion in the HD disease protein, huntingtin (HTT).	polyglutamine	92-97	huntingtin	Mus musculus	148-151
28986324-2	2018	PolyQ expansion promotes misfolding and aggregation of mutant HTT (mHTT) within neurons.	polyglutamine	0-5	huntingtin	Mus musculus	62-65
28986324-2	2018	PolyQ expansion promotes misfolding and aggregation of mutant HTT (mHTT) within neurons.	polyglutamine	0-5	huntingtin	Mus musculus	67-71
28986324-5	2018	By virtue of its N-terminal polyQ domain, HTT has an intrinsically disordered amino terminus.	polyglutamine	28-33	huntingtin	Mus musculus	42-45
29212711-3	2017	We recently determined that transcriptional dysregulation of PPARdelta contributes to Huntington"s disease (HD), a progressive neurodegenerative disorder resulting from a CAG-polyglutamine repeat expansion in the huntingtin gene.	polyglutamine	175-188	huntingtin	Mus musculus	213-223
29151587-7	2017	Interestingly, their effects on HTT levels are mHTT-dependent, providing a feedback mechanism in which mHTT enhances its own level thus contributing to mHTT accumulation and disease progression.	mhtt	47-51	huntingtin	Mus musculus	32-35
29151587-7	2017	Interestingly, their effects on HTT levels are mHTT-dependent, providing a feedback mechanism in which mHTT enhances its own level thus contributing to mHTT accumulation and disease progression.	mhtt	103-107	huntingtin	Mus musculus	32-35
29151587-7	2017	Interestingly, their effects on HTT levels are mHTT-dependent, providing a feedback mechanism in which mHTT enhances its own level thus contributing to mHTT accumulation and disease progression.	mhtt	103-107	huntingtin	Mus musculus	32-35
29166617-1	2017	Aggregation of polyglutamine-expanded huntingtin exon 1 (HttEx1) in Huntington"s disease (HD) proceeds from soluble oligomers to late-stage inclusions.	polyglutamine	15-28	huntingtin	Mus musculus	38-48
29019003-2	2017	The primary genetic cause is an expansion of cytosine adenine guanine (CAG) nucleotides of the huntingtin gene, which codes an important protein involved with neuronal signaling.	cytosine adenine guanine	45-69	huntingtin	Mus musculus	95-105
29019003-2	2017	The primary genetic cause is an expansion of cytosine adenine guanine (CAG) nucleotides of the huntingtin gene, which codes an important protein involved with neuronal signaling.	cag) nucleotides	71-87	huntingtin	Mus musculus	95-105
28593442-7	2017	Nogalamycin modulated the expression of the H3K9me3-landscaped epigenome in medium spiny neurons and reduced mutant HTT nuclear inclusion formation.	Nogalamycin	0-11	huntingtin	Mus musculus	116-119
29160844-1	2017	Huntington"s disease (HD) is caused by an unstable cytosine adenine guanine (CAG) trinucleotide repeat expansion encoding a polyglutamine tract in the huntingtin protein.	cytosine adenine guanine (cag) trinucleotide	51-95	huntingtin	Mus musculus	151-161
29070884-5	2017	Telmisartan also reversed the decrease in PPARdelta and 5-HTT levels in the hippocampus of depression-like mice.	Telmisartan	0-11	huntingtin	Mus musculus	58-61
29843246-1	2018	BACKGROUND: Huntington"s disease (HD) is a progressive neurodegenerative disorder associated with aging, caused by an expanded polyglutamine (polyQ) repeat within the Huntingtin (HTT) protein.	polyglutamine	127-140	huntingtin	Mus musculus	167-177
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	Mus musculus	42-46
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	Mus musculus	42-46
28213125-9	2017	These data support a hypothesis that mutant HTT leads to a selective deficiency of neuronal Mn at an early disease stage, contributing to HD striatal urea-cycle pathophysiology through an effect on arginase activity.	Urea	150-154	huntingtin	Mus musculus	44-47
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	Mus musculus	182-186
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	Mus musculus	182-186
28653853-2	2017	PTMs of polyglutamine-expanded huntingtin (Htt) protein, which causes Huntington"s disease (HD), are likely modulators of HD pathogenesis.	polyglutamine	8-21	huntingtin	Mus musculus	31-41
28653853-2	2017	PTMs of polyglutamine-expanded huntingtin (Htt) protein, which causes Huntington"s disease (HD), are likely modulators of HD pathogenesis.	polyglutamine	8-21	huntingtin	Mus musculus	43-46
28391067-1	2017	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.	polyglutamine	90-103	huntingtin	Mus musculus	150-160
28391067-1	2017	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.	polyglutamine	90-103	huntingtin	Mus musculus	162-165
27957684-1	2017	Among several mechanisms underlying the well-known trophic and protective effects of 17beta-estradiol (E2) in the brain, we recently reported that E2 induces the up-regulation of two anti-apoptotic and neuroprotectant proteins: huntingtin (HTT) and neuroglobin (NGB).	Estradiol	85-101	huntingtin	Mus musculus	228-238
27957684-1	2017	Among several mechanisms underlying the well-known trophic and protective effects of 17beta-estradiol (E2) in the brain, we recently reported that E2 induces the up-regulation of two anti-apoptotic and neuroprotectant proteins: huntingtin (HTT) and neuroglobin (NGB).	Estradiol	85-101	huntingtin	Mus musculus	240-243
27957684-4	2017	All E2 effects were completely abolished in HTT-knocked out SK-N-BE cells and in striatal neurons expressing the mutated form of HTT (mHTT; i.e., polyQ111) typical of Huntington"s disease (HD).	sk-n-be	60-67	huntingtin	Mus musculus	44-47
28743452-1	2017	Huntington"s disease is caused by polyglutamine (polyQ)-expansion mutations in the CAG tandem repeat of the Huntingtin gene.	polyglutamine	34-47	huntingtin	Mus musculus	108-118
28743452-1	2017	Huntington"s disease is caused by polyglutamine (polyQ)-expansion mutations in the CAG tandem repeat of the Huntingtin gene.	polyglutamine	49-54	huntingtin	Mus musculus	108-118
28632387-4	2017	The designed poly(trehalose) nanoparticles are 1000-10000 times more efficient than molecular trehalose in inhibiting protein fibrillation in extra-cellular space, in blocking aggregation of polyglutamine-containing mutant huntingtin protein in model neuronal cells, and in suppressing mutant huntingtin aggregates in HD mouse brain.	poly(trehalose)	13-28	huntingtin	Mus musculus	223-233
28632387-4	2017	The designed poly(trehalose) nanoparticles are 1000-10000 times more efficient than molecular trehalose in inhibiting protein fibrillation in extra-cellular space, in blocking aggregation of polyglutamine-containing mutant huntingtin protein in model neuronal cells, and in suppressing mutant huntingtin aggregates in HD mouse brain.	poly(trehalose)	13-28	huntingtin	Mus musculus	293-303
28632387-4	2017	The designed poly(trehalose) nanoparticles are 1000-10000 times more efficient than molecular trehalose in inhibiting protein fibrillation in extra-cellular space, in blocking aggregation of polyglutamine-containing mutant huntingtin protein in model neuronal cells, and in suppressing mutant huntingtin aggregates in HD mouse brain.	Trehalose	18-27	huntingtin	Mus musculus	223-233
28632387-4	2017	The designed poly(trehalose) nanoparticles are 1000-10000 times more efficient than molecular trehalose in inhibiting protein fibrillation in extra-cellular space, in blocking aggregation of polyglutamine-containing mutant huntingtin protein in model neuronal cells, and in suppressing mutant huntingtin aggregates in HD mouse brain.	Trehalose	18-27	huntingtin	Mus musculus	293-303
28632387-4	2017	The designed poly(trehalose) nanoparticles are 1000-10000 times more efficient than molecular trehalose in inhibiting protein fibrillation in extra-cellular space, in blocking aggregation of polyglutamine-containing mutant huntingtin protein in model neuronal cells, and in suppressing mutant huntingtin aggregates in HD mouse brain.	polyglutamine	191-204	huntingtin	Mus musculus	223-233
28632387-5	2017	We show that the nanoparticle form of trehalose with zwitterionic surface charge and a trehalose multivalency (i.e., number of trehalose molecules per nanoparticle) of ~80-200 are crucial for efficient brain targeting, entry into neuronal cells, and suppression of mutant huntingtin aggregation.	Trehalose	38-47	huntingtin	Mus musculus	272-282
28715425-0	2017	Elimination of huntingtin in the adult mouse leads to progressive behavioral deficits, bilateral thalamic calcification, and altered brain iron homeostasis.	Iron	139-143	huntingtin	Mus musculus	15-25
28715425-7	2017	Here we show that elimination of Htt expression in the adult mouse results in behavioral deficits, progressive neuropathological changes including bilateral thalamic calcification, and altered brain iron homeostasis.	Iron	199-203	huntingtin	Mus musculus	33-36
28359739-4	2017	Therefore, counteracting mutant huntingtin (mHtt)-induced oxidative stress and mitochondrial dysfunction appears as a new approach to treat this devastating disease.	mhtt	44-48	huntingtin	Mus musculus	32-42
28628038-1	2017	Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine repeat in the Huntingtin gene (HTT).	polyglutamine	65-78	huntingtin	Mus musculus	93-103
28628038-1	2017	Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine repeat in the Huntingtin gene (HTT).	polyglutamine	65-78	huntingtin	Mus musculus	110-113
28462988-2	2017	We recently described the activity and safety profile of a docosahexaenoic acid (DHA)-conjugated, hydrophobic siRNA (DHA-hsiRNA) targeting Huntingtin (Htt) mRNA in mouse brain.	Docosahexaenoic Acids	59-79	huntingtin	Mus musculus	139-149
28462988-2	2017	We recently described the activity and safety profile of a docosahexaenoic acid (DHA)-conjugated, hydrophobic siRNA (DHA-hsiRNA) targeting Huntingtin (Htt) mRNA in mouse brain.	Docosahexaenoic Acids	59-79	huntingtin	Mus musculus	151-154
28462988-2	2017	We recently described the activity and safety profile of a docosahexaenoic acid (DHA)-conjugated, hydrophobic siRNA (DHA-hsiRNA) targeting Huntingtin (Htt) mRNA in mouse brain.	Docosahexaenoic Acids	81-84	huntingtin	Mus musculus	139-149
28462988-2	2017	We recently described the activity and safety profile of a docosahexaenoic acid (DHA)-conjugated, hydrophobic siRNA (DHA-hsiRNA) targeting Huntingtin (Htt) mRNA in mouse brain.	Docosahexaenoic Acids	81-84	huntingtin	Mus musculus	151-154
28462988-5	2017	We demonstrate that PC-DHA-hsiRNA silences Htt in mouse primary cortical neurons and astrocytes.	pc-dha	20-26	huntingtin	Mus musculus	43-46
28632780-3	2017	Recent work suggests that treating invertebrate and mice HD models with metformin, a well-known AMPK activator which is used worldwide to treat type 2-diabetes, reduces mutant huntingtin from cells and alleviates many of the phenotypes associated to HD.	Metformin	72-81	huntingtin	Mus musculus	176-186
28391013-1	2017	Huntington"s disease (HD) is a hereditary neurodegenerative disorder resulting from N-terminal polyglutamine expansion in the huntingtin protein.	polyglutamine	95-108	huntingtin	Mus musculus	126-136
28533744-1	2017	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder characterized by a polyglutamine expansion within the N-terminal region of huntingtin protein (HTT).	polyglutamine	98-111	huntingtin	Mus musculus	154-164
28596754-7	2017	In conclusion, mutant huntingtin-expressing cells showed a negligible effect of Ang II on potassium current, a result probably due to the reduced expression of AT1 receptors at the surface cell membrane.	Potassium	90-99	huntingtin	Mus musculus	22-32
28638078-6	2017	MAP4343, 17ssE2 and isoquercitrin also promote stress resistance in mutant Htt striatal cells derived from knock-in HD mice.	Pregnenolone methyl ether	0-7	huntingtin	Mus musculus	75-78
28638078-6	2017	MAP4343, 17ssE2 and isoquercitrin also promote stress resistance in mutant Htt striatal cells derived from knock-in HD mice.	17sse2	9-15	huntingtin	Mus musculus	75-78
28638078-6	2017	MAP4343, 17ssE2 and isoquercitrin also promote stress resistance in mutant Htt striatal cells derived from knock-in HD mice.	isoquercitrin	20-33	huntingtin	Mus musculus	75-78
28537272-1	2017	Polyglutamine expansion in the huntingtin protein is the primary genetic cause of Huntington"s disease (HD).	polyglutamine	0-13	huntingtin	Mus musculus	31-41
28533744-1	2017	Huntington"s disease (HD) is a dominantly inherited neurodegenerative disorder characterized by a polyglutamine expansion within the N-terminal region of huntingtin protein (HTT).	polyglutamine	98-111	huntingtin	Mus musculus	174-177
28453524-4	2017	To test this hypothesis, we lowered levels of huntingtin by treating mice with antisense oligonucleotides (ASOs) targeting the murine Huntingtin gene.	Oligonucleotides	89-105	huntingtin	Mus musculus	46-56
28153533-11	2017	This finding suggests that mHTT is a competitor instead of a recruiter of polyQ-containing transcription factors in the transcription process in HD.	polyglutamine	74-79	huntingtin	Mus musculus	27-31
28445460-1	2017	Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3).	polyglutamine	55-68	huntingtin	Mus musculus	115-125
28445460-1	2017	Nine neurodegenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such as huntingtin in Huntington"s disease and ataxin 3 in spinocerebellar ataxia type 3 (SCA3).	polyglutamine	70-75	huntingtin	Mus musculus	115-125
28319609-7	2017	These data suggest that mutant huntingtin impairs neurodevelopmental pathways that could disrupt synaptic homeostasis and increase vulnerability to the pathologic consequence of expanded polyglutamine repeats over time.	polyglutamine	187-200	huntingtin	Mus musculus	31-41
28300621-1	2017	We hypothesized that expression of mutant Huntingtin (HTT) would modulate the neurotoxicity of the commonly used organophosphate insecticide, chlorpyrifos (CPF), revealing cellular mechanisms underlying neurodegeneration.	Organophosphates	113-128	huntingtin	Mus musculus	42-52
28300621-1	2017	We hypothesized that expression of mutant Huntingtin (HTT) would modulate the neurotoxicity of the commonly used organophosphate insecticide, chlorpyrifos (CPF), revealing cellular mechanisms underlying neurodegeneration.	Organophosphates	113-128	huntingtin	Mus musculus	54-57
28300621-1	2017	We hypothesized that expression of mutant Huntingtin (HTT) would modulate the neurotoxicity of the commonly used organophosphate insecticide, chlorpyrifos (CPF), revealing cellular mechanisms underlying neurodegeneration.	Chlorpyrifos	142-154	huntingtin	Mus musculus	42-52
28300621-1	2017	We hypothesized that expression of mutant Huntingtin (HTT) would modulate the neurotoxicity of the commonly used organophosphate insecticide, chlorpyrifos (CPF), revealing cellular mechanisms underlying neurodegeneration.	Chlorpyrifos	142-154	huntingtin	Mus musculus	54-57
28300621-1	2017	We hypothesized that expression of mutant Huntingtin (HTT) would modulate the neurotoxicity of the commonly used organophosphate insecticide, chlorpyrifos (CPF), revealing cellular mechanisms underlying neurodegeneration.	Chlorpyrifos	156-159	huntingtin	Mus musculus	42-52
28300621-1	2017	We hypothesized that expression of mutant Huntingtin (HTT) would modulate the neurotoxicity of the commonly used organophosphate insecticide, chlorpyrifos (CPF), revealing cellular mechanisms underlying neurodegeneration.	Chlorpyrifos	156-159	huntingtin	Mus musculus	54-57
28453524-4	2017	To test this hypothesis, we lowered levels of huntingtin by treating mice with antisense oligonucleotides (ASOs) targeting the murine Huntingtin gene.	Oligonucleotides	89-105	huntingtin	Mus musculus	134-144
28453524-4	2017	To test this hypothesis, we lowered levels of huntingtin by treating mice with antisense oligonucleotides (ASOs) targeting the murine Huntingtin gene.	Oligonucleotides, Antisense	107-111	huntingtin	Mus musculus	46-56
28453524-4	2017	To test this hypothesis, we lowered levels of huntingtin by treating mice with antisense oligonucleotides (ASOs) targeting the murine Huntingtin gene.	Oligonucleotides, Antisense	107-111	huntingtin	Mus musculus	134-144
28453524-7	2017	Peripheral treatment with ASOs led to persistent reduction of huntingtin protein in peripheral organs, including liver (64% knockdown), brown adipose (66% knockdown), and white adipose tissues (71% knockdown).	Oligonucleotides, Antisense	26-30	huntingtin	Mus musculus	62-72
28400517-4	2017	Here, we provide detailed structural mechanisms for aggregation of several protein fragments encoded by HTT exon 1 by using the associative memory, water-mediated, structure and energy model (AWSEM) to construct their free energy landscapes.	Water	148-153	huntingtin	Mus musculus	104-107
28400517-6	2017	The combination of both terminal additions in HTT exon 1 fragment leads to a complex aggregation mechanism with a basic core that resembles that found for the aggregation of pure polyQ repeats using AWSEM.	polyglutamine	179-184	huntingtin	Mus musculus	46-49
28384474-0	2017	Polyglutamine-Expanded Huntingtin Exacerbates Age-Related Disruption of Nuclear Integrity and Nucleocytoplasmic Transport.	polyglutamine	0-13	huntingtin	Mus musculus	23-33
28384474-4	2017	Huntingtin-linked polyglutamine initially accumulates in nuclei, leading to disruption of nuclear envelope architecture, partial sequestration of factors essential for nucleocytoplasmic transport (Gle1 and RanGAP1), and intranuclear accumulation of mRNA.	polyglutamine	18-31	huntingtin	Mus musculus	0-10
28263187-2	2017	While motor impairment mediated by polyQ-expanded HTT has been intensively studied, molecular mechanisms for nonmotor symptoms in HD, such as psychiatric manifestations, remain elusive.	polyglutamine	35-40	huntingtin	Mus musculus	50-53
28263187-3	2017	Here we have demonstrated that HTT forms a ternary protein complex with the scaffolding protein DISC1 and cAMP-degrading phosphodiesterase 4 (PDE4) to regulate PDE4 activity.	Cyclic AMP	106-110	huntingtin	Mus musculus	31-34
28368337-3	2017	The mutant Huntingtin gene (mHTT) contains extra poly-glutamine (CAG) repeats from which the translated mutant huntingtin proteins (mHTT) undergo inappropriate post-translational modifications, conferring a toxic gain of function, in addition to its non-functional property.	polyglutamine	49-63	huntingtin	Mus musculus	111-121
28368337-3	2017	The mutant Huntingtin gene (mHTT) contains extra poly-glutamine (CAG) repeats from which the translated mutant huntingtin proteins (mHTT) undergo inappropriate post-translational modifications, conferring a toxic gain of function, in addition to its non-functional property.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	65-68	huntingtin	Mus musculus	11-21
28368337-3	2017	The mutant Huntingtin gene (mHTT) contains extra poly-glutamine (CAG) repeats from which the translated mutant huntingtin proteins (mHTT) undergo inappropriate post-translational modifications, conferring a toxic gain of function, in addition to its non-functional property.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	65-68	huntingtin	Mus musculus	111-121
28123081-2	2017	We showed previously that the histone deacetylase inhibitors (HDACIs) trichostatin A and sodium butyrate (SB) ameliorate mitochondrial function in cells expressing mutant huntingtin.	trichostatin A	70-84	huntingtin	Mus musculus	171-181
28368337-3	2017	The mutant Huntingtin gene (mHTT) contains extra poly-glutamine (CAG) repeats from which the translated mutant huntingtin proteins (mHTT) undergo inappropriate post-translational modifications, conferring a toxic gain of function, in addition to its non-functional property.	polyglutamine	49-63	huntingtin	Mus musculus	11-21
27992085-1	2017	Involuntary choreiform movements are clinical hallmark of Huntington"s disease, an autosomal dominant neurodegenerative disorder caused by an increased number of CAG trinucleotide repeats in the huntingtin gene.	trinucleotide	166-179	huntingtin	Mus musculus	195-205
27221610-1	2017	Huntington"s disease (HD) is a devastating neurodegenerative disease caused by cytosine-adenine-guanine trinucleotide repeat expansion in the huntingtin gene.	cytosine-adenine-guanine trinucleotide	79-117	huntingtin	Mus musculus	142-152
28270748-3	2017	This results in the production of mutant HTT protein with an increased stretch of glutamines near the N-terminus.	Glutamine	82-92	huntingtin	Mus musculus	41-44
27553284-1	2017	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by a polyglutamine expansion within the huntingtin (HTT) gene.	polyglutamine	80-93	huntingtin	Mus musculus	115-125
27553284-1	2017	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by a polyglutamine expansion within the huntingtin (HTT) gene.	polyglutamine	80-93	huntingtin	Mus musculus	127-130
28194040-1	2017	Huntington"s Disease (HD) is a neurodegenerative disease caused by poly-glutamine expansion in the Htt protein, resulting in Htt misfolding and cell death.	polyglutamine	67-81	huntingtin	Mus musculus	99-102
28194040-1	2017	Huntington"s Disease (HD) is a neurodegenerative disease caused by poly-glutamine expansion in the Htt protein, resulting in Htt misfolding and cell death.	polyglutamine	67-81	huntingtin	Mus musculus	125-128
28288000-1	2017	Expansion of polyglutamine stretch in the huntingtin (HTT) protein is a major cause of Huntington"s disease (HD).	polyglutamine	13-26	huntingtin	Mus musculus	42-52
28288000-1	2017	Expansion of polyglutamine stretch in the huntingtin (HTT) protein is a major cause of Huntington"s disease (HD).	polyglutamine	13-26	huntingtin	Mus musculus	54-57
28288000-2	2017	The polyglutamine part in HTT interacts with various proteins implicated in epigenetic regulation of genes, suggesting that mutant HTT may disturb the integrity of the epigenetic system.	polyglutamine	4-17	huntingtin	Mus musculus	26-29
28288000-2	2017	The polyglutamine part in HTT interacts with various proteins implicated in epigenetic regulation of genes, suggesting that mutant HTT may disturb the integrity of the epigenetic system.	polyglutamine	4-17	huntingtin	Mus musculus	131-134
28303108-1	2017	Huntington"s disease (HD) is a fatal neurodegenerative disorder, caused by a polyglutamine expansion in the huntingtin protein (HTT).	polyglutamine	77-90	huntingtin	Mus musculus	108-118
28303108-1	2017	Huntington"s disease (HD) is a fatal neurodegenerative disorder, caused by a polyglutamine expansion in the huntingtin protein (HTT).	polyglutamine	77-90	huntingtin	Mus musculus	128-131
28182673-1	2017	The aim of these studies was to demonstrate the therapeutic capacity of an antisense oligonucleotide with the sequence (CUG)7 targeting the expanded CAG repeat in huntingtin (HTT) mRNA in vivo in the R6/2 N-terminal fragment and Q175 knock-in Huntington"s disease (HD) mouse models.	Oligonucleotides	85-100	huntingtin	Mus musculus	163-173
28182673-1	2017	The aim of these studies was to demonstrate the therapeutic capacity of an antisense oligonucleotide with the sequence (CUG)7 targeting the expanded CAG repeat in huntingtin (HTT) mRNA in vivo in the R6/2 N-terminal fragment and Q175 knock-in Huntington"s disease (HD) mouse models.	Oligonucleotides	85-100	huntingtin	Mus musculus	175-178
28123081-2	2017	We showed previously that the histone deacetylase inhibitors (HDACIs) trichostatin A and sodium butyrate (SB) ameliorate mitochondrial function in cells expressing mutant huntingtin.	Butyric Acid	89-104	huntingtin	Mus musculus	171-181
28123081-2	2017	We showed previously that the histone deacetylase inhibitors (HDACIs) trichostatin A and sodium butyrate (SB) ameliorate mitochondrial function in cells expressing mutant huntingtin.	Butyric Acid	106-108	huntingtin	Mus musculus	171-181
27938392-4	2016	Polyglutamine expansion in huntingtin (Htt) causes aberrant accumulation of the aggregated protein and disrupts various cellular pathways including autophagy, a lysosomal degradation pathway, underlying the pathogenesis of Huntington"s disease (HD).	polyglutamine	0-13	huntingtin	Mus musculus	27-37
27913616-1	2017	Huntington"s disease (HD) is a neurodegenerative disorder caused by the expansion of a CAG trinucleotide repeat in exon 1 of the HTT gene.	trinucleotide	91-104	huntingtin	Mus musculus	129-132
27913616-9	2017	We also found that lines harboring a neomycin resistance cassette upstream of Htt showed reduced expansion frequency, indicative of a contributing role for sequences in cis, with the expanded repeat as modifiers of intergenerational instability.	Neomycin	37-45	huntingtin	Mus musculus	78-81
28007908-1	2017	Huntington"s disease (HD) is a dominantly inherited progressive neurodegenerative disorder caused by the accumulation of polyglutamine expanded mutant huntingtin as inclusion bodies primarily in the brain.	polyglutamine	121-134	huntingtin	Mus musculus	151-161
28007908-5	2017	Interestingly, topotecan treatment also significantly reduced insoluble mutant huntingtin load in the HD mouse brain.	Topotecan	15-24	huntingtin	Mus musculus	79-89
28007908-6	2017	Finally, we show that topotecan treatment to HD mouse not only inhibits the expression of transgenic mutant huntingtin, but also at the same time induces the expression of Ube3a, an ubiquitin ligase linked to the clearance of mutant huntingtin.	Topotecan	22-31	huntingtin	Mus musculus	108-118
28007908-6	2017	Finally, we show that topotecan treatment to HD mouse not only inhibits the expression of transgenic mutant huntingtin, but also at the same time induces the expression of Ube3a, an ubiquitin ligase linked to the clearance of mutant huntingtin.	Topotecan	22-31	huntingtin	Mus musculus	233-243
28976800-2	2017	The soluble mHTT has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, among which the one recognized by the polyQ antibody 3B5H10 is the most toxic due to unknown mechanisms.	polyglutamine	33-46	huntingtin	Mus musculus	12-16
28976800-2	2017	The soluble mHTT has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, among which the one recognized by the polyQ antibody 3B5H10 is the most toxic due to unknown mechanisms.	polyglutamine	48-53	huntingtin	Mus musculus	12-16
28211815-0	2017	Generation and Characterization of Knock-in Mouse Models Expressing Versions of Huntingtin with Either an N17 or a Combined PolyQ and Proline-Rich Region Deletion.	polyglutamine	124-129	huntingtin	Mus musculus	80-90
28211815-0	2017	Generation and Characterization of Knock-in Mouse Models Expressing Versions of Huntingtin with Either an N17 or a Combined PolyQ and Proline-Rich Region Deletion.	Proline	134-141	huntingtin	Mus musculus	80-90
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	polyglutamine	16-29	huntingtin	Mus musculus	53-63
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	polyglutamine	16-29	huntingtin	Mus musculus	73-76
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	polyglutamine	31-36	huntingtin	Mus musculus	53-63
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	polyglutamine	31-36	huntingtin	Mus musculus	73-76
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	17 amino acid	122-135	huntingtin	Mus musculus	53-63
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	17 amino acid	122-135	huntingtin	Mus musculus	73-76
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	Proline	167-174	huntingtin	Mus musculus	53-63
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	Proline	167-174	huntingtin	Mus musculus	73-76
28339401-5	2017	However, recent studies have also demonstrated that HTT participates in several cellular functions that are important for neuronal homeostasis and survival including sensing reactive oxygen species (ROS), DNA damage repair, and stress responses, in addition to its role in selective macroautophagy.	Reactive Oxygen Species	174-197	huntingtin	Mus musculus	52-55
28339401-5	2017	However, recent studies have also demonstrated that HTT participates in several cellular functions that are important for neuronal homeostasis and survival including sensing reactive oxygen species (ROS), DNA damage repair, and stress responses, in addition to its role in selective macroautophagy.	Reactive Oxygen Species	199-202	huntingtin	Mus musculus	52-55
27811172-2	2017	Impairment of cAMP/cGMP signaling by mutant huntingtin is hypothesized as the molecular mechanism underlying degeneration of MSNs.	Cyclic AMP	14-18	huntingtin	Mus musculus	44-54
27811172-2	2017	Impairment of cAMP/cGMP signaling by mutant huntingtin is hypothesized as the molecular mechanism underlying degeneration of MSNs.	Cyclic GMP	19-23	huntingtin	Mus musculus	44-54
27938392-4	2016	Polyglutamine expansion in huntingtin (Htt) causes aberrant accumulation of the aggregated protein and disrupts various cellular pathways including autophagy, a lysosomal degradation pathway, underlying the pathogenesis of Huntington"s disease (HD).	polyglutamine	0-13	huntingtin	Mus musculus	39-42
27525439-0	2016	Serine 421 regulates mutant huntingtin toxicity and clearance in mice.	Serine	0-6	huntingtin	Mus musculus	28-38
27225841-0	2016	Metformin Protects Cells from Mutant Huntingtin Toxicity Through Activation of AMPK and Modulation of Mitochondrial Dynamics.	Metformin	0-9	huntingtin	Mus musculus	37-47
27225841-6	2016	In this study, we showed that metformin rescued cells from mutant huntingtin (HTT)-induced toxicity, as indicated by reduced lactate dehydrogenase (LDH) release from cells and preserved ATP levels in cells expressing mutant HTT.	Metformin	30-39	huntingtin	Mus musculus	66-76
27225841-6	2016	In this study, we showed that metformin rescued cells from mutant huntingtin (HTT)-induced toxicity, as indicated by reduced lactate dehydrogenase (LDH) release from cells and preserved ATP levels in cells expressing mutant HTT.	Metformin	30-39	huntingtin	Mus musculus	78-81
27225841-6	2016	In this study, we showed that metformin rescued cells from mutant huntingtin (HTT)-induced toxicity, as indicated by reduced lactate dehydrogenase (LDH) release from cells and preserved ATP levels in cells expressing mutant HTT.	Metformin	30-39	huntingtin	Mus musculus	224-227
27225841-6	2016	In this study, we showed that metformin rescued cells from mutant huntingtin (HTT)-induced toxicity, as indicated by reduced lactate dehydrogenase (LDH) release from cells and preserved ATP levels in cells expressing mutant HTT.	Adenosine Triphosphate	186-189	huntingtin	Mus musculus	66-76
27225841-6	2016	In this study, we showed that metformin rescued cells from mutant huntingtin (HTT)-induced toxicity, as indicated by reduced lactate dehydrogenase (LDH) release from cells and preserved ATP levels in cells expressing mutant HTT.	Adenosine Triphosphate	186-189	huntingtin	Mus musculus	78-81
27225841-7	2016	Further mechanistic study indicated that metformin activated AMP-activated protein kinase (AMPK) and that inhibition of AMPK activation reduced its protective effects on mutant HTT toxicity, suggesting that AMPK mediates the protection of metformin in HD cells.	Metformin	239-248	huntingtin	Mus musculus	177-180
27821553-1	2016	Huntington"s disease (HD) is a rare genetic disease caused by expanded polyglutamine repeats in the huntingtin protein resulting in selective neuronal loss.	polyglutamine	71-84	huntingtin	Mus musculus	100-110
27820862-1	2016	Huntington s disease (HD) is a hereditary neurodegenerative disease resulting from an expanded polyglutamine sequence (poly-Q) in the protein huntingtin (HTT).	polyglutamine	95-108	huntingtin	Mus musculus	142-152
27820862-1	2016	Huntington s disease (HD) is a hereditary neurodegenerative disease resulting from an expanded polyglutamine sequence (poly-Q) in the protein huntingtin (HTT).	polyglutamine	95-108	huntingtin	Mus musculus	154-157
27820862-1	2016	Huntington s disease (HD) is a hereditary neurodegenerative disease resulting from an expanded polyglutamine sequence (poly-Q) in the protein huntingtin (HTT).	poly-q	119-125	huntingtin	Mus musculus	142-152
27820862-1	2016	Huntington s disease (HD) is a hereditary neurodegenerative disease resulting from an expanded polyglutamine sequence (poly-Q) in the protein huntingtin (HTT).	poly-q	119-125	huntingtin	Mus musculus	154-157
27529534-1	2016	Huntington"s disease (HD) is caused by a CAG-repeat encoding a polyglutamine (polyQ) tract in the huntingtin protein.	polyglutamine	78-83	huntingtin	Mus musculus	98-108
27721240-3	2016	Here, we have shown that a locked nucleic acid-modified antisense oligonucleotide complementary to the CAG repeat (LNA-CTG) preferentially binds to mutant HTT without affecting HTT mRNA or protein levels.	Oligonucleotides	66-81	huntingtin	Mus musculus	155-158
27721240-3	2016	Here, we have shown that a locked nucleic acid-modified antisense oligonucleotide complementary to the CAG repeat (LNA-CTG) preferentially binds to mutant HTT without affecting HTT mRNA or protein levels.	Oligonucleotides	66-81	huntingtin	Mus musculus	177-180
27466181-0	2016	Huntingtin N17 domain is a reactive oxygen species sensor regulating huntingtin phosphorylation and localization.	oxygen species	36-50	huntingtin	Mus musculus	69-79
27466181-2	2016	In Huntington"s disease (HD), mutant huntingtin is hypo-phosphorylated at serines 13 and 16 within N17, and increasing N17 phosphorylation has been shown to be protective in HD mouse models.	Serine	74-81	huntingtin	Mus musculus	37-47
27466181-5	2016	Here, we demonstrate that huntingtin localization can be specifically affected by reactive oxygen species (ROS) stress.	Reactive Oxygen Species	82-105	huntingtin	Mus musculus	26-36
27466181-5	2016	Here, we demonstrate that huntingtin localization can be specifically affected by reactive oxygen species (ROS) stress.	Reactive Oxygen Species	107-110	huntingtin	Mus musculus	26-36
27466181-10	2016	This ability of huntingtin to sense ROS levels at the ER, with phosphorylation and nuclear localization as a response, suggests that ROS stress due to aging could be a critical molecular trigger of huntingtin functions and dysfunctions in HD and may explain the age-onset nature of the disorder.	Reactive Oxygen Species	36-39	huntingtin	Mus musculus	16-26
27466181-10	2016	This ability of huntingtin to sense ROS levels at the ER, with phosphorylation and nuclear localization as a response, suggests that ROS stress due to aging could be a critical molecular trigger of huntingtin functions and dysfunctions in HD and may explain the age-onset nature of the disorder.	Reactive Oxygen Species	36-39	huntingtin	Mus musculus	198-208
27466181-10	2016	This ability of huntingtin to sense ROS levels at the ER, with phosphorylation and nuclear localization as a response, suggests that ROS stress due to aging could be a critical molecular trigger of huntingtin functions and dysfunctions in HD and may explain the age-onset nature of the disorder.	Reactive Oxygen Species	133-136	huntingtin	Mus musculus	16-26
27466181-10	2016	This ability of huntingtin to sense ROS levels at the ER, with phosphorylation and nuclear localization as a response, suggests that ROS stress due to aging could be a critical molecular trigger of huntingtin functions and dysfunctions in HD and may explain the age-onset nature of the disorder.	Reactive Oxygen Species	133-136	huntingtin	Mus musculus	198-208
27751235-2	2016	In Huntington"s disease (HD), neurotoxicity correlates with an increased aggregation propensity of a polyglutamine (polyQ) expansion in exon 1 of mutant huntingtin protein (mHtt).	polyglutamine	101-114	huntingtin	Mus musculus	173-177
27751235-2	2016	In Huntington"s disease (HD), neurotoxicity correlates with an increased aggregation propensity of a polyglutamine (polyQ) expansion in exon 1 of mutant huntingtin protein (mHtt).	polyglutamine	116-121	huntingtin	Mus musculus	173-177
27751235-3	2016	Here we establish how the domains flanking the polyQ tract shape the mHtt conformational landscape in vitro and in neurons.	polyglutamine	47-52	huntingtin	Mus musculus	69-73
27751235-8	2016	Linking mHtt structural properties to its neuronal proteostasis should inform new strategies for neuroprotection in polyQ-expansion diseases.	polyglutamine	116-121	huntingtin	Mus musculus	8-12
27739513-5	2016	Co-aggregation between FUS/TLS and mutant huntingtin resulted in the depletion of free FUS/TLS protein in HD mice that was detected as a monomer in SDS-PAGE analysis.	Sodium Dodecyl Sulfate	148-151	huntingtin	Mus musculus	42-52
27611938-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a polyglutamine-repeat expansion in the huntingtin protein.	polyglutamine	82-95	huntingtin	Mus musculus	120-130
27525439-1	2016	Huntington"s disease (HD) is a progressive, adult-onset neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the N-terminal region of the protein huntingtin (HTT).	polyglutamine	94-107	huntingtin	Mus musculus	166-176
27525439-1	2016	Huntington"s disease (HD) is a progressive, adult-onset neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the N-terminal region of the protein huntingtin (HTT).	polyglutamine	94-107	huntingtin	Mus musculus	178-181
27525439-1	2016	Huntington"s disease (HD) is a progressive, adult-onset neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the N-terminal region of the protein huntingtin (HTT).	polyglutamine	109-114	huntingtin	Mus musculus	166-176
27525439-1	2016	Huntington"s disease (HD) is a progressive, adult-onset neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the N-terminal region of the protein huntingtin (HTT).	polyglutamine	109-114	huntingtin	Mus musculus	178-181
27525439-3	2016	HTT has a highly conserved Akt phosphorylation site at serine 421, and prior work in HD models found that phosphorylation at S421 (S421-P) diminishes the toxicity of mutant HTT (mHTT) fragments in neuronal cultures.	Serine	55-61	huntingtin	Mus musculus	0-3
27525439-3	2016	HTT has a highly conserved Akt phosphorylation site at serine 421, and prior work in HD models found that phosphorylation at S421 (S421-P) diminishes the toxicity of mutant HTT (mHTT) fragments in neuronal cultures.	Serine	55-61	huntingtin	Mus musculus	173-176
27525439-6	2016	Specifically, we mutated the human mHTT gene within a BAC to express either an aspartic acid or an alanine at position 421, mimicking tonic phosphorylation (mHTT-S421D mice) or preventing phosphorylation (mHTT-S421A mice), respectively.	Aspartic Acid	79-92	huntingtin	Mus musculus	35-39
27525439-6	2016	Specifically, we mutated the human mHTT gene within a BAC to express either an aspartic acid or an alanine at position 421, mimicking tonic phosphorylation (mHTT-S421D mice) or preventing phosphorylation (mHTT-S421A mice), respectively.	Alanine	99-106	huntingtin	Mus musculus	35-39
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	trinucleotide	60-73	huntingtin	Mus musculus	112-122
27559163-0	2016	Mutant Huntingtin Impairs BDNF Release from Astrocytes by Disrupting Conversion of Rab3a-GTP into Rab3a-GDP.	Guanosine Diphosphate	104-107	huntingtin	Mus musculus	7-17
27559163-15	2016	We found that mutant huntingtin protein (mHtt) at the endogenous level decreases BDNF secretion from astrocytes by disrupting the conversion of GTP-Rab3a into GDP-Rab3a and that overexpressing Rab3a can rescue this deficient BDNF release and early neuropathology in HD knock-in mouse brain.	Guanosine Triphosphate	144-147	huntingtin	Mus musculus	21-31
27516062-2	2016	Using an epigenetic pathway-targeted drug screen, we report that inhibitors of DNA methyltransferases (DNMTs), decitabine and FdCyd, block mutant huntingtin (Htt)-induced toxicity in primary cortical and striatal neurons.	Decitabine	111-121	huntingtin	Mus musculus	146-156
27516062-2	2016	Using an epigenetic pathway-targeted drug screen, we report that inhibitors of DNA methyltransferases (DNMTs), decitabine and FdCyd, block mutant huntingtin (Htt)-induced toxicity in primary cortical and striatal neurons.	Decitabine	111-121	huntingtin	Mus musculus	158-161
27516062-5	2016	Accordingly, the Bdnf promoter exhibited aberrant cytosine methylation in mutant Htt-expressing cortical neurons.	Cytosine	50-58	huntingtin	Mus musculus	81-84
27484239-4	2016	Functional domain mapping based on super-resolution imaging reveals an unexpected role of aromatic amino acids in promoting protein-mHtt aggregate interactions.	Amino Acids, Aromatic	90-110	huntingtin	Mus musculus	132-136
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	trinucleotide	60-73	huntingtin	Mus musculus	124-127
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	trinucleotide	60-73	huntingtin	Mus musculus	192-195
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	polyglutamine	216-229	huntingtin	Mus musculus	112-122
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	polyglutamine	216-229	huntingtin	Mus musculus	124-127
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	polyglutamine	216-229	huntingtin	Mus musculus	192-195
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	polyglutamine	231-236	huntingtin	Mus musculus	112-122
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	polyglutamine	231-236	huntingtin	Mus musculus	124-127
27107943-1	2016	Huntington"s disease (HD) is caused by the expansion of CAG trinucleotide repeats in exon 1 of HD gene encoding huntingtin (Htt), which is characterized by aggregation and formation of mutant Htt containing expanded polyglutamine (polyQ) repeats.	polyglutamine	231-236	huntingtin	Mus musculus	192-195
27107943-8	2016	Further analysis revealed that WWP1 ubiquitinated mHtt at an atypical position of Lys-63, which may have inhibited degradation of mutant Htt through the ubiquitin-proteasome pathway.	Lysine	82-85	huntingtin	Mus musculus	51-54
27147652-1	2016	UNLABELLED: Huntington"s disease (HD) is a heritable neurodegenerative disorder caused by expansion of CAG (glutamine) repeats in the HTT gene.	Glutamine	108-117	huntingtin	Mus musculus	134-137
27002149-0	2016	An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation.	polyglutamine	113-126	huntingtin	Mus musculus	56-66
27258586-1	2016	BACKGROUND: Huntington"s disease (HD) is a rare, incurable neurodegenerative disorder caused by a CAG trinucleotide expansion with the first exon of the huntingtin gene.	trinucleotide	102-115	huntingtin	Mus musculus	153-163
27033979-8	2016	Increased cytokine release in YAC128 microglia can be blocked by cannabinoid activation or by mutant huntingtin knockdown with anti-sense oligonucleotide treatment.	Oligonucleotides	138-153	huntingtin	Mus musculus	101-111
26321735-6	2016	When tested in the Hdh(Q111) mouse model of HD, the DMTP and DNMTP tasks revealed significant deficits in reversal learning.	dmtp	52-56	huntingtin	Mus musculus	19-22
26321735-6	2016	When tested in the Hdh(Q111) mouse model of HD, the DMTP and DNMTP tasks revealed significant deficits in reversal learning.	dnmtp	61-66	huntingtin	Mus musculus	19-22
27203582-1	2016	The Huntington"s disease (HD) protein, huntingtin (HTT), is a large protein consisting of 3144 amino acids and has conserved N-terminal sequences that are followed by a polyglutamine (polyQ) repeat.	polyglutamine	169-182	huntingtin	Mus musculus	39-49
27203582-1	2016	The Huntington"s disease (HD) protein, huntingtin (HTT), is a large protein consisting of 3144 amino acids and has conserved N-terminal sequences that are followed by a polyglutamine (polyQ) repeat.	polyglutamine	169-182	huntingtin	Mus musculus	51-54
27203582-1	2016	The Huntington"s disease (HD) protein, huntingtin (HTT), is a large protein consisting of 3144 amino acids and has conserved N-terminal sequences that are followed by a polyglutamine (polyQ) repeat.	polyglutamine	184-189	huntingtin	Mus musculus	39-49
27203582-1	2016	The Huntington"s disease (HD) protein, huntingtin (HTT), is a large protein consisting of 3144 amino acids and has conserved N-terminal sequences that are followed by a polyglutamine (polyQ) repeat.	polyglutamine	184-189	huntingtin	Mus musculus	51-54
27203582-10	2016	Thus, the N-terminal HTT region may not be essential for the survival of developing neurons, but when carrying a large polyQ repeat, can cause selective neuropathology.	polyglutamine	119-124	huntingtin	Mus musculus	21-24
27203582-11	2016	These findings imply a possible therapeutic benefit of removing the N-terminal region of HTT containing the polyQ repeat to treat the neurodegeneration in HD.	polyglutamine	108-113	huntingtin	Mus musculus	89-92
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	Mus musculus	187-191
26920069-1	2016	Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	51-64	huntingtin	Mus musculus	86-96
26920069-1	2016	Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	51-64	huntingtin	Mus musculus	98-101
26920069-1	2016	Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	66-71	huntingtin	Mus musculus	86-96
26920069-1	2016	Huntington"s disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein.	polyglutamine	66-71	huntingtin	Mus musculus	98-101
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	Mus musculus	187-191
26371883-1	2016	Huntington"s disease (HD) is caused by an expansion of cytosine-adenine-guanine (CAG) repeats within the coding region of the HD gene, which expresses the protein huntingtin and is characterized by selective degeneration of specific neuronal populations, mainly in the striatum and the cortex.	cytosine-adenine-guanine	55-79	huntingtin	Mus musculus	163-173
27141414-5	2016	Results from a second model of Huntington"s disease, the Hdh (Q111) knock-in mouse, confirm olesoxime"s calpain-suppressing effects and support the therapeutic value of olesoxime for Huntington"s disease and other disorders involving calpain overactivation.	olesoxime	92-101	huntingtin	Mus musculus	57-60
26912634-1	2016	Huntington"s disease is an autosomal dominant neurodegenerative disease caused by abnormal polyglutamine expansion in huntingtin (Exp-HTT) leading to degeneration of striatal neurons.	polyglutamine	91-104	huntingtin	Mus musculus	118-128
26681807-6	2016	Similarly, AMPK activation using genetic manipulation and low-dose metformin treatment protects mouse striatal cells expressing full-length mutant Htt (mHtt), counteracting their vulnerability to stress, with reduction of soluble mHtt levels by metformin and compensation of cytotoxicity by AMPKalpha1.	Metformin	67-76	huntingtin	Mus musculus	147-150
26681807-6	2016	Similarly, AMPK activation using genetic manipulation and low-dose metformin treatment protects mouse striatal cells expressing full-length mutant Htt (mHtt), counteracting their vulnerability to stress, with reduction of soluble mHtt levels by metformin and compensation of cytotoxicity by AMPKalpha1.	Metformin	67-76	huntingtin	Mus musculus	152-156
26681807-6	2016	Similarly, AMPK activation using genetic manipulation and low-dose metformin treatment protects mouse striatal cells expressing full-length mutant Htt (mHtt), counteracting their vulnerability to stress, with reduction of soluble mHtt levels by metformin and compensation of cytotoxicity by AMPKalpha1.	Metformin	67-76	huntingtin	Mus musculus	230-234
26681807-6	2016	Similarly, AMPK activation using genetic manipulation and low-dose metformin treatment protects mouse striatal cells expressing full-length mutant Htt (mHtt), counteracting their vulnerability to stress, with reduction of soluble mHtt levels by metformin and compensation of cytotoxicity by AMPKalpha1.	Metformin	245-254	huntingtin	Mus musculus	230-234
26783111-1	2016	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by expansion of CAG trinucleotide repeats in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	92-95	huntingtin	Mus musculus	125-135
26783111-1	2016	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by expansion of CAG trinucleotide repeats in the huntingtin gene.	trinucleotide	96-109	huntingtin	Mus musculus	125-135
26859386-1	2016	Huntington"s disease (HD) is caused by an expansion of the trinucleotide poly (CAG) tract located in exon 1 of the huntingtin (Htt) gene leading to progressive neurodegeneration in selected brain regions, and associated functional impairments in motor, cognitive, and psychiatric domains.	trinucleotide	59-72	huntingtin	Mus musculus	115-125
26859386-1	2016	Huntington"s disease (HD) is caused by an expansion of the trinucleotide poly (CAG) tract located in exon 1 of the huntingtin (Htt) gene leading to progressive neurodegeneration in selected brain regions, and associated functional impairments in motor, cognitive, and psychiatric domains.	trinucleotide	59-72	huntingtin	Mus musculus	127-130
26859386-1	2016	Huntington"s disease (HD) is caused by an expansion of the trinucleotide poly (CAG) tract located in exon 1 of the huntingtin (Htt) gene leading to progressive neurodegeneration in selected brain regions, and associated functional impairments in motor, cognitive, and psychiatric domains.	poly (cag)	73-83	huntingtin	Mus musculus	115-125
26859386-1	2016	Huntington"s disease (HD) is caused by an expansion of the trinucleotide poly (CAG) tract located in exon 1 of the huntingtin (Htt) gene leading to progressive neurodegeneration in selected brain regions, and associated functional impairments in motor, cognitive, and psychiatric domains.	poly (cag)	73-83	huntingtin	Mus musculus	127-130
26371883-1	2016	Huntington"s disease (HD) is caused by an expansion of cytosine-adenine-guanine (CAG) repeats within the coding region of the HD gene, which expresses the protein huntingtin and is characterized by selective degeneration of specific neuronal populations, mainly in the striatum and the cortex.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	81-84	huntingtin	Mus musculus	163-173
26796203-2	2016	It is caused by a polyglutamine expansion in the huntingtin (htt) protein, which then leads to neurodegeneration that span both the central and peripheral nervous system.	polyglutamine	18-31	huntingtin	Mus musculus	49-59
26796203-2	2016	It is caused by a polyglutamine expansion in the huntingtin (htt) protein, which then leads to neurodegeneration that span both the central and peripheral nervous system.	polyglutamine	18-31	huntingtin	Mus musculus	61-64
26581643-4	2016	In this study we employed 2D SDS-PAGE/MALDI-MS coupled with 2D-DIGE and real-time PCR experiments of an array of genes focused to HD pathway to determine altered protein and gene expressions in STHdh(Q111)/Hdh(Q111) cells, a cell model of HD and compared with STHdh(Q7)/Hdh(Q7) cells, its wild type counterpart.	Sodium Dodecyl Sulfate	29-32	huntingtin	Mus musculus	196-199
26740655-18	2016	We use it to demonstrate that sensitization of type 1 inositol (1,4,5)-trisphosphate receptors by mHtt, which depletes endoplasmic reticulum calcium, contributes to synaptotoxic enhancement of STIM2-dependent store-operated calcium (SOC) entry.	(1,4,5)-trisphosphate	63-84	huntingtin	Mus musculus	98-102
26740655-18	2016	We use it to demonstrate that sensitization of type 1 inositol (1,4,5)-trisphosphate receptors by mHtt, which depletes endoplasmic reticulum calcium, contributes to synaptotoxic enhancement of STIM2-dependent store-operated calcium (SOC) entry.	Calcium	141-148	huntingtin	Mus musculus	98-102
26740655-18	2016	We use it to demonstrate that sensitization of type 1 inositol (1,4,5)-trisphosphate receptors by mHtt, which depletes endoplasmic reticulum calcium, contributes to synaptotoxic enhancement of STIM2-dependent store-operated calcium (SOC) entry.	Calcium	224-231	huntingtin	Mus musculus	98-102
26581643-23	2016	One of this was Hypk, a Htt-interacting chaperone protein with the ability to solubilize mHtt aggregated structures in cell lines.	mhtt	89-93	huntingtin	Mus musculus	24-27
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	82-85	huntingtin	Mus musculus	124-134
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	82-85	huntingtin	Mus musculus	136-139
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	82-85	huntingtin	Mus musculus	190-193
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	trinucleotide	86-99	huntingtin	Mus musculus	124-134
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	trinucleotide	86-99	huntingtin	Mus musculus	136-139
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	trinucleotide	86-99	huntingtin	Mus musculus	190-193
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	polyglutamine	163-176	huntingtin	Mus musculus	124-134
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	polyglutamine	163-176	huntingtin	Mus musculus	136-139
26642438-1	2016	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene, which encodes a polyglutamine tract in the HTT protein.	polyglutamine	163-176	huntingtin	Mus musculus	190-193
26485309-2	2016	HD is caused by an expanded CAG repeat in the first exon of the HTT gene, resulting in an expanded polyglutamine section.	polyglutamine	99-112	huntingtin	Mus musculus	64-67
26254860-4	2015	T1-11 exerted a therapeutic effect on HD transgenic mouse by decreasing protein level of polyglutamine-expanded huntingtin in the striatum.	t1-11	0-5	huntingtin	Mus musculus	112-122
26691307-1	2015	Huntington"s disease is the result of a long polyglutamine tract in the gene encoding huntingtin protein, which in turn causes a large number of cellular changes and ultimately results in neurodegeneration of striatal neurons.	polyglutamine	45-58	huntingtin	Mus musculus	86-96
26691307-8	2015	Both of the cell lines expressing huntingtin with 111 glutamines showed a large reduction in nearly all of the peptides detected in the cells, relative to levels of these peptides in cells homozygous for 7 glutamines.	Glutamine	54-64	huntingtin	Mus musculus	34-44
26691307-8	2015	Both of the cell lines expressing huntingtin with 111 glutamines showed a large reduction in nearly all of the peptides detected in the cells, relative to levels of these peptides in cells homozygous for 7 glutamines.	Glutamine	206-216	huntingtin	Mus musculus	34-44
26691307-10	2015	Taken together, these results support the hypothesis that proteasome function is impaired by the expression of huntingtin protein containing long polyglutamine tracts.	polyglutamine	146-159	huntingtin	Mus musculus	111-121
26192473-1	2015	Huntington"s Disease (HD) is a neurodegenerative disorder that results from the abnormal expansion of poly-glutamine (polyQ) repeats in the Huntingtin (HTT) gene.	polyglutamine	102-116	huntingtin	Mus musculus	152-155
26192473-1	2015	Huntington"s Disease (HD) is a neurodegenerative disorder that results from the abnormal expansion of poly-glutamine (polyQ) repeats in the Huntingtin (HTT) gene.	polyglutamine	118-123	huntingtin	Mus musculus	152-155
26254860-4	2015	T1-11 exerted a therapeutic effect on HD transgenic mouse by decreasing protein level of polyglutamine-expanded huntingtin in the striatum.	polyglutamine	89-102	huntingtin	Mus musculus	112-122
26635623-0	2015	Both Orai1 and TRPC1 are Involved in Excessive Store-Operated Calcium Entry in Striatal Neurons Expressing Mutant Huntingtin Exon 1.	Calcium	62-69	huntingtin	Mus musculus	114-124
26586297-3	2015	The results of the present study demonstrated that mHtt aggregation in the nucleus was altered by the activity of multidrug resistance protein 1 (MDR1), which was experimentally modulated by verapamil, siRNA and an expression vector.	Verapamil	191-200	huntingtin	Mus musculus	51-55
26586297-5	2015	When they were treated with verapamil, R6/2 mice showed a progressive decline in rotarod performance and increased mHtt aggregation in the brain.	Verapamil	28-37	huntingtin	Mus musculus	115-119
26586297-7	2015	When MDR1 activity in cells was decreased by verapamil or siRNA, mHtt aggregation in the nuclei increased, whereas the induction of MDR1 resulted in a decrease in mHtt aggregation.	Verapamil	45-54	huntingtin	Mus musculus	65-69
26153070-0	2015	Quercetin improves the activity of the ubiquitin-proteasomal system in 150Q mutated huntingtin-expressing cells but exerts detrimental effects on neuronal survivability.	Quercetin	0-9	huntingtin	Mus musculus	84-94
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	trinucleotide	41-54	huntingtin	Mus musculus	73-83
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	trinucleotide	41-54	huntingtin	Mus musculus	90-93
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	trinucleotide	41-54	huntingtin	Mus musculus	157-167
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	trinucleotide	41-54	huntingtin	Mus musculus	177-181
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	polyglutamine	127-140	huntingtin	Mus musculus	73-83
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	polyglutamine	127-140	huntingtin	Mus musculus	90-93
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	polyglutamine	127-140	huntingtin	Mus musculus	157-167
26664998-1	2015	Huntington"s disease (HD) is caused by a trinucleotide CAG repeat in the huntingtin gene (HTT) that results in expression of a polyglutamine-expanded mutant huntingtin protein (mHTT).	polyglutamine	127-140	huntingtin	Mus musculus	177-181
26664998-4	2015	There is evidence for aberrant thiol oxidation within mHTT and other proteins in HD models.	Sulfhydryl Compounds	31-36	huntingtin	Mus musculus	54-58
26153070-4	2015	Mutated Htt (mHtt)-induced reduction in proteasomal activity of the ubiquitin-proteasomal system (UPS) was significantly attenuated by 20 microM quercetin.	Quercetin	145-154	huntingtin	Mus musculus	8-11
26153070-4	2015	Mutated Htt (mHtt)-induced reduction in proteasomal activity of the ubiquitin-proteasomal system (UPS) was significantly attenuated by 20 microM quercetin.	Quercetin	145-154	huntingtin	Mus musculus	13-17
26153070-6	2015	Our results imply that the neuroprotective effect of quercetin arises out of the upregulation of UPS activity, which causes a decrease in the number of mHtt aggregate-harboring cells.	Quercetin	53-62	huntingtin	Mus musculus	152-156
26048156-1	2015	Huntington"s disease (HD) is caused by an expansion of glutamine repeats in the huntingtin protein (mHtt) that invokes early and prominent damage of the striatum, a region that controls motor behaviors.	Glutamine	55-64	huntingtin	Mus musculus	80-90
25989602-1	2015	Huntington"s disease (HD) is a neurodegenerative disorder caused by the toxic expansion of polyglutamine in the Huntingtin (HTT) protein.	polyglutamine	91-104	huntingtin	Mus musculus	112-122
26122704-12	2015	However, NBI-641449 treatment reduced the huntingtin protein aggregates in the cortex of YAC128 mice.	nbi-641449	9-19	huntingtin	Mus musculus	42-52
26122704-12	2015	However, NBI-641449 treatment reduced the huntingtin protein aggregates in the cortex of YAC128 mice.	yac128	89-95	huntingtin	Mus musculus	42-52
26153070-8	2015	These results suggest that, although quercetin at a low dose protects against mHtt-mediated cell death, higher doses are toxic to the cells, clearly demarcating a narrow therapeutic window for this dietary flavonoid.	Quercetin	37-46	huntingtin	Mus musculus	78-82
26153070-8	2015	These results suggest that, although quercetin at a low dose protects against mHtt-mediated cell death, higher doses are toxic to the cells, clearly demarcating a narrow therapeutic window for this dietary flavonoid.	Flavonoids	206-215	huntingtin	Mus musculus	78-82
25989602-1	2015	Huntington"s disease (HD) is a neurodegenerative disorder caused by the toxic expansion of polyglutamine in the Huntingtin (HTT) protein.	polyglutamine	91-104	huntingtin	Mus musculus	124-127
26225560-5	2015	We found that BBR can reduce the accumulation of mutant huntingtin in cultured cells.	Berberine	14-17	huntingtin	Mus musculus	56-66
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	Mus musculus	74-84
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	Mus musculus	74-84
26037141-5	2015	Here we show that prefibrillar HTT oligomers are remarkably stable and are potent seeds of polyglutamine amyloid formation.	polyglutamine	91-104	huntingtin	Mus musculus	31-34
25556834-1	2015	Huntington"s disease (HD) is caused by a polyglutamine tract expansion in huntingtin (HTT).	polyglutamine	41-54	huntingtin	Mus musculus	74-84
25574027-1	2015	The CAG repeat expansion in the Huntington"s disease gene HTT extends a polyglutamine tract in mutant huntingtin that enhances its ability to facilitate polycomb repressive complex 2 (PRC2).	polyglutamine	72-85	huntingtin	Mus musculus	58-61
25574027-1	2015	The CAG repeat expansion in the Huntington"s disease gene HTT extends a polyglutamine tract in mutant huntingtin that enhances its ability to facilitate polycomb repressive complex 2 (PRC2).	polyglutamine	72-85	huntingtin	Mus musculus	102-112
25859666-1	2015	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	90-93	huntingtin	Mus musculus	132-142
25859666-1	2015	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin gene.	trinucleotide	94-107	huntingtin	Mus musculus	132-142
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	trinucleotide	60-73	huntingtin	Mus musculus	88-98
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	trinucleotide	60-73	huntingtin	Mus musculus	100-103
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	trinucleotide	60-73	huntingtin	Mus musculus	153-163
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	polyglutamine	211-224	huntingtin	Mus musculus	88-98
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	polyglutamine	211-224	huntingtin	Mus musculus	100-103
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	polyglutamine	211-224	huntingtin	Mus musculus	153-163
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	polyglutamine	226-233	huntingtin	Mus musculus	88-98
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	polyglutamine	226-233	huntingtin	Mus musculus	100-103
25505248-2	2015	Hereditary HD is primarily caused by the expansion of a CAG trinucleotide repeat in the huntingtin (Htt) gene, which results in the production of mutant huntingtin protein (mHTT) with an expanded amino-terminal polyglutamine (poly(Q)) stretch.	polyglutamine	226-233	huntingtin	Mus musculus	153-163
25963273-5	2015	We speculate that this may happen because of mHtt-mediated sequestration of free fatty acids thereby increasing resistance of mitochondria to Ca(2+)-induced damage.	Fatty Acids, Nonesterified	76-92	huntingtin	Mus musculus	45-49
25963273-10	2015	We propose that this may happen due to mHtt-mediated sequestration of free fatty acids thereby increasing resistance of mitochondria to Ca(2+)-induced damage.	Fatty Acids, Nonesterified	70-86	huntingtin	Mus musculus	39-43
25732261-15	2015	IHC demonstrated microgliosis in and around the injection site and mHTT-positive inclusions in serotonin-producing neurons and a small percentage of astrocytes in animals injected with N171-82Q compared to controls.	Serotonin	95-104	huntingtin	Mus musculus	67-71
25931812-1	2015	Huntington"s disease (HD) is caused by a genetic mutation that results in polyglutamine expansion in the N-terminal regions of huntingtin.	polyglutamine	74-87	huntingtin	Mus musculus	127-137
25931812-2	2015	As a result, this polyQ expansion leads to the misfolding and aggregation of mutant huntingtin as well as age-dependent neurodegeneration.	polyglutamine	18-23	huntingtin	Mus musculus	84-94
25661181-2	2015	Recent studies suggest the first 17-amino-acid domain (N17) of mutant huntingtin (mHTT) mediates its nuclear exclusion in cultured cells.	17-amino-acid	33-46	huntingtin	Mus musculus	70-80
25305080-1	2015	Huntington"s disease (HD) is a dominantly inherited genetic disease caused by mutant huntingtin (htt) protein with expanded polyglutamine (polyQ) tracts.	polyglutamine	124-137	huntingtin	Mus musculus	85-95
25305080-1	2015	Huntington"s disease (HD) is a dominantly inherited genetic disease caused by mutant huntingtin (htt) protein with expanded polyglutamine (polyQ) tracts.	polyglutamine	124-137	huntingtin	Mus musculus	97-100
25305080-1	2015	Huntington"s disease (HD) is a dominantly inherited genetic disease caused by mutant huntingtin (htt) protein with expanded polyglutamine (polyQ) tracts.	polyglutamine	139-144	huntingtin	Mus musculus	85-95
25305080-1	2015	Huntington"s disease (HD) is a dominantly inherited genetic disease caused by mutant huntingtin (htt) protein with expanded polyglutamine (polyQ) tracts.	polyglutamine	139-144	huntingtin	Mus musculus	97-100
25556834-1	2015	Huntington"s disease (HD) is caused by a polyglutamine tract expansion in huntingtin (HTT).	polyglutamine	41-54	huntingtin	Mus musculus	86-89
26203463-14	2015	Morphological and electrophysiological alterations, in conjunction with the presence of mutant huntingtin in LCIs, could explain impaired ACh release in HD mouse models.	Acetylcholine	138-141	huntingtin	Mus musculus	95-105
25205109-1	2015	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by polyglutamine expansions in the amino-terminal region of the huntingtin (Htt) protein.	polyglutamine	88-101	huntingtin	Mus musculus	149-159
25205109-1	2015	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by polyglutamine expansions in the amino-terminal region of the huntingtin (Htt) protein.	polyglutamine	88-101	huntingtin	Mus musculus	161-164
26397898-8	2015	We report that treatment with methylene blue (MB), a protective compound in mitochondria-related diseases, partially protects the fly"s heart against mHtt-induced toxicity, but does not rescue neuronal or glial phenotypes in other fly models of HD.	Methylene Blue	30-44	huntingtin	Mus musculus	150-154
26397898-8	2015	We report that treatment with methylene blue (MB), a protective compound in mitochondria-related diseases, partially protects the fly"s heart against mHtt-induced toxicity, but does not rescue neuronal or glial phenotypes in other fly models of HD.	Methylene Blue	46-48	huntingtin	Mus musculus	150-154
26397899-2	2015	Huntingtin associates with membranes and can interact directly with glycerophospholipids in membranes.	Glycerophospholipids	68-88	huntingtin	Mus musculus	0-10
25332397-1	2014	Huntington"s disease is a fatal neurodegenerative disease caused by polyglutamine-expansion in huntingtin (HTT).	polyglutamine	68-81	huntingtin	Mus musculus	95-105
25467848-1	2015	BACKGROUND: PBT2 is a metal protein-attenuating compound that might reduce metal-induced aggregation of mutant huntingtin and has prolonged survival in a mouse model of Huntington"s disease.	Metals	22-27	huntingtin	Mus musculus	111-121
25467848-1	2015	BACKGROUND: PBT2 is a metal protein-attenuating compound that might reduce metal-induced aggregation of mutant huntingtin and has prolonged survival in a mouse model of Huntington"s disease.	Metals	75-80	huntingtin	Mus musculus	111-121
25160573-1	2015	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in the amino-terminal region of the huntingtin protein (htt), leading to motor dysfunction, cognitive decline, psychiatric alterations, and death.	polyglutamine	90-103	huntingtin	Mus musculus	150-168
25160573-1	2015	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in the amino-terminal region of the huntingtin protein (htt), leading to motor dysfunction, cognitive decline, psychiatric alterations, and death.	polyglutamine	90-103	huntingtin	Mus musculus	170-173
25160573-9	2015	Thus, CDPPB is a potential drug to treat HD, preventing neuronal cell loss and htt aggregate formation and delaying HD symptoms.	3-cyano-N-(1,3-diphenyl-1H-pyrazol-5-yl)benzamide	6-11	huntingtin	Mus musculus	79-82
25871323-1	2015	BACKGROUND: Huntington"s disease (HD) is a late-onset fatal neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene coding for the protein huntingtin and is characterised by progressive motor, psychiatric and cognitive decline.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	99-102	huntingtin	Mus musculus	169-179
25871323-1	2015	BACKGROUND: Huntington"s disease (HD) is a late-onset fatal neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the gene coding for the protein huntingtin and is characterised by progressive motor, psychiatric and cognitive decline.	trinucleotide	103-116	huntingtin	Mus musculus	169-179
25035419-0	2014	Phosphorodiamidate morpholino oligomers suppress mutant huntingtin expression and attenuate neurotoxicity.	phosphorodiamidate morpholino	0-29	huntingtin	Mus musculus	56-66
25035419-1	2014	Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	70-73	huntingtin	Mus musculus	112-122
25035419-1	2014	Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	70-73	huntingtin	Mus musculus	124-127
25035419-1	2014	Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene.	trinucleotide	74-87	huntingtin	Mus musculus	112-122
25035419-1	2014	Huntington"s disease (HD) is a neurodegenerative disorder caused by a CAG trinucleotide repeat expansion in the huntingtin (HTT) gene.	trinucleotide	74-87	huntingtin	Mus musculus	124-127
25035419-4	2014	Antisense oligonucleotides (ASOs) targeted to the CAG repeat region of HTT transcripts have been of particular interest due to their potential capacity to discriminate between normal and mutant HTT transcripts.	Oligonucleotides	10-26	huntingtin	Mus musculus	71-74
25035419-4	2014	Antisense oligonucleotides (ASOs) targeted to the CAG repeat region of HTT transcripts have been of particular interest due to their potential capacity to discriminate between normal and mutant HTT transcripts.	Oligonucleotides	10-26	huntingtin	Mus musculus	194-197
25035419-4	2014	Antisense oligonucleotides (ASOs) targeted to the CAG repeat region of HTT transcripts have been of particular interest due to their potential capacity to discriminate between normal and mutant HTT transcripts.	Oligonucleotides, Antisense	28-32	huntingtin	Mus musculus	71-74
25035419-4	2014	Antisense oligonucleotides (ASOs) targeted to the CAG repeat region of HTT transcripts have been of particular interest due to their potential capacity to discriminate between normal and mutant HTT transcripts.	Oligonucleotides, Antisense	28-32	huntingtin	Mus musculus	194-197
25035419-10	2014	Finally, CTG28 reduced mutant HTT expression and improved the phenotype of Hdh(Q7/Q150) knock-in HD mice.	ctg28	9-14	huntingtin	Mus musculus	30-33
25035419-10	2014	Finally, CTG28 reduced mutant HTT expression and improved the phenotype of Hdh(Q7/Q150) knock-in HD mice.	ctg28	9-14	huntingtin	Mus musculus	75-78
25101598-0	2014	In vivo evaluation of candidate allele-specific mutant huntingtin gene silencing antisense oligonucleotides.	Oligonucleotides	91-107	huntingtin	Mus musculus	55-65
25101598-3	2014	The mutant HTT protein (muHTT) acquires toxic functions, and there is significant evidence that muHTT lowering would be therapeutically efficacious.	muhtt	24-29	huntingtin	Mus musculus	11-14
25703232-1	2015	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG repeat expansion that encodes a polyglutamine tract in huntingtin (htt) protein.	polyglutamine	118-131	huntingtin	Mus musculus	141-151
25703232-1	2015	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a CAG repeat expansion that encodes a polyglutamine tract in huntingtin (htt) protein.	polyglutamine	118-131	huntingtin	Mus musculus	153-156
25703232-8	2015	We have demonstrated an interaction between the mutant huntingtin gene and iron supplementation in neonatal HD mice.	Iron	75-79	huntingtin	Mus musculus	55-65
25332397-1	2014	Huntington"s disease is a fatal neurodegenerative disease caused by polyglutamine-expansion in huntingtin (HTT).	polyglutamine	68-81	huntingtin	Mus musculus	107-110
24951540-6	2014	We also observed that the serine-threonine kinase IRE1 involved in endoplasmic reticulum (ER) stress responses is activated in mutant Htt-expressing cells in culture as well as in the striatum of mutant Htt transgenic (BACHD) mice.	Serine	26-32	huntingtin	Mus musculus	134-137
24951540-6	2014	We also observed that the serine-threonine kinase IRE1 involved in endoplasmic reticulum (ER) stress responses is activated in mutant Htt-expressing cells in culture as well as in the striatum of mutant Htt transgenic (BACHD) mice.	Serine	26-32	huntingtin	Mus musculus	203-206
25348412-1	2014	Huntington"s disease (HD) is caused by an expanded CAG trinucleotide repeat within the gene encoding the protein huntingtin.	trinucleotide	55-68	huntingtin	Mus musculus	113-123
25027318-2	2014	Mutant huntingtin undergoes proteolytic processing and its N-terminal fragment containing polyglutamine repeat accumulates as inclusion not only in nucleus but also in cytoplasm and neuronal processes.	polyglutamine	90-103	huntingtin	Mus musculus	7-17
25014023-4	2014	HD mice, which were supplemented with sodium selenite from 6 to 14 weeks of age, demonstrated increased motor endurance, decreased loss of brain weight, decreased mutant huntingtin aggregate burden and decreased brain oxidized glutathione levels.	Sodium Selenite	38-53	huntingtin	Mus musculus	170-180
25134728-1	2014	Huntington"s disease (HD) is caused by an expanded polyglutamine repeat in huntingtin protein that disrupts synaptic function in specific neuronal populations and results in characteristic motor, cognitive and affective deficits.	polyglutamine	51-64	huntingtin	Mus musculus	75-85
25348412-2	2014	The resulting elongated glutamine (poly-Q) sequence of mutant huntingtin (mhtt) affects both central neurons and skeletal muscle.	Glutamine	24-33	huntingtin	Mus musculus	62-72
25348412-2	2014	The resulting elongated glutamine (poly-Q) sequence of mutant huntingtin (mhtt) affects both central neurons and skeletal muscle.	polyglutamine	35-41	huntingtin	Mus musculus	62-72
24949563-1	2014	Huntington"s disease (HD) is a progressive and fatal neurodegenerative disorder caused by a polyglutamine expansion in the gene encoding the protein huntingtin.	polyglutamine	92-105	huntingtin	Mus musculus	149-159
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	Mus musculus	78-82
24634145-4	2014	Inhibitory phosphorylation of GSK3 (pGSK3) was elevated in mhtt cells and this appeared related to an overall energy metabolism deficit as the mhtt cells had less ATP and inhibiting ATP production in control cells expressing non-pathogenic htt with paraquat also increased pGSK3.	Adenosine Triphosphate	163-166	huntingtin	Mus musculus	60-63
24946181-1	2014	Huntington"s disease (HD) is an autosomal dominant neurological disorder that is induced by a CAG trinucleotide expansion in exon 1 of the Huntingtin (HTT) gene.	trinucleotide	98-111	huntingtin	Mus musculus	139-149
24946181-1	2014	Huntington"s disease (HD) is an autosomal dominant neurological disorder that is induced by a CAG trinucleotide expansion in exon 1 of the Huntingtin (HTT) gene.	trinucleotide	98-111	huntingtin	Mus musculus	151-154
24946181-3	2014	In the present study, we demonstrated that the elevated oxidative stress that was evoked by a polyQ-expanded mutant HTT (mHTT) caused the abnormal activation of AMPK-alpha1 and, subsequently, resulted in neurotoxicity in a striatal progenitor cell line (STHdh(Q109)) and in the striatum of a transgenic mouse model of HD (R6/2).	polyglutamine	94-99	huntingtin	Mus musculus	116-119
24938402-1	2014	Huntington"s disease (HD) is caused by cytosine-adenine-guanine (CAG) repeat expansions in the huntingtin (Htt) gene.	cytosine-adenine-guanine	39-63	huntingtin	Mus musculus	95-105
24938402-1	2014	Huntington"s disease (HD) is caused by cytosine-adenine-guanine (CAG) repeat expansions in the huntingtin (Htt) gene.	cytosine-adenine-guanine	39-63	huntingtin	Mus musculus	107-110
24938402-1	2014	Huntington"s disease (HD) is caused by cytosine-adenine-guanine (CAG) repeat expansions in the huntingtin (Htt) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	65-68	huntingtin	Mus musculus	95-105
24938402-1	2014	Huntington"s disease (HD) is caused by cytosine-adenine-guanine (CAG) repeat expansions in the huntingtin (Htt) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	65-68	huntingtin	Mus musculus	107-110
24938402-3	2014	Using the BACHD mice that express the full-length mutant huntingtin (mHtt) protein with 97 glutamine repeats, we first demonstrated localized in vivo changes in brain glucose use reminiscent of what is observed in premanifest HD carriers.	Glutamine	91-100	huntingtin	Mus musculus	57-67
24938402-3	2014	Using the BACHD mice that express the full-length mutant huntingtin (mHtt) protein with 97 glutamine repeats, we first demonstrated localized in vivo changes in brain glucose use reminiscent of what is observed in premanifest HD carriers.	Glucose	167-174	huntingtin	Mus musculus	57-67
24634145-4	2014	Inhibitory phosphorylation of GSK3 (pGSK3) was elevated in mhtt cells and this appeared related to an overall energy metabolism deficit as the mhtt cells had less ATP and inhibiting ATP production in control cells expressing non-pathogenic htt with paraquat also increased pGSK3.	Adenosine Triphosphate	182-185	huntingtin	Mus musculus	60-63
24633813-6	2014	MMs isolated from brains of aged Hdh Q111/Q111 knock-in mice showed a significant decrease in 1,6-diphenyl-hexatriene (DPH) anisotropy, which is inversely correlated with membrane fluidity.	Diphenylhexatriene	94-117	huntingtin	Mus musculus	33-36
24633813-6	2014	MMs isolated from brains of aged Hdh Q111/Q111 knock-in mice showed a significant decrease in 1,6-diphenyl-hexatriene (DPH) anisotropy, which is inversely correlated with membrane fluidity.	Diphenylhexatriene	119-122	huntingtin	Mus musculus	33-36
25038828-4	2014	Finally, alterations in serine/arginine-rich splicing factor-6 coincide with tau missplicing, and a role of tau in HD pathogenesis is evidenced by the attenuation of motor abnormalities of mutant HTT transgenic mice in tau knockout backgrounds.	Serine	24-30	huntingtin	Mus musculus	196-199
25268775-1	2014	Huntington"s disease (HD) is neurodegenerative disorder for which the mutation results in an extra-long tract of glutamines that causes the huntingtin protein to aggregate.	Glutamine	113-123	huntingtin	Mus musculus	140-150
25057205-1	2014	A polyglutamine expansion in huntingtin (HTT) causes the specific death of adult neurons in Huntington"s disease (HD).	polyglutamine	2-15	huntingtin	Mus musculus	29-39
25057205-1	2014	A polyglutamine expansion in huntingtin (HTT) causes the specific death of adult neurons in Huntington"s disease (HD).	polyglutamine	2-15	huntingtin	Mus musculus	41-44
25057205-5	2014	The serine/threonine kinase Akt, which regulates HTT function, rescued the spindle misorientation caused by the mHTT, by serine 421 (S421) phosphorylation, in cultured cells and in mice.	mhtt	112-116	huntingtin	Mus musculus	49-52
25057205-5	2014	The serine/threonine kinase Akt, which regulates HTT function, rescued the spindle misorientation caused by the mHTT, by serine 421 (S421) phosphorylation, in cultured cells and in mice.	Serine	4-10	huntingtin	Mus musculus	49-52
25038828-4	2014	Finally, alterations in serine/arginine-rich splicing factor-6 coincide with tau missplicing, and a role of tau in HD pathogenesis is evidenced by the attenuation of motor abnormalities of mutant HTT transgenic mice in tau knockout backgrounds.	Arginine	31-39	huntingtin	Mus musculus	196-199
24948797-2	2014	Polyglutamine expansion in the HD protein, huntingtin (Htt), causes selective neurodegeneration that is more severe in the striatum and cortex than in other brain regions, but the mechanism behind this selectivity is unknown.	polyglutamine	0-13	huntingtin	Mus musculus	43-53
25009276-1	2014	Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a poly-glutamine (poly-Q) stretch in the huntingtin (Htt) protein.	polyglutamine	86-100	huntingtin	Mus musculus	125-135
25009276-1	2014	Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a poly-glutamine (poly-Q) stretch in the huntingtin (Htt) protein.	polyglutamine	86-100	huntingtin	Mus musculus	137-140
25009276-1	2014	Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a poly-glutamine (poly-Q) stretch in the huntingtin (Htt) protein.	polyglutamine	102-108	huntingtin	Mus musculus	125-135
25009276-1	2014	Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a poly-glutamine (poly-Q) stretch in the huntingtin (Htt) protein.	polyglutamine	102-108	huntingtin	Mus musculus	137-140
25009276-9	2014	To determine whether the disease-causing poly-Q mutation in Htt affects synapse development, we next investigated the synaptic connectivity in a full-length knock-in mouse model of HD, the zQ175 mouse.	polyglutamine	41-47	huntingtin	Mus musculus	60-63
24948797-2	2014	Polyglutamine expansion in the HD protein, huntingtin (Htt), causes selective neurodegeneration that is more severe in the striatum and cortex than in other brain regions, but the mechanism behind this selectivity is unknown.	polyglutamine	0-13	huntingtin	Mus musculus	55-58
24301680-5	2014	The beneficial effect of FTY720 administration was associated with a significant strengthening of neuronal activity and connectivity and, with reduction of mutant huntingtin aggregates, and it was also paralleled by increased phosphorylation of mutant huntingtin at serine 13/16 residues that are predicted to attenuate protein toxicity.	Fingolimod Hydrochloride	25-31	huntingtin	Mus musculus	163-173
24738557-2	2014	In neurodegenerative diseases, lithium enhances degradation of aggregate-prone proteins, including mutated huntingtin, phosphorylated tau, and alpha-synuclein, and causes damaged mitochondria to degrade, while in a mouse model of cerebral ischemia and Alzheimer"s disease autophagy downregulation by lithium is observed.	Lithium	31-38	huntingtin	Mus musculus	107-117
24960609-5	2014	The Ryk-ICD fragment suppressed neuroprotection by lin-18/Ryk loss-of-function in expanded-polyQ nematodes, repressed FOXO transcriptional activity, and abolished beta-catenin protection of mutant htt striatal cells against cell death vulnerability.	polyglutamine	91-96	huntingtin	Mus musculus	197-200
24381308-1	2014	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by abnormal expansion of glutamine repeats in the protein huntingtin.	Glutamine	101-110	huntingtin	Mus musculus	134-144
24381308-2	2014	In HD brain, mutant huntingtin undergoes proteolytic processing, and its N-terminal fragment containing poly-glutamine repeats accumulate as insoluble aggregates leading to the defect in cellular protein quality control system and heat shock response (HSR).	polyglutamine	104-118	huntingtin	Mus musculus	20-30
24301680-5	2014	The beneficial effect of FTY720 administration was associated with a significant strengthening of neuronal activity and connectivity and, with reduction of mutant huntingtin aggregates, and it was also paralleled by increased phosphorylation of mutant huntingtin at serine 13/16 residues that are predicted to attenuate protein toxicity.	Fingolimod Hydrochloride	25-31	huntingtin	Mus musculus	252-262
24301680-5	2014	The beneficial effect of FTY720 administration was associated with a significant strengthening of neuronal activity and connectivity and, with reduction of mutant huntingtin aggregates, and it was also paralleled by increased phosphorylation of mutant huntingtin at serine 13/16 residues that are predicted to attenuate protein toxicity.	Serine	266-272	huntingtin	Mus musculus	252-262
24784230-1	2014	Huntington"s disease (HD) is a fatal dominantly inherited neurodegenerative disorder caused by a CAG repeat expansion leading to an elongated polyglutamine stretch in huntingtin.	polyglutamine	142-155	huntingtin	Mus musculus	167-177
24484067-1	2014	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disease caused by an increase in the number of polyglutamine residues in the huntingtin (Htt) protein.	polyglutamine	121-134	huntingtin	Mus musculus	151-161
24484067-1	2014	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disease caused by an increase in the number of polyglutamine residues in the huntingtin (Htt) protein.	polyglutamine	121-134	huntingtin	Mus musculus	163-166
24836077-1	2014	Mitochondrial dysfunction is associated with neuronal loss in Huntington"s disease (HD), a neurodegenerative disease caused by an abnormal polyglutamine expansion in huntingtin (Htt).	polyglutamine	139-152	huntingtin	Mus musculus	166-176
24836077-1	2014	Mitochondrial dysfunction is associated with neuronal loss in Huntington"s disease (HD), a neurodegenerative disease caused by an abnormal polyglutamine expansion in huntingtin (Htt).	polyglutamine	139-152	huntingtin	Mus musculus	178-181
24383989-7	2014	To further examine whether sulforaphane promotes mutant huntingtin (mHtt) degradation, we treated Huntington"s disease cells with sulforaphane and found that sulforaphane not only enhanced mHtt degradation but also reduced mHtt cytotoxicity.	sulforaphane	27-39	huntingtin	Mus musculus	56-66
24670645-1	2014	Huntington"s disease is an autosomal dominant disease associated with a mutation in the gene encoding huntingtin (Htt) leading to expanded polyglutamine repeats of mutant Htt (mHtt) that elicit oxidative stress, neurotoxicity, and motor and behavioural changes.	polyglutamine	139-152	huntingtin	Mus musculus	102-112
24670645-1	2014	Huntington"s disease is an autosomal dominant disease associated with a mutation in the gene encoding huntingtin (Htt) leading to expanded polyglutamine repeats of mutant Htt (mHtt) that elicit oxidative stress, neurotoxicity, and motor and behavioural changes.	polyglutamine	139-152	huntingtin	Mus musculus	114-117
24670645-1	2014	Huntington"s disease is an autosomal dominant disease associated with a mutation in the gene encoding huntingtin (Htt) leading to expanded polyglutamine repeats of mutant Htt (mHtt) that elicit oxidative stress, neurotoxicity, and motor and behavioural changes.	polyglutamine	139-152	huntingtin	Mus musculus	171-174
24198227-5	2014	Additionally, treatment with SC-51089 improved the expression of specific synaptic markers and reduced the number of huntingtin nuclear inclusions in the striatum and hippocampus of 18-week-old R6/1 mice.	SC 51089	29-37	huntingtin	Mus musculus	117-127
24282028-1	2014	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in the amino-terminal region of the huntingtin protein, which promotes progressive neuronal cell loss, neurological symptoms and death.	polyglutamine	90-103	huntingtin	Mus musculus	150-160
24282028-2	2014	In the present study, we show that blockade of mGluR5 with MTEP promotes increased locomotor activity in both control (Hdh(Q20/Q20)) and mutant HD (Hdh(Q111/Q111)) mice.	3-((2-methyl-1,3-thiazol-4-yl)ethynyl)piperidine	59-63	huntingtin	Mus musculus	119-122
24282028-2	2014	In the present study, we show that blockade of mGluR5 with MTEP promotes increased locomotor activity in both control (Hdh(Q20/Q20)) and mutant HD (Hdh(Q111/Q111)) mice.	3-((2-methyl-1,3-thiazol-4-yl)ethynyl)piperidine	59-63	huntingtin	Mus musculus	148-151
24389360-1	2014	Huntington"s disease (HD) is an inherited progressive neurodegenerative disorder caused by a pathological CAG trinucleotide repeat expansion in the large multi-exon gene, huntingtin (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	106-109	huntingtin	Mus musculus	171-181
24389360-1	2014	Huntington"s disease (HD) is an inherited progressive neurodegenerative disorder caused by a pathological CAG trinucleotide repeat expansion in the large multi-exon gene, huntingtin (HTT).	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	106-109	huntingtin	Mus musculus	183-186
24389360-1	2014	Huntington"s disease (HD) is an inherited progressive neurodegenerative disorder caused by a pathological CAG trinucleotide repeat expansion in the large multi-exon gene, huntingtin (HTT).	trinucleotide	110-123	huntingtin	Mus musculus	171-181
24389360-1	2014	Huntington"s disease (HD) is an inherited progressive neurodegenerative disorder caused by a pathological CAG trinucleotide repeat expansion in the large multi-exon gene, huntingtin (HTT).	trinucleotide	110-123	huntingtin	Mus musculus	183-186
24706802-2	2014	In Huntington disease, polyglutamine expansion causes N-terminal huntingtin (Htt) to misfold, inducing neurodegeneration.	polyglutamine	23-36	huntingtin	Mus musculus	65-75
24706802-2	2014	In Huntington disease, polyglutamine expansion causes N-terminal huntingtin (Htt) to misfold, inducing neurodegeneration.	polyglutamine	23-36	huntingtin	Mus musculus	77-80
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	Mus musculus	36-40
24594939-1	2014	A hallmark of Huntington"s disease is the pronounced sensitivity of striatal neurons to polyglutamine-expanded huntingtin expression.	polyglutamine	88-101	huntingtin	Mus musculus	111-121
24347167-6	2014	In contrast, antisense oligonucleotide knockdown of HTT in WT co-cultures resulted in a significant reduction of PSD-95 clustering in SPNs.	Oligonucleotides	23-38	huntingtin	Mus musculus	52-55
24380395-0	2014	Preventing formation of toxic N-terminal huntingtin fragments through antisense oligonucleotide-mediated protein modification.	Oligonucleotides	80-95	huntingtin	Mus musculus	41-51
24380395-1	2014	Huntington"s disease (HD) is a progressive autosomal dominant disorder, caused by a CAG repeat expansion in the HTT gene, which results in expansion of a polyglutamine stretch at the N-terminal end of the huntingtin protein.	polyglutamine	154-167	huntingtin	Mus musculus	112-115
24380395-1	2014	Huntington"s disease (HD) is a progressive autosomal dominant disorder, caused by a CAG repeat expansion in the HTT gene, which results in expansion of a polyglutamine stretch at the N-terminal end of the huntingtin protein.	polyglutamine	154-167	huntingtin	Mus musculus	205-215
24380395-4	2014	Here we report proof of concept using antisense oligonucleotides to induce skipping of exon 12 in huntingtin pre-mRNA, thereby preventing the formation of a 586 amino acid N-terminal huntingtin fragment implicated in HD toxicity.	Oligonucleotides	48-64	huntingtin	Mus musculus	98-108
24380395-4	2014	Here we report proof of concept using antisense oligonucleotides to induce skipping of exon 12 in huntingtin pre-mRNA, thereby preventing the formation of a 586 amino acid N-terminal huntingtin fragment implicated in HD toxicity.	Oligonucleotides	48-64	huntingtin	Mus musculus	183-193
24380395-8	2014	Recent advances to inhibit the formation of mutant huntingtin using oligonucleotides seem promising therapeutic strategies for HD.	Oligonucleotides	68-84	huntingtin	Mus musculus	51-61
24105466-5	2014	Htt-MeCP2 interactions are enhanced in the presence of the expanded polyglutamine (polyQ) tract and are stronger in the nucleus compared with the cytoplasm.	polyglutamine	68-81	huntingtin	Mus musculus	0-3
24105466-5	2014	Htt-MeCP2 interactions are enhanced in the presence of the expanded polyglutamine (polyQ) tract and are stronger in the nucleus compared with the cytoplasm.	polyglutamine	83-88	huntingtin	Mus musculus	0-3
24121117-3	2014	Here, we use the cre-lox system to drive expression of mutant huntingtin (mthtt) in parvalbumin (PV)-positive neurons and find that mutant mice exhibit diffuse mthtt immunoreactivity in PV-rich areas at 10months of age and mthtt aggregates in PV-positive processes at 24months of age.	mthtt	74-79	huntingtin	Mus musculus	62-72
24121117-3	2014	Here, we use the cre-lox system to drive expression of mutant huntingtin (mthtt) in parvalbumin (PV)-positive neurons and find that mutant mice exhibit diffuse mthtt immunoreactivity in PV-rich areas at 10months of age and mthtt aggregates in PV-positive processes at 24months of age.	mthtt	160-165	huntingtin	Mus musculus	62-72
24121117-3	2014	Here, we use the cre-lox system to drive expression of mutant huntingtin (mthtt) in parvalbumin (PV)-positive neurons and find that mutant mice exhibit diffuse mthtt immunoreactivity in PV-rich areas at 10months of age and mthtt aggregates in PV-positive processes at 24months of age.	mthtt	160-165	huntingtin	Mus musculus	62-72
24376631-1	2013	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an expanded polyglutamine repeat in the huntingtin protein.	polyglutamine	86-99	huntingtin	Mus musculus	114-124
24475300-1	2014	Huntington"s Disease (HD) is a neurodegenerative disorder that is caused by abnormal expansion of a polyglutamine tract in huntingtin (htt) protein.	polyglutamine	100-113	huntingtin	Mus musculus	123-133
24475300-1	2014	Huntington"s Disease (HD) is a neurodegenerative disorder that is caused by abnormal expansion of a polyglutamine tract in huntingtin (htt) protein.	polyglutamine	100-113	huntingtin	Mus musculus	135-138
24475300-8	2014	Similar analysis of R6/2 animals revealed that ubiquilin is localized in huntingtin aggregates and that ubiquilin levels decrease progressively to 30% during the end-stage of disease.	ubiquilin	47-56	huntingtin	Mus musculus	73-83
24453320-2	2014	Defects in autophagy have been implicated in the neurodegenerative disorder Huntington"s disease (HD), in which polyglutamine-expanded huntingtin (polyQ-htt) is predominantly cleared by autophagy.	polyglutamine	112-125	huntingtin	Mus musculus	135-145
24453320-2	2014	Defects in autophagy have been implicated in the neurodegenerative disorder Huntington"s disease (HD), in which polyglutamine-expanded huntingtin (polyQ-htt) is predominantly cleared by autophagy.	polyglutamine	112-125	huntingtin	Mus musculus	153-156
24453320-10	2014	The resulting defective clearance of both polyQ-htt aggregates and dysfunctional mitochondria by neuronal autophagosomes may contribute to neurodegeneration and cell death in HD.	polyglutamine	42-47	huntingtin	Mus musculus	48-51
24333873-5	2014	We administered the GABA(B) receptor agonist, baclofen, to wild-type or mutant huntingtin-expressing striatal cells (HD19 or HD43).	Baclofen	46-54	huntingtin	Mus musculus	79-89
24333873-6	2014	Chymotrypsin-like proteasome activity and cell viability were significantly increased in the mutant huntingtin-expressing striatal cells (HD43) after GABA(B) receptor agonist treatment.	gamma-Aminobutyric Acid	150-154	huntingtin	Mus musculus	100-110
25575955-1	2014	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a polyglutamine expansion in the Huntingtin protein which results in the selective degeneration of striatal medium spiny neurons (MSN).	polyglutamine	82-95	huntingtin	Mus musculus	113-123
25575958-1	2014	BACKGROUND: Huntington"s disease (HD), caused by polyglutamine expansion in huntingtin (Htt), results in severe neurodegeneration in the striatum, and to a lesser extent, cortex and hippocampus.	polyglutamine	49-62	huntingtin	Mus musculus	76-86
25575958-1	2014	BACKGROUND: Huntington"s disease (HD), caused by polyglutamine expansion in huntingtin (Htt), results in severe neurodegeneration in the striatum, and to a lesser extent, cortex and hippocampus.	polyglutamine	49-62	huntingtin	Mus musculus	88-91
25575960-0	2014	Presymptomatic glutamate levels in prefrontal cortex in the Hdh(CAG150) mouse model of Huntington"s disease.	Glutamic Acid	15-24	huntingtin	Mus musculus	60-63
25575960-4	2014	OBJECTIVE: The present study was designed to determine if a similar deficit in glutamate function occurs in the prefrontal cortex (PFC) of Hdh(CAG150) mice.	Glutamic Acid	79-88	huntingtin	Mus musculus	139-142
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	Mus musculus	36-40
24302884-2	2013	We hypothesised that it may be involved in the molecular pathogenesis of Huntington"s disease (HD), a protein-folding neurodegenerative disorder caused by an aggregation-prone polyglutamine expansion in the huntingtin protein.	polyglutamine	176-189	huntingtin	Mus musculus	207-217
24324398-1	2013	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by the expansion of a polyglutamine stretch in the huntingtin (HTT) protein and characterized by dysregulated calcium homeostasis.	polyglutamine	97-110	huntingtin	Mus musculus	126-136
24324398-1	2013	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by the expansion of a polyglutamine stretch in the huntingtin (HTT) protein and characterized by dysregulated calcium homeostasis.	polyglutamine	97-110	huntingtin	Mus musculus	138-141
24324398-1	2013	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by the expansion of a polyglutamine stretch in the huntingtin (HTT) protein and characterized by dysregulated calcium homeostasis.	Calcium	185-192	huntingtin	Mus musculus	126-136
24324398-1	2013	Huntington"s disease (HD) is a hereditary neurodegenerative disease caused by the expansion of a polyglutamine stretch in the huntingtin (HTT) protein and characterized by dysregulated calcium homeostasis.	Calcium	185-192	huntingtin	Mus musculus	138-141
24324398-4	2013	HTT mutation caused the increased expression of some components of the calcium signalosome, including calretinin, presenilin 2, and calmyrin 1, and the increased expression of genes indirectly involved in calcium homeostasis, such as huntingtin-associated protein 1 and calcyclin-binding protein.	Calcium	71-78	huntingtin	Mus musculus	0-3
24324398-4	2013	HTT mutation caused the increased expression of some components of the calcium signalosome, including calretinin, presenilin 2, and calmyrin 1, and the increased expression of genes indirectly involved in calcium homeostasis, such as huntingtin-associated protein 1 and calcyclin-binding protein.	Calcium	205-212	huntingtin	Mus musculus	0-3
24324398-6	2013	Using single-cell imaging with Fura-2AM, we found that store-operated Ca(2+) entry but not endoplasmic reticulum (ER) store content was changed as a result of the expression of mutant HTT.	fura-2-am	31-39	huntingtin	Mus musculus	184-187
22633949-2	2013	The expanded trinucleotide (CAG) repeat leads to an extended polyglutamine tract in the huntingtin protein and a subsequent cascade of molecular and cellular pathogenesis.	trinucleotide	13-26	huntingtin	Mus musculus	88-98
24256709-1	2013	Huntington"s disease (HD) is an adult-onset neurodegenerative disorder caused by a mutated CAG repeat in the huntingtin gene that is translated into an expanded polyglutamine tract.	polyglutamine	161-174	huntingtin	Mus musculus	109-119
24041806-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded trinucleotide CAG repeat in the Huntingtin (Htt) gene.	trinucleotide	80-93	huntingtin	Mus musculus	112-122
24041806-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expanded trinucleotide CAG repeat in the Huntingtin (Htt) gene.	trinucleotide	80-93	huntingtin	Mus musculus	124-127
22633949-2	2013	The expanded trinucleotide (CAG) repeat leads to an extended polyglutamine tract in the huntingtin protein and a subsequent cascade of molecular and cellular pathogenesis.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	28-31	huntingtin	Mus musculus	88-98
22633949-2	2013	The expanded trinucleotide (CAG) repeat leads to an extended polyglutamine tract in the huntingtin protein and a subsequent cascade of molecular and cellular pathogenesis.	polyglutamine	61-74	huntingtin	Mus musculus	88-98
24081492-5	2013	We found that polyglutamine-expanded exon1 htt binds to the C-terminal region of synapsin-1 to reduce synapsin-1 phosphorylation.	polyglutamine	14-27	huntingtin	Mus musculus	43-46
24146952-1	2013	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a polyglutamine-encoding CAG expansion in the huntingtin gene.	polyglutamine	82-95	huntingtin	Mus musculus	126-136
24019939-2	2013	HD is caused by an abnormal polyglutamine (polyQ) expansion in the huntingtin (HTT) protein.	polyglutamine	28-41	huntingtin	Mus musculus	67-77
24086450-2	2013	The encoded poly-glutamine stretch renders mutant huntingtin prone to aggregation.	polyglutamine	12-26	huntingtin	Mus musculus	50-60
24019939-2	2013	HD is caused by an abnormal polyglutamine (polyQ) expansion in the huntingtin (HTT) protein.	polyglutamine	28-41	huntingtin	Mus musculus	79-82
23852340-1	2013	Huntington"s disease is caused by an expanded polyglutamine repeat in the huntingtin protein (HTT), but the pathophysiological sequence of events that trigger synaptic failure and neuronal loss are not fully understood.	polyglutamine	46-59	huntingtin	Mus musculus	74-84
24012756-4	2013	Here, we report that the Golgi protein acyl-CoA binding domain containing 3 (ACBD3) mediates mHtt cytotoxicity via a Rhes/mHtt/ACBD3 complex.	Acyl Coenzyme A	39-47	huntingtin	Mus musculus	93-97
23967334-1	2013	Huntington"s disease (HD) is a neurodegenerative disease caused by abnormal polyglutamine expansion in the huntingtin protein (Htt).	polyglutamine	76-89	huntingtin	Mus musculus	107-117
23967334-1	2013	Huntington"s disease (HD) is a neurodegenerative disease caused by abnormal polyglutamine expansion in the huntingtin protein (Htt).	polyglutamine	76-89	huntingtin	Mus musculus	127-130
23852340-1	2013	Huntington"s disease is caused by an expanded polyglutamine repeat in the huntingtin protein (HTT), but the pathophysiological sequence of events that trigger synaptic failure and neuronal loss are not fully understood.	polyglutamine	46-59	huntingtin	Mus musculus	94-97
23678106-2	2013	Here, we demonstrate that wild-type huntingtin, the protein mutated in HD, modulates anxiety/depression-related behaviors according to its phosphorylation at serines 1181 and 1201.	Serine	158-165	huntingtin	Mus musculus	36-46
23864673-1	2013	Huntington"s disease (HD) is caused by a polyglutamine expansion within the huntingtin (Htt) protein.	polyglutamine	41-54	huntingtin	Mus musculus	76-86
23864673-1	2013	Huntington"s disease (HD) is caused by a polyglutamine expansion within the huntingtin (Htt) protein.	polyglutamine	41-54	huntingtin	Mus musculus	88-91
23864673-2	2013	Both loss of function of normal Htt and gain of a toxic function by the polyglutamine-expanded mutant Htt protein have been proposed to be responsible for HD, although the molecular mechanisms involved are unclear.	polyglutamine	72-85	huntingtin	Mus musculus	102-105
23347954-4	2013	Rho-kinase (ROCK) inhibitor Y27632 reduced brain level of polyglutamine-expanded huntingtin in HD transgenic mouse.	Y 27632	28-34	huntingtin	Mus musculus	81-91
23347954-4	2013	Rho-kinase (ROCK) inhibitor Y27632 reduced brain level of polyglutamine-expanded huntingtin in HD transgenic mouse.	polyglutamine	58-71	huntingtin	Mus musculus	81-91
23446639-7	2013	Moreover, 4"-DMA-7,8-DHF preserved DARPP32 levels in the striatum and rescued mutant huntingtin-induced impairment of neurogenesis in the N171-82Q HD mice.	4"-dma-7,8-dhf	10-24	huntingtin	Mus musculus	85-95
23489026-1	2013	BACKGROUND AND PURPOSE: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin protein.	polyglutamine	114-127	huntingtin	Mus musculus	145-155
23691206-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by abnormal polyglutamine expansion in the amino-terminal end of the huntingtin protein (Htt) and characterized by progressive striatal and cortical pathology.	polyglutamine	77-90	huntingtin	Mus musculus	134-144
23691206-1	2013	Huntington"s disease (HD) is a neurodegenerative disorder caused by abnormal polyglutamine expansion in the amino-terminal end of the huntingtin protein (Htt) and characterized by progressive striatal and cortical pathology.	polyglutamine	77-90	huntingtin	Mus musculus	154-157
23455440-1	2013	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by an expanded trinucleotide CAG repeat in the gene coding for huntingtin.	trinucleotide	99-112	huntingtin	Mus musculus	147-157
23549885-1	2013	Huntington"s disease (HD) is an autosomal dominant hereditary disease caused by a trinucleotide repeat mutation in the huntingtin gene that results in an increased number of glutamine residues in the N terminus of huntingtin protein.	trinucleotide	82-95	huntingtin	Mus musculus	119-129
23446639-2	2013	This disease is caused by an expanded CAG trinucleotide repeat in the gene encoding the protein huntingtin.	trinucleotide	42-55	huntingtin	Mus musculus	96-106
23549885-1	2013	Huntington"s disease (HD) is an autosomal dominant hereditary disease caused by a trinucleotide repeat mutation in the huntingtin gene that results in an increased number of glutamine residues in the N terminus of huntingtin protein.	trinucleotide	82-95	huntingtin	Mus musculus	214-224
23549885-1	2013	Huntington"s disease (HD) is an autosomal dominant hereditary disease caused by a trinucleotide repeat mutation in the huntingtin gene that results in an increased number of glutamine residues in the N terminus of huntingtin protein.	Glutamine	174-183	huntingtin	Mus musculus	119-129
23549885-1	2013	Huntington"s disease (HD) is an autosomal dominant hereditary disease caused by a trinucleotide repeat mutation in the huntingtin gene that results in an increased number of glutamine residues in the N terminus of huntingtin protein.	Glutamine	174-183	huntingtin	Mus musculus	214-224
25063516-4	2013	OBJECTIVE: To examine if transcriptional dysregulation can be ameliorated with antisense oligonucleotides that reduce levels of mutant Htt and provide therapeutic benefit in the YAC128 mouse model of HD.	Oligonucleotides	89-105	huntingtin	Mus musculus	135-138
23373812-1	2013	Huntington"s disease (HD) is a devastating genetic neurodegenerative disease caused by CAG trinucleotide expansion in the exon-1 region of the huntingtin gene.	cag trinucleotide	87-104	huntingtin	Mus musculus	143-153
23373812-6	2013	We now report that the PPAR-gamma agonist, rosiglitazone (RSG), significantly attenuated mutant HTT-induced toxicity in striatal cells and that the protective effect of RSG is mediated by activation of PPAR-gamma.	Rosiglitazone	43-56	huntingtin	Mus musculus	96-99
23373812-6	2013	We now report that the PPAR-gamma agonist, rosiglitazone (RSG), significantly attenuated mutant HTT-induced toxicity in striatal cells and that the protective effect of RSG is mediated by activation of PPAR-gamma.	Rosiglitazone	58-61	huntingtin	Mus musculus	96-99
23373812-6	2013	We now report that the PPAR-gamma agonist, rosiglitazone (RSG), significantly attenuated mutant HTT-induced toxicity in striatal cells and that the protective effect of RSG is mediated by activation of PPAR-gamma.	Rosiglitazone	169-172	huntingtin	Mus musculus	96-99
23598407-9	2013	Accordingly, pharmacological inhibition of PP1 by okadaic acid (OA) prevented mutant huntingtin striatal cell death induced by NMDA and BDNF.	Okadaic Acid	50-62	huntingtin	Mus musculus	85-95
23598407-9	2013	Accordingly, pharmacological inhibition of PP1 by okadaic acid (OA) prevented mutant huntingtin striatal cell death induced by NMDA and BDNF.	N-Methylaspartate	127-131	huntingtin	Mus musculus	85-95
23497526-8	2013	Further, although ethanol altered a distinct set of genes depending on developmental timing, many of these show interrelatedness and can be associated with one another via "hub" molecules and pathways such as those related to huntingtin and brain-derived neurotrophic factor.	Ethanol	18-25	huntingtin	Mus musculus	226-236
23197653-2	2013	Mouse homozygous (HM) and heterozygous (HT) mutant striatal cells with two or one allele encoding for a mutant huntingtin protein with 111 polyGln repeats showed a significant impairment of the mitochondrial disulfide relay system (MDRS).	Disulfides	208-217	huntingtin	Mus musculus	111-121
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	Mus musculus	144-148
23575829-7	2013	In HD, the polyQ expansion in HTT alters the binding of TrkB-containing vesicles to microtubules and reduces transport.	polyglutamine	11-16	huntingtin	Mus musculus	30-33
23297360-5	2013	We show that the nuclear localization of huntingtin depends upon the RanGTP/GDP gradient, and that N17 phosphorylation can also distinguish localization of endogenous huntingtin between the basal body and stalk of the primary cilium.	rangtp	69-75	huntingtin	Mus musculus	41-51
23219902-2	2013	Here we studied the effect of anomalous polyglutamine expansion in huntingtin on the interaction of coat proteins with membranes, in areas of mouse brain or in cultured striatal cells.	polyglutamine	40-53	huntingtin	Mus musculus	67-77
23219902-6	2013	It was also confirmed that huntingtin mutation made the cells more vulnerable to the action of quinolinic acid, with an increasing degradation of the AP-2 alpha subunits.	Quinolinic Acid	95-110	huntingtin	Mus musculus	27-37
23219902-7	2013	On the basis of these results, we conclude that abnormal polyglutamine expansion in huntingtin affects clathrin-mediated endocytosis, and may be one of the pathogenic mechanisms of neurodegeneration.	polyglutamine	57-70	huntingtin	Mus musculus	84-94
23123142-2	2013	It is a genetic disease caused by an elongation of the polyglutamine repeats in the huntingtin gene.	polyglutamine	55-68	huntingtin	Mus musculus	84-94
23300147-1	2013	In Huntington disease (HD), polyglutamine expansion in the huntingtin protein causes specific neuronal death.	polyglutamine	28-41	huntingtin	Mus musculus	59-69
23352662-1	2013	Huntington disease (HD), a dominantly inherited neurodegenerative disorder caused by the expansion of a CAG-encoded polyglutamine (polyQ) repeat in huntingtin (Htt), displays a highly heterogeneous etiopathology and disease onset.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	104-107	huntingtin	Mus musculus	148-158
23352662-1	2013	Huntington disease (HD), a dominantly inherited neurodegenerative disorder caused by the expansion of a CAG-encoded polyglutamine (polyQ) repeat in huntingtin (Htt), displays a highly heterogeneous etiopathology and disease onset.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	104-107	huntingtin	Mus musculus	160-163
23352662-1	2013	Huntington disease (HD), a dominantly inherited neurodegenerative disorder caused by the expansion of a CAG-encoded polyglutamine (polyQ) repeat in huntingtin (Htt), displays a highly heterogeneous etiopathology and disease onset.	polyglutamine	116-129	huntingtin	Mus musculus	148-158
23352662-1	2013	Huntington disease (HD), a dominantly inherited neurodegenerative disorder caused by the expansion of a CAG-encoded polyglutamine (polyQ) repeat in huntingtin (Htt), displays a highly heterogeneous etiopathology and disease onset.	polyglutamine	116-129	huntingtin	Mus musculus	160-163
23352662-1	2013	Huntington disease (HD), a dominantly inherited neurodegenerative disorder caused by the expansion of a CAG-encoded polyglutamine (polyQ) repeat in huntingtin (Htt), displays a highly heterogeneous etiopathology and disease onset.	polyglutamine	131-136	huntingtin	Mus musculus	148-158
23352662-1	2013	Huntington disease (HD), a dominantly inherited neurodegenerative disorder caused by the expansion of a CAG-encoded polyglutamine (polyQ) repeat in huntingtin (Htt), displays a highly heterogeneous etiopathology and disease onset.	polyglutamine	131-136	huntingtin	Mus musculus	160-163
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	Mus musculus	56-66
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	Mus musculus	56-66
22422149-6	2013	Here, we report the generation of transgenic mice carrying GFP fused with mutant HTT exon 1 containing 84 CAG trinucleotide repeats, and the evaluation of phenotypes via molecular, neuropathological and behavioral analyses.	trinucleotide	110-123	huntingtin	Mus musculus	81-84
22974734-4	2013	hMTH1 expression protected these cells from 3-NP and H2O2-induced killing, by counteracting the mutant htt-dependent increased vulnerability and accumulation of nuclear and mitochondrial DNA 8-hydroxyguanine levels.	Hydrogen Peroxide	53-57	huntingtin	Mus musculus	103-106
22974734-4	2013	hMTH1 expression protected these cells from 3-NP and H2O2-induced killing, by counteracting the mutant htt-dependent increased vulnerability and accumulation of nuclear and mitochondrial DNA 8-hydroxyguanine levels.	8-hydroxyguanine	191-207	huntingtin	Mus musculus	103-106
23099177-7	2013	Methylone had little effect on behavior or neurotransmitter levels in mice but produced a widespread depletion of 5-HT and 5-HTT levels in rats.	methylone	0-9	huntingtin	Mus musculus	125-128
23469253-1	2013	Huntington disease (HD) is an inherited neurodegenerative disease resulting from an abnormal expansion of polyglutamine in huntingtin (Htt).	polyglutamine	106-119	huntingtin	Mus musculus	123-133
23469253-1	2013	Huntington disease (HD) is an inherited neurodegenerative disease resulting from an abnormal expansion of polyglutamine in huntingtin (Htt).	polyglutamine	106-119	huntingtin	Mus musculus	135-138
23409115-6	2013	Its binding to Htt is regulated by the rho-associated kinase (ROCK), which phosphorylates profilin at Ser-137.	Serine	102-105	huntingtin	Mus musculus	15-18
22892315-0	2012	A series of N-terminal epitope tagged Hdh knock-in alleles expressing normal and mutant huntingtin: their application to understanding the effect of increasing the length of normal Huntingtin"s polyglutamine stretch on CAG140 mouse model pathogenesis.	polyglutamine	194-207	huntingtin	Mus musculus	181-191
24696705-0	2013	Striatal synaptosomes from Hdh140Q/140Q knock-in mice have altered protein levels, novel sites of methionine oxidation, and excess glutamate release after stimulation.	Methionine	98-108	huntingtin	Mus musculus	27-30
24696705-0	2013	Striatal synaptosomes from Hdh140Q/140Q knock-in mice have altered protein levels, novel sites of methionine oxidation, and excess glutamate release after stimulation.	Glutamic Acid	131-140	huntingtin	Mus musculus	27-30
23131566-0	2012	Calcium leak through ryanodine receptor is involved in neuronal death induced by mutant huntingtin.	Calcium	0-7	huntingtin	Mus musculus	88-98
23131566-1	2012	Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormal expansion of polyglutamine (polyQ) tract in huntingtin (htt) protein.	polyglutamine	93-106	huntingtin	Mus musculus	124-134
23131566-1	2012	Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormal expansion of polyglutamine (polyQ) tract in huntingtin (htt) protein.	polyglutamine	93-106	huntingtin	Mus musculus	136-139
23131566-1	2012	Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormal expansion of polyglutamine (polyQ) tract in huntingtin (htt) protein.	polyglutamine	108-113	huntingtin	Mus musculus	124-134
23131566-1	2012	Huntington"s disease (HD) is a neurodegenerative disorder caused by an abnormal expansion of polyglutamine (polyQ) tract in huntingtin (htt) protein.	polyglutamine	108-113	huntingtin	Mus musculus	136-139
22932698-1	2012	Huntington disease (HD) results from CAG repeats that encode expanded polyglutamine tracts in the HTT/huntingtin protein.	polyglutamine	70-83	huntingtin	Mus musculus	98-101
22932698-1	2012	Huntington disease (HD) results from CAG repeats that encode expanded polyglutamine tracts in the HTT/huntingtin protein.	polyglutamine	70-83	huntingtin	Mus musculus	102-112
24336051-4	2013	Here using striatal neurons derived from knock-in mice expressing mutant huntingtin (STHdhQ cells), we study ascorbic acid transport.	Ascorbic Acid	109-122	huntingtin	Mus musculus	73-83
22999956-0	2012	Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties.	Serine	0-6	huntingtin	Mus musculus	34-44
22999956-2	2012	Consistent with this hypothesis, two Ser-to-Asp mutations in the 17-amino-acid N-terminal htt(NT) segment abrogate both visible brain aggregates and disease symptoms in a full-length Q(97) htt mouse model while compromising aggregation kinetics and aggregate morphology in an htt fragment in vitro [Gu et al.	17-amino-acid	65-78	huntingtin	Mus musculus	90-93
22999956-2	2012	Consistent with this hypothesis, two Ser-to-Asp mutations in the 17-amino-acid N-terminal htt(NT) segment abrogate both visible brain aggregates and disease symptoms in a full-length Q(97) htt mouse model while compromising aggregation kinetics and aggregate morphology in an htt fragment in vitro [Gu et al.	17-amino-acid	65-78	huntingtin	Mus musculus	189-192
22999956-2	2012	Consistent with this hypothesis, two Ser-to-Asp mutations in the 17-amino-acid N-terminal htt(NT) segment abrogate both visible brain aggregates and disease symptoms in a full-length Q(97) htt mouse model while compromising aggregation kinetics and aggregate morphology in an htt fragment in vitro [Gu et al.	17-amino-acid	65-78	huntingtin	Mus musculus	189-192
22999956-8	2012	First, these negatively charged Ser replacements impair the assembly of the alpha-helical oligomers that play a critical role in htt amyloid nucleation, thus providing an explanation for reduced amyloid formation rates.	Serine	32-35	huntingtin	Mus musculus	129-132
22698685-1	2012	Huntington"s disease (HD) is a devastating autosomal-dominant neurodegenerative disorder initiated by an abnormally expanded polyglutamine in the huntingtin protein.	polyglutamine	125-138	huntingtin	Mus musculus	146-156
22698685-4	2012	A role for TG2 in HD has been suggested because a polypeptide-bound glutamine is a rate-limiting factor for a TG2-catalyzed reaction, and TG2 can cross-link mutant huntingtin in vitro.	Glutamine	68-77	huntingtin	Mus musculus	164-174
22787151-3	2012	Here, we demonstrate that the ubiquitin ligase Ube3a, which is implicated in synaptic plasticity and involved in the clearance of misfolded polyglutamine protein, is strongly recruited to the mutant huntingtin nuclear aggregates, resulting in significant loss of its functional pool in different regions of HD mouse brain.	polyglutamine	140-153	huntingtin	Mus musculus	199-209
22892315-2	2012	Although studies in vitro have suggested that the mutant htt can act in a potentially dominant negative fashion by sequestering wild-type htt into insoluble protein aggregates, the role of the length of the normal htt polyQ stretch, and the adjacent proline-rich region (PRR) in modulating HD mouse model pathogenesis is currently unknown.	Proline	250-257	huntingtin	Mus musculus	57-60
22892315-5	2012	When the sequences encoding normal mouse htt"s polyQ stretch and PRR are replaced with non-pathogenic human sequence in mice also expressing 140Q-htt, aggregation foci within the striatum, and the mean size of htt inclusions are increased, along with an increase in striatal lipofuscin and gliosis.	polyglutamine	47-52	huntingtin	Mus musculus	41-44
22589249-1	2012	Huntington"s disease (HD) is an incurable neurological disorder caused by an abnormal glutamine repeat expansion in the huntingtin (Htt) protein.	Glutamine	86-95	huntingtin	Mus musculus	120-130
22589249-1	2012	Huntington"s disease (HD) is an incurable neurological disorder caused by an abnormal glutamine repeat expansion in the huntingtin (Htt) protein.	Glutamine	86-95	huntingtin	Mus musculus	132-135
22892315-1	2012	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease that is caused by the expansion of a polyglutamine (polyQ) stretch within Huntingtin (htt), the protein product of the HD gene.	polyglutamine	126-139	huntingtin	Mus musculus	163-173
22892315-1	2012	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease that is caused by the expansion of a polyglutamine (polyQ) stretch within Huntingtin (htt), the protein product of the HD gene.	polyglutamine	126-139	huntingtin	Mus musculus	175-178
22892315-1	2012	BACKGROUND: Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease that is caused by the expansion of a polyglutamine (polyQ) stretch within Huntingtin (htt), the protein product of the HD gene.	polyglutamine	141-146	huntingtin	Mus musculus	163-173
22593067-7	2012	Expression of mHtt (148Q) resulted in a selective increase in NMDAR(EX) activity, compared with wild-type Htt (18Q), and increased vulnerability to NMDA excitotoxicity.	N-Methylaspartate	62-66	huntingtin	Mus musculus	14-18
22786682-1	2012	Huntington"s disease (HD) is caused by CAG repeat expansions in the huntingtin (htt) gene, yielding proteins containing polyglutamine repeats that become misfolded and resist degradation.	polyglutamine	120-133	huntingtin	Mus musculus	68-78
22786682-1	2012	Huntington"s disease (HD) is caused by CAG repeat expansions in the huntingtin (htt) gene, yielding proteins containing polyglutamine repeats that become misfolded and resist degradation.	polyglutamine	120-133	huntingtin	Mus musculus	80-83
22556411-1	2012	Huntington disease is a neurodegenerative disorder caused by a CAG repeat amplification in the gene huntingtin (HTT) that is reflected by a polyglutamine expansion in the Htt protein.	polyglutamine	140-153	huntingtin	Mus musculus	100-110
22556411-1	2012	Huntington disease is a neurodegenerative disorder caused by a CAG repeat amplification in the gene huntingtin (HTT) that is reflected by a polyglutamine expansion in the Htt protein.	polyglutamine	140-153	huntingtin	Mus musculus	112-115
22556411-1	2012	Huntington disease is a neurodegenerative disorder caused by a CAG repeat amplification in the gene huntingtin (HTT) that is reflected by a polyglutamine expansion in the Htt protein.	polyglutamine	140-153	huntingtin	Mus musculus	171-174
22328089-4	2012	While YAC128 mice exhibit significant and widespread accumulation of mHTT striatal aggregates, these mHTT aggregates are absent in BACHD mice.	yac128	6-12	huntingtin	Mus musculus	69-73
22726826-3	2012	(2012) show the benefit of transient antisense oligonucleotide (ASO) therapy to degrade Huntingtin mRNA and elicit sustained therapeutic benefit in HD mice.	Oligonucleotides	47-62	huntingtin	Mus musculus	88-98
22726826-3	2012	(2012) show the benefit of transient antisense oligonucleotide (ASO) therapy to degrade Huntingtin mRNA and elicit sustained therapeutic benefit in HD mice.	Oligonucleotides, Antisense	64-67	huntingtin	Mus musculus	88-98
22726834-1	2012	The primary cause of Huntington"s disease (HD) is expression of huntingtin with a polyglutamine expansion.	polyglutamine	82-95	huntingtin	Mus musculus	64-74
22726834-3	2012	With antisense oligonucleotides (ASOs) that catalyze RNase H-mediated degradation of huntingtin mRNA, we demonstrate that transient infusion into the cerebrospinal fluid of symptomatic HD mouse models not only delays disease progression but mediates a sustained reversal of disease phenotype that persists longer than the huntingtin knockdown.	Oligonucleotides	15-31	huntingtin	Mus musculus	85-95
22726834-3	2012	With antisense oligonucleotides (ASOs) that catalyze RNase H-mediated degradation of huntingtin mRNA, we demonstrate that transient infusion into the cerebrospinal fluid of symptomatic HD mouse models not only delays disease progression but mediates a sustained reversal of disease phenotype that persists longer than the huntingtin knockdown.	Oligonucleotides	15-31	huntingtin	Mus musculus	322-332
22511757-1	2012	Huntington disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine expansion in the protein huntingtin (Htt).	polyglutamine	88-101	huntingtin	Mus musculus	127-137
22511757-1	2012	Huntington disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine expansion in the protein huntingtin (Htt).	polyglutamine	88-101	huntingtin	Mus musculus	139-142
22511757-6	2012	In addition, R59949 decreased the accumulation of a 513-amino acid N-terminal Htt fragment processed by caspase-3 and blocked alterations in lipid metabolism during serum withdrawal.	R 59949	13-19	huntingtin	Mus musculus	78-81
22560595-0	2012	The dopaminergic stabilizer, (-)-OSU6162, rescues striatal neurons with normal and expanded polyglutamine chains in huntingtin protein from exposure to free radicals and mitochondrial toxins.	OSU 6162	29-40	huntingtin	Mus musculus	116-126
22560595-0	2012	The dopaminergic stabilizer, (-)-OSU6162, rescues striatal neurons with normal and expanded polyglutamine chains in huntingtin protein from exposure to free radicals and mitochondrial toxins.	polyglutamine	92-105	huntingtin	Mus musculus	116-126
22560595-1	2012	Huntington"s disease (HD) is a neurodegenerative disease characterized by progressive motor, cognitive and psychiatric deficits, associated with predominant loss of striatal neurons and caused by a polyglutamine expansion in the huntingtin protein.	polyglutamine	198-211	huntingtin	Mus musculus	229-239
22560595-5	2012	We investigated the effects of (-)-OSU6162 on huntingtin knocked-in striatal neurons in culture.	OSU 6162	31-42	huntingtin	Mus musculus	46-56
20457229-1	2012	Huntington"s disease is caused by a single mutation resulting in an expanded polyglutamine sequence which causes the production of a mutant variant of the protein huntingtin, which is ultimately responsible for the motor, cognitive and emotional symptoms and early death of the individual.	polyglutamine	77-90	huntingtin	Mus musculus	163-173
20457230-5	2012	The results indicate that the Hdh(Q150/Q150) mice were impaired on each of the measures used, with deficits appearing on a 3-stage water maze test at 4 months of age and on prepulse inhibition at 6 months of age, both of which were prior to the manifestation of motor abnormalities.	Water	131-136	huntingtin	Mus musculus	30-33
21272613-1	2012	Huntington"s disease is caused by a single mutation on the HTT gene which produces an expansion in the number of glutamine repeats present in the huntingtin protein.	Glutamine	113-122	huntingtin	Mus musculus	59-62
21272613-1	2012	Huntington"s disease is caused by a single mutation on the HTT gene which produces an expansion in the number of glutamine repeats present in the huntingtin protein.	Glutamine	113-122	huntingtin	Mus musculus	146-156
21620935-1	2012	Huntington"s disease (HD) is a progressive neurodegenerative disease caused by the insertion of an expanded polyglutamine sequence within the huntingtin protein.	polyglutamine	108-121	huntingtin	Mus musculus	142-152
21763407-2	2012	The disease is caused by a single mutation in the gene responsible for the protein huntingtin, increasing the number of polyQ repeats and conferring a toxic gain of function to the mutant protein, which ultimately induces cell death.	polyglutamine	120-125	huntingtin	Mus musculus	83-93
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	Mus musculus	209-213
22623107-7	2012	In addition, prevention of phosphorylation at the two serine sites altered mHtt toxicity and accumulation.	Serine	54-60	huntingtin	Mus musculus	75-79
22337954-1	2012	Mutations leading to expansion of a poly-glutamine track in Huntingtin (Htt) cause Huntington"s disease (HD).	polyglutamine	36-50	huntingtin	Mus musculus	60-70
22337954-1	2012	Mutations leading to expansion of a poly-glutamine track in Huntingtin (Htt) cause Huntington"s disease (HD).	polyglutamine	36-50	huntingtin	Mus musculus	72-75
22593067-7	2012	Expression of mHtt (148Q) resulted in a selective increase in NMDAR(EX) activity, compared with wild-type Htt (18Q), and increased vulnerability to NMDA excitotoxicity.	N-Methylaspartate	62-66	huntingtin	Mus musculus	15-18
22433867-9	2012	Further, we demonstrate that expanded huntingtin shortstop has a reduced ability to form amyloid-like fibrils characteristic of the aggregation pathway for toxic expanded polyglutamine proteins.	polyglutamine	171-184	huntingtin	Mus musculus	38-48
22508027-3	2012	HD is a heritable neurodegenerative disease caused by a mutation resulting in an increased number of glutamines (Q) within a polyglutamine tract in Huntingtin (Htt).	Glutamine	101-111	huntingtin	Mus musculus	148-158
22402331-1	2012	Growing evidence suggests that Huntington"s disease (HD), a neurodegenerative movement disorder caused by the mutant huntingtin (htt) with an expanded polyglutamine (polyQ) repeat, is associated with the altered intracellular trafficking and synaptic function.	polyglutamine	151-164	huntingtin	Mus musculus	117-127
22402331-1	2012	Growing evidence suggests that Huntington"s disease (HD), a neurodegenerative movement disorder caused by the mutant huntingtin (htt) with an expanded polyglutamine (polyQ) repeat, is associated with the altered intracellular trafficking and synaptic function.	polyglutamine	151-164	huntingtin	Mus musculus	129-132
22402331-1	2012	Growing evidence suggests that Huntington"s disease (HD), a neurodegenerative movement disorder caused by the mutant huntingtin (htt) with an expanded polyglutamine (polyQ) repeat, is associated with the altered intracellular trafficking and synaptic function.	polyglutamine	166-171	huntingtin	Mus musculus	117-127
22402331-1	2012	Growing evidence suggests that Huntington"s disease (HD), a neurodegenerative movement disorder caused by the mutant huntingtin (htt) with an expanded polyglutamine (polyQ) repeat, is associated with the altered intracellular trafficking and synaptic function.	polyglutamine	166-171	huntingtin	Mus musculus	129-132
22649225-1	2012	Huntington"s disease (HD) is caused by a mutation in the huntingtin (htt) gene encoding an expansion of glutamine repeats at the N terminus of the Htt protein.	Glutamine	104-113	huntingtin	Mus musculus	57-67
22649225-1	2012	Huntington"s disease (HD) is caused by a mutation in the huntingtin (htt) gene encoding an expansion of glutamine repeats at the N terminus of the Htt protein.	Glutamine	104-113	huntingtin	Mus musculus	69-72
22649225-1	2012	Huntington"s disease (HD) is caused by a mutation in the huntingtin (htt) gene encoding an expansion of glutamine repeats at the N terminus of the Htt protein.	Glutamine	104-113	huntingtin	Mus musculus	147-150
22649225-3	2012	In particular, it has been postulated that proteolysis of Htt at the putative caspase-6 cleavage site (at amino acid Asp-586) plays a critical role in disease progression and pathogenesis.	Aspartic Acid	117-120	huntingtin	Mus musculus	58-61
22649225-9	2012	Importantly, we detected the presence of Htt fragments consistent with cleavage at amino acid Asp-586 of Htt in the BACHD Casp6(-/-) mouse, indicating that caspase-6 activity cannot fully account for the generation of the Htt 586 fragment in vivo.	Aspartic Acid	94-97	huntingtin	Mus musculus	41-44
22649225-9	2012	Importantly, we detected the presence of Htt fragments consistent with cleavage at amino acid Asp-586 of Htt in the BACHD Casp6(-/-) mouse, indicating that caspase-6 activity cannot fully account for the generation of the Htt 586 fragment in vivo.	Aspartic Acid	94-97	huntingtin	Mus musculus	105-108
22649225-9	2012	Importantly, we detected the presence of Htt fragments consistent with cleavage at amino acid Asp-586 of Htt in the BACHD Casp6(-/-) mouse, indicating that caspase-6 activity cannot fully account for the generation of the Htt 586 fragment in vivo.	Aspartic Acid	94-97	huntingtin	Mus musculus	105-108
22445760-0	2012	AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington"s disease.	CHEMBL2031461	0-3	huntingtin	Mus musculus	89-99
22475209-5	2012	RESULTS: KI mice fed a curcumin-containing diet since conception showed decreased huntingtin aggregates and increased striatal DARPP-32 and D1 receptor mRNAs, as well as an amelioration of rearing deficits.	Curcumin	23-31	huntingtin	Mus musculus	82-92
22508027-3	2012	HD is a heritable neurodegenerative disease caused by a mutation resulting in an increased number of glutamines (Q) within a polyglutamine tract in Huntingtin (Htt).	Glutamine	101-111	huntingtin	Mus musculus	160-163
22508027-6	2012	Compared to Htt(7Q/7Q) NS cells, HD Htt(140Q/140Q) NS cells showed significantly reduced levels of cholesterol, increased levels of reactive oxygen species (ROS), and impaired motility.	Cholesterol	99-110	huntingtin	Mus musculus	36-39
22508027-6	2012	Compared to Htt(7Q/7Q) NS cells, HD Htt(140Q/140Q) NS cells showed significantly reduced levels of cholesterol, increased levels of reactive oxygen species (ROS), and impaired motility.	Oxygen	141-147	huntingtin	Mus musculus	36-39
22508027-9	2012	Huntingtin "knock-out" NS cells (Htt(-/-)) also had impaired motility, but in contrast to HD cells had increased cholesterol.	Cholesterol	113-124	huntingtin	Mus musculus	0-10
22187438-3	2012	Using synthetic polyglutamine peptides as the substrate for amyloid formation, we found that partially purified misfolded HTT obtained from end-stage brain tissue of two Tg HD mouse models and brain tissue of post-mortem human HD patients was capable of specifically accelerating polyglutamine amyloid formation compared with unseeded reactions and controls.	polyglutamine peptides	16-38	huntingtin	Mus musculus	122-125
22227000-1	2012	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an excessive expansion of a CAG trinucleotide repeat in the gene encoding the protein huntingtin, resulting in an elongated stretch of glutamines near the N-terminus of the protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	116-119	huntingtin	Mus musculus	174-184
22227000-1	2012	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an excessive expansion of a CAG trinucleotide repeat in the gene encoding the protein huntingtin, resulting in an elongated stretch of glutamines near the N-terminus of the protein.	trinucleotide	120-133	huntingtin	Mus musculus	174-184
22227000-1	2012	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disorder caused by an excessive expansion of a CAG trinucleotide repeat in the gene encoding the protein huntingtin, resulting in an elongated stretch of glutamines near the N-terminus of the protein.	Glutamine	223-233	huntingtin	Mus musculus	174-184
22100502-5	2012	HD is caused by a polyglutamine repeat expansion in the huntingtin protein, and decades of work have established mitochondrial dysfunction as a key feature of HD pathogenesis.	polyglutamine	18-31	huntingtin	Mus musculus	56-66
22191580-2	2012	We recently reported a gene-environment interaction wherein expression of mutant HTT is associated with neuroprotection against manganese (Mn) toxicity.	Manganese	128-137	huntingtin	Mus musculus	81-84
22198502-1	2012	Huntington disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the protein huntingtin (htt).	polyglutamine	88-101	huntingtin	Mus musculus	135-145
22198502-1	2012	Huntington disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the protein huntingtin (htt).	polyglutamine	88-101	huntingtin	Mus musculus	147-150
22198502-1	2012	Huntington disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the protein huntingtin (htt).	polyglutamine	103-108	huntingtin	Mus musculus	135-145
22198502-1	2012	Huntington disease (HD) is a dominantly inherited neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the protein huntingtin (htt).	polyglutamine	103-108	huntingtin	Mus musculus	147-150
22331905-0	2012	Ganglioside GM1 induces phosphorylation of mutant huntingtin and restores normal motor behavior in Huntington disease mice.	Gangliosides	0-11	huntingtin	Mus musculus	50-60
22331905-1	2012	Huntington disease (HD) is a progressive neurodegenerative monogenic disorder caused by expansion of a polyglutamine stretch in the huntingtin (Htt) protein.	polyglutamine	103-116	huntingtin	Mus musculus	132-142
22331905-1	2012	Huntington disease (HD) is a progressive neurodegenerative monogenic disorder caused by expansion of a polyglutamine stretch in the huntingtin (Htt) protein.	polyglutamine	103-116	huntingtin	Mus musculus	144-147
22331905-4	2012	We report that intraventricular infusion of ganglioside GM1 induces phosphorylation of mutant huntingtin at specific serine amino acid residues that attenuate huntingtin toxicity, and restores normal motor function in already symptomatic HD mice.	serine amino acid	117-134	huntingtin	Mus musculus	94-104
22331905-4	2012	We report that intraventricular infusion of ganglioside GM1 induces phosphorylation of mutant huntingtin at specific serine amino acid residues that attenuate huntingtin toxicity, and restores normal motor function in already symptomatic HD mice.	serine amino acid	117-134	huntingtin	Mus musculus	159-169
22365609-1	2012	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by the amplification of a polyglutamine stretch at the N terminus of the huntingtin protein.	polyglutamine	102-115	huntingtin	Mus musculus	149-159
22116937-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	112-115	huntingtin	Mus musculus	165-175
22116937-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	112-115	huntingtin	Mus musculus	177-180
22116937-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene.	polyglutamine	116-129	huntingtin	Mus musculus	165-175
22116937-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder caused by an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene.	polyglutamine	116-129	huntingtin	Mus musculus	177-180
22116937-6	2012	Finally, and consistent with a role of CBP in cognitive impairment in Hdh(Q7/Q111) mice, administration of the histone deacetylase inhibitor trichostatin A rescues recognition memory deficits and transcription of selective CREB/CBP target genes in Hdh(Q7/Q111) mice.	trichostatin A	141-155	huntingtin	Mus musculus	70-73
22116937-6	2012	Finally, and consistent with a role of CBP in cognitive impairment in Hdh(Q7/Q111) mice, administration of the histone deacetylase inhibitor trichostatin A rescues recognition memory deficits and transcription of selective CREB/CBP target genes in Hdh(Q7/Q111) mice.	trichostatin A	141-155	huntingtin	Mus musculus	248-251
22178857-3	2012	We report here that knock-in Hdh(Q111) mice, an animal model of HD, that carry an expanded polyglutamine stretch in the mouse HD protein show an anxio-depressive-like phenotype prior to any impairment of the locomotor function.	polyglutamine	91-104	huntingtin	Mus musculus	29-32
22123819-8	2012	In addition, in 4-month-old knock-in Hdh(Q111/+) mice, the earliest metabolic alterations consisted of increased phosphocreatine in the frontal cortex and increased the pAMPK/AMPK ratio.	Phosphocreatine	113-128	huntingtin	Mus musculus	37-40
22045254-2	2012	Previously we found that primary neurons from embryonic cortex of mice bearing the Huntington"s disease mutation (140 glutamines inserted into exon 1 of huntingtin) showed higher levels of reactive oxygen species before cell death.	Glutamine	118-128	huntingtin	Mus musculus	153-163
22045254-2	2012	Previously we found that primary neurons from embryonic cortex of mice bearing the Huntington"s disease mutation (140 glutamines inserted into exon 1 of huntingtin) showed higher levels of reactive oxygen species before cell death.	Oxygen	198-204	huntingtin	Mus musculus	153-163
22649566-1	2012	The molecular mechanisms by which polyglutamine (polyQ)-expanded huntingtin (Htt) causes neurodegeneration in Huntington"s disease (HD) remain unclear.	polyglutamine	49-54	huntingtin	Mus musculus	65-75
22219281-1	2012	Huntington"s disease (HD) is caused by a polyglutamine expansion in the Huntingtin (Htt) protein.	polyglutamine	41-54	huntingtin	Mus musculus	72-82
22219281-1	2012	Huntington"s disease (HD) is caused by a polyglutamine expansion in the Huntingtin (Htt) protein.	polyglutamine	41-54	huntingtin	Mus musculus	84-87
22219281-5	2012	To test this hypothesis, and further characterize the role of this fragment, we have generated transgenic mice expressing the N-terminal 586 aa of Htt with a polyglutamine repeat length of 82 (N586-82Q), under the control of the prion promoter.	polyglutamine	158-171	huntingtin	Mus musculus	147-150
21954231-1	2012	Huntington"s disease (HD), an inherited neurodegenerative disorder, is caused by an expansion of cytosine-adenine-guanine repeats in the huntingtin gene.	cytosine-adenine-guanine	97-121	huntingtin	Mus musculus	137-147
22956985-0	2012	Deletion of the huntingtin proline-rich region does not significantly affect normal huntingtin function in mice.	Proline	27-34	huntingtin	Mus musculus	16-26
22956985-1	2012	The N-terminus of Huntingtin, the protein encoded by the Huntington"s disease gene, contains a stretch of polyglutamine residues that is expanded in Huntington"s disease.	polyglutamine	106-119	huntingtin	Mus musculus	18-28
23393546-7	2012	RESULTS: We found that in striatal Hdh(Q111/Q111) cells, pizotifen treatment caused transient ERK activation and inhibition of ERK activation prevented rescue of cell death in this model.	Pizotyline	57-66	huntingtin	Mus musculus	35-38
23833693-6	2012	Mice of the FVB/N strain, which are highly vulnerable to excitotoxicity, become extremely resistant to quinolinic acid-induced striatal neurodegeneration with age, when carrying a huntingtin (Htt) allele expressing a HD transgene (CAG140).	Quinolinic Acid	103-118	huntingtin	Mus musculus	180-190
23833693-6	2012	Mice of the FVB/N strain, which are highly vulnerable to excitotoxicity, become extremely resistant to quinolinic acid-induced striatal neurodegeneration with age, when carrying a huntingtin (Htt) allele expressing a HD transgene (CAG140).	Quinolinic Acid	103-118	huntingtin	Mus musculus	192-195
24353748-1	2012	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an expanded CAG trinucleotide repeat sequence in the huntingtin gene.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	92-95	huntingtin	Mus musculus	133-143
24353748-1	2012	Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by an expanded CAG trinucleotide repeat sequence in the huntingtin gene.	trinucleotide	96-109	huntingtin	Mus musculus	133-143
24353748-2	2012	The resulting poly-glutamine expansion in the huntingtin protein imparts a novel toxic gain of function causing selective loss of medium spiny neurons (MSNs) in the striatum.	polyglutamine	14-28	huntingtin	Mus musculus	46-56
25063329-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder due to an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene that causes the preferential degeneration of striatal neurons.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	109-112	huntingtin	Mus musculus	162-172
25063329-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder due to an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene that causes the preferential degeneration of striatal neurons.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	109-112	huntingtin	Mus musculus	174-177
25063329-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder due to an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene that causes the preferential degeneration of striatal neurons.	polyglutamine	113-126	huntingtin	Mus musculus	162-172
25063329-1	2012	Huntington"s disease (HD) is an autosomal dominant progressive neurodegenerative disorder due to an expanded CAG/polyglutamine repeat in the coding region of the huntingtin (htt) gene that causes the preferential degeneration of striatal neurons.	polyglutamine	113-126	huntingtin	Mus musculus	174-177
25063332-1	2012	BACKGROUND: There is evidence that interaction with biologically important metals, particularly copper and iron, contributes to the pathological aggregation and toxicity of the mutant huntingtin protein in HD.	Copper	96-102	huntingtin	Mus musculus	184-194
25063332-1	2012	BACKGROUND: There is evidence that interaction with biologically important metals, particularly copper and iron, contributes to the pathological aggregation and toxicity of the mutant huntingtin protein in HD.	Iron	107-111	huntingtin	Mus musculus	184-194
22072510-2	2012	When the R6/2 mouse was first developed, it carried exon 1 of the huntingtin gene with ~150 cytosine-adenine-guanine (CAG) repeats.	cytosine-adenine-guanine	92-116	huntingtin	Mus musculus	66-76
22072510-2	2012	When the R6/2 mouse was first developed, it carried exon 1 of the huntingtin gene with ~150 cytosine-adenine-guanine (CAG) repeats.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	118-121	huntingtin	Mus musculus	66-76
21907283-1	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	Mus musculus	124-134
21907283-1	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	Mus musculus	136-139
21907283-7	2012	By reducing Htt aggregates and thereby ameliorating the recruitment of PPARgamma into Htt aggregates, TZD treatment also elevated the availability of PPARgamma level and subsequently normalized the expression of downstream genes (including PGC-1alpha and several mitochondrial genes) in the cortex.	tzd	102-105	huntingtin	Mus musculus	12-15
21907283-7	2012	By reducing Htt aggregates and thereby ameliorating the recruitment of PPARgamma into Htt aggregates, TZD treatment also elevated the availability of PPARgamma level and subsequently normalized the expression of downstream genes (including PGC-1alpha and several mitochondrial genes) in the cortex.	tzd	102-105	huntingtin	Mus musculus	86-89
22649566-1	2012	The molecular mechanisms by which polyglutamine (polyQ)-expanded huntingtin (Htt) causes neurodegeneration in Huntington"s disease (HD) remain unclear.	polyglutamine	49-54	huntingtin	Mus musculus	77-80
22649566-4	2012	We find that, under non-stress conditions, the proteostatic capacity of cells expressing full length polyQ-expanded Htt is adequate.	polyglutamine	101-106	huntingtin	Mus musculus	116-119
22649566-5	2012	Yet, under stress conditions, the presence of polyQ-expanded Htt impairs the heat shock response, a key component of cellular proteostasis.	polyglutamine	46-51	huntingtin	Mus musculus	61-64
22649566-7	2012	We demonstrate that in cells expressing polyQ-expanded Htt the levels of heat shock transcription factor 1 (HSF1) are reduced, and, as a consequence, these cells have an impaired a heat shock response.	polyglutamine	40-45	huntingtin	Mus musculus	55-58
22649566-9	2012	Our results suggests that full length, non-aggregated polyQ-expanded Htt blocks the effective induction of the heat shock response under stress conditions and may thus trigger the accumulation of cellular damage during the course of HD pathogenesis.	polyglutamine	54-59	huntingtin	Mus musculus	69-72
22363539-12	2012	Finally, we show that mutant HTT suppresses some Mn-dependent changes, such as decreased DA levels, while it exacerbates others, such as dendritic pathology.	Dopamine	89-91	huntingtin	Mus musculus	29-32
22179316-2	2011	Here we show that Sirt1 has a neuroprotective role in models of Huntington"s disease, an inherited neurodegenerative disorder caused by a glutamine repeat expansion in huntingtin protein (HTT).	Glutamine	138-147	huntingtin	Mus musculus	168-178
22179316-2	2011	Here we show that Sirt1 has a neuroprotective role in models of Huntington"s disease, an inherited neurodegenerative disorder caused by a glutamine repeat expansion in huntingtin protein (HTT).	Glutamine	138-147	huntingtin	Mus musculus	188-191
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	Mus musculus	12-16
22118545-1	2011	BACKGROUND: Huntington"s disease (HD) is a progressive neurodegenerative disorder caused by a polyglutamine expansion in the Huntingtin protein which results in the selective degeneration of striatal medium spiny neurons (MSNs).	polyglutamine	94-107	huntingtin	Mus musculus	125-135
22649566-0	2012	Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin.	polyglutamine	61-74	huntingtin	Mus musculus	84-94
22649566-1	2012	The molecular mechanisms by which polyglutamine (polyQ)-expanded huntingtin (Htt) causes neurodegeneration in Huntington"s disease (HD) remain unclear.	polyglutamine	34-47	huntingtin	Mus musculus	65-75
22649566-1	2012	The molecular mechanisms by which polyglutamine (polyQ)-expanded huntingtin (Htt) causes neurodegeneration in Huntington"s disease (HD) remain unclear.	polyglutamine	34-47	huntingtin	Mus musculus	77-80
21985783-2	2011	It is caused by expansion of a CAG repeat in the first exon of the huntingtin (HTT) gene that encodes a mutant HTT protein with a polyglutamine (polyQ) expansion at the amino terminus.	polyglutamine	130-143	huntingtin	Mus musculus	67-77
21985783-2	2011	It is caused by expansion of a CAG repeat in the first exon of the huntingtin (HTT) gene that encodes a mutant HTT protein with a polyglutamine (polyQ) expansion at the amino terminus.	polyglutamine	130-143	huntingtin	Mus musculus	79-82
21985783-2	2011	It is caused by expansion of a CAG repeat in the first exon of the huntingtin (HTT) gene that encodes a mutant HTT protein with a polyglutamine (polyQ) expansion at the amino terminus.	polyglutamine	130-143	huntingtin	Mus musculus	111-114
21985783-2	2011	It is caused by expansion of a CAG repeat in the first exon of the huntingtin (HTT) gene that encodes a mutant HTT protein with a polyglutamine (polyQ) expansion at the amino terminus.	polyglutamine	145-150	huntingtin	Mus musculus	67-77
21985783-2	2011	It is caused by expansion of a CAG repeat in the first exon of the huntingtin (HTT) gene that encodes a mutant HTT protein with a polyglutamine (polyQ) expansion at the amino terminus.	polyglutamine	145-150	huntingtin	Mus musculus	79-82
21985783-2	2011	It is caused by expansion of a CAG repeat in the first exon of the huntingtin (HTT) gene that encodes a mutant HTT protein with a polyglutamine (polyQ) expansion at the amino terminus.	polyglutamine	145-150	huntingtin	Mus musculus	111-114
21994366-0	2011	The melatonin MT1 receptor axis modulates mutant Huntingtin-mediated toxicity.	Melatonin	4-13	huntingtin	Mus musculus	49-59
21994366-6	2011	Moreover, we demonstrate that melatonin inhibits mutant htt-induced caspase activation and preserves MT1 receptor expression.	Melatonin	30-39	huntingtin	Mus musculus	56-59
21896647-7	2011	Treatment with ER stressors, tunicamycin or DTT, rapidly decreased BiP-GFP mobility in mHtt striatal cells and accelerated UPR activation compared with wild-type cells.	Tunicamycin	29-40	huntingtin	Mus musculus	87-91
21896647-7	2011	Treatment with ER stressors, tunicamycin or DTT, rapidly decreased BiP-GFP mobility in mHtt striatal cells and accelerated UPR activation compared with wild-type cells.	Dithiothreitol	44-47	huntingtin	Mus musculus	87-91
21161248-5	2011	Notably, 4-HNE immunoreactivity was colocalized with mutant huntingtin inclusions in the striatal neurons of R6/2 HD mice.	4-hydroxy-2-nonenal	9-14	huntingtin	Mus musculus	60-70
21703318-3	2011	In the present study, we show the protective effects of FK506 in two striatal HD models, primary rat striatal neurons treated with 3-nitropropionic acid (3-NP) and immortalized striatal STHdh cells derived from HD knock-in mice expressing normal (STHdh(7/7)) or full-length mutant huntingtin (FL-mHtt) with 111 glutamines (STHdh(111/111)), under basal conditions and after exposure to 3-NP or staurosporine (STS).	Tacrolimus	56-61	huntingtin	Mus musculus	281-291
21832090-2	2011	However, it is largely unknown whether AMPA receptor trafficking, which is crucial for controlling the efficacy of synaptic excitation, is affected by the mutant huntingtin with polyglutamine expansion (polyQ-htt).	polyglutamine	178-191	huntingtin	Mus musculus	162-172
21832090-2	2011	However, it is largely unknown whether AMPA receptor trafficking, which is crucial for controlling the efficacy of synaptic excitation, is affected by the mutant huntingtin with polyglutamine expansion (polyQ-htt).	polyglutamine	178-191	huntingtin	Mus musculus	209-212
21832090-3	2011	In this study, we found that expressing polyQ-htt in neuronal cultures significantly decreased the amplitude and frequency of AMPAR-mediated miniature excitatory postsynaptic current (mEPSC), while expressing wild-type huntingtin (WT-htt) increased mEPSC.	polyglutamine	40-45	huntingtin	Mus musculus	46-49
21832090-3	2011	In this study, we found that expressing polyQ-htt in neuronal cultures significantly decreased the amplitude and frequency of AMPAR-mediated miniature excitatory postsynaptic current (mEPSC), while expressing wild-type huntingtin (WT-htt) increased mEPSC.	polyglutamine	40-45	huntingtin	Mus musculus	219-229
21832090-3	2011	In this study, we found that expressing polyQ-htt in neuronal cultures significantly decreased the amplitude and frequency of AMPAR-mediated miniature excitatory postsynaptic current (mEPSC), while expressing wild-type huntingtin (WT-htt) increased mEPSC.	polyglutamine	40-45	huntingtin	Mus musculus	234-237
21832090-5	2011	The effect of polyQ-htt on mEPSC was mimicked by knockdown of HAP1 and occluded by the dominant negative HAP1.	polyglutamine	14-19	huntingtin	Mus musculus	20-23
21651979-1	2011	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	Mus musculus	124-134
21651979-1	2011	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	Mus musculus	136-139
21454471-3	2011	Here, we report that tumor necrosis factor receptor-associated factor 6 (TRAF6) binds to WT and polyQ-expanded N-HTT in vitro as well as to endogenous full-length proteins in mouse and human brain in vivo.	polyglutamine	96-101	huntingtin	Mus musculus	113-116
21493629-1	2011	Huntington"s disease (HD) is a neurodegenerative disorder due to abnormal polyglutamine expansion in huntingtin protein (Exp-Htt).	polyglutamine	74-87	huntingtin	Mus musculus	101-111
21542802-3	2011	To determine the extent of cell-autonomous effects of mhtt (mutant huntingtin) protein on vulnerability to excitotoxic insult in MSNs in vivo, we measured the number of degenerating neurons in response to intrastriatal injection of QA (quinolinic acid) in presymptomatic and symptomatic transgenic (D9-N171-98Q, also known as DE5) mice that express mhtt in MSNs but not in cortex.	mhtt	54-58	huntingtin	Mus musculus	67-77
21632937-11	2011	In Tet/HD94 mice striatum, mutant huntingtin transgene shutdown reestablished STEP expression.	tetramethylenedisulfotetramine	3-6	huntingtin	Mus musculus	34-44
21623356-1	2011	Two serine residues within the first 17 amino acid residues of huntingtin (N17) are crucial for modulation of mutant huntingtin toxicity in cell and mouse genetic models of Huntington"s disease.	Serine	4-10	huntingtin	Mus musculus	63-73
21623356-1	2011	Two serine residues within the first 17 amino acid residues of huntingtin (N17) are crucial for modulation of mutant huntingtin toxicity in cell and mouse genetic models of Huntington"s disease.	Serine	4-10	huntingtin	Mus musculus	117-127
21623356-3	2011	Polyglutamine-expanded mutant huntingtin is hypophosphorylated in N17 in both homozygous and heterozygous cell contexts.	polyglutamine	0-13	huntingtin	Mus musculus	30-40
21636527-1	2011	Huntington disease (HD) is caused by polyglutamine expansion in the huntingtin (HTT) protein.	polyglutamine	37-50	huntingtin	Mus musculus	68-78
21636527-1	2011	Huntington disease (HD) is caused by polyglutamine expansion in the huntingtin (HTT) protein.	polyglutamine	37-50	huntingtin	Mus musculus	80-83
21636527-2	2011	Huntingtin-interacting protein 14 (HIP14), one of 23 DHHC domain-containing palmitoyl acyl transferases (PATs), binds to HTT and robustly palmitoylates HTT at cysteine 214.	Cysteine	159-167	huntingtin	Mus musculus	152-155
21536587-1	2011	Huntington"s disease is initiated by the expression of a CAG repeat-encoded polyglutamine region in full-length huntingtin, with dominant effects that vary continuously with CAG size.	polyglutamine	76-89	huntingtin	Mus musculus	112-122
21536587-7	2011	Thus, varying the polyglutamine size in full-length huntingtin produced gene expression changes that were distinct from, but related to, the effects of lack of huntingtin.	polyglutamine	18-31	huntingtin	Mus musculus	52-62
21447599-5	2011	Consistent with decreased N-cadherin function, STHdh(Q111) striatal cells displayed profound deficits in calcium-dependent N-cadherin-mediated cell clustering and cell-substratum adhesion, and primary Hdh(Q111) striatal neuronal cells exhibited decreased N-cadherin and an abundance of immature neurites, featuring diffuse, rather than clustered, staining for N-cadherin and synaptic vesicle markers, which was partially rescued by adenine treatment.	Calcium	105-112	huntingtin	Mus musculus	49-52
21447599-5	2011	Consistent with decreased N-cadherin function, STHdh(Q111) striatal cells displayed profound deficits in calcium-dependent N-cadherin-mediated cell clustering and cell-substratum adhesion, and primary Hdh(Q111) striatal neuronal cells exhibited decreased N-cadherin and an abundance of immature neurites, featuring diffuse, rather than clustered, staining for N-cadherin and synaptic vesicle markers, which was partially rescued by adenine treatment.	Adenine	432-439	huntingtin	Mus musculus	49-52
21454633-0	2011	Cysteine oxidation within N-terminal mutant huntingtin promotes oligomerization and delays clearance of soluble protein.	Cysteine	0-8	huntingtin	Mus musculus	44-54
21454633-1	2011	Huntington disease (HD) is a progressive neurodegenerative disorder caused by expression of polyglutamine-expanded mutant huntingtin protein (mhtt).	polyglutamine	92-105	huntingtin	Mus musculus	122-132
21454633-4	2011	We have shown previously that copper interacts with and oxidizes the polyglutamine-containing N171 fragment of huntingtin.	Copper	30-36	huntingtin	Mus musculus	111-121
21454633-4	2011	We have shown previously that copper interacts with and oxidizes the polyglutamine-containing N171 fragment of huntingtin.	polyglutamine	69-82	huntingtin	Mus musculus	111-121
21552328-9	2011	In Dictyostelium, huntingtin deficiency is compatible with survival of the organism but renders cells sensitive to low osmolarity, which produces pleiotropic cell autonomous defects that affect cAMP signaling and as a consequence development.	Cyclic AMP	194-198	huntingtin	Mus musculus	18-28
21192926-2	2011	HD is caused by the expansion of a polyglutamine repeat region in the N-terminal of the huntingtin protein.	polyglutamine	35-48	huntingtin	Mus musculus	88-98
21192926-3	2011	Here we examine the behavioral, transcriptional, histopathological and anatomical characteristics of a knock-in HD mouse model with a 140 polyglutamine expansion in the huntingtin protein.	polyglutamine	138-151	huntingtin	Mus musculus	169-179
20977939-5	2011	Moreover, ampakine treatments prevented the decrease in total striatal area, blocked the loss of striatal DARPP-32 immunoreactivity and reduced by 36% the size of intra-nuclear huntingtin aggregates in R6/2 striatum.	ampakine	10-18	huntingtin	Mus musculus	177-187
21245084-1	2011	An expanded polyglutamine tract (>37 glutamines) in the N-terminal region of huntingtin (htt) causes htt to accumulate in the nucleus, leading to transcriptional dysregulation in Huntington disease (HD).	Glutamine	37-47	huntingtin	Mus musculus	77-87
21245084-1	2011	An expanded polyglutamine tract (>37 glutamines) in the N-terminal region of huntingtin (htt) causes htt to accumulate in the nucleus, leading to transcriptional dysregulation in Huntington disease (HD).	Glutamine	37-47	huntingtin	Mus musculus	89-92
21245084-1	2011	An expanded polyglutamine tract (>37 glutamines) in the N-terminal region of huntingtin (htt) causes htt to accumulate in the nucleus, leading to transcriptional dysregulation in Huntington disease (HD).	Glutamine	37-47	huntingtin	Mus musculus	101-104
21245084-4	2011	Here, we report that serine 16 (S16) in htt is important for the generation of small N-terminal fragments that are able to accumulate in the nucleus and form aggregates.	Serine	21-27	huntingtin	Mus musculus	40-43
21106706-1	2011	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by expanded polyglutamine repeats in the huntingtin (Htt) protein.	polyglutamine	88-101	huntingtin	Mus musculus	117-127
21106706-1	2011	Huntington"s disease (HD) is an inherited neurodegenerative disorder caused by expanded polyglutamine repeats in the huntingtin (Htt) protein.	polyglutamine	88-101	huntingtin	Mus musculus	129-132
21248135-1	2011	In Huntington"s disease (HD), the expansion of polyglutamine (polyQ) repeats at the N terminus of the ubiquitous protein huntingtin (htt) leads to neurodegeneration in specific brain areas.	polyglutamine	47-60	huntingtin	Mus musculus	121-131
21059370-0	2011	The common inhaled anesthetic isoflurane increases aggregation of huntingtin and alters calcium homeostasis in a cell model of Huntington"s disease.	Isoflurane	30-40	huntingtin	Mus musculus	66-76
21059370-2	2011	We hypothesized that isoflurane will have similar effects on the polyglutamine huntingtin protein and will cause alterations in intracellular calcium homeostasis.	Isoflurane	21-31	huntingtin	Mus musculus	79-89
21059370-3	2011	We tested this hypothesis in striatal cells from the expanded glutamine huntingtin knock-in mouse (STHdh(Q111/Q111)) and wild type (STHdh(Q7/Q7)) striatal neurons.	Glutamine	62-71	huntingtin	Mus musculus	72-82
21059370-6	2011	Isoflurane, sevoflurane, and desflurane all increased the aggregation of huntingtin in STHdh(Q111/Q111) cells, with isoflurane having the largest effect.	Isoflurane	0-10	huntingtin	Mus musculus	73-83
21059370-6	2011	Isoflurane, sevoflurane, and desflurane all increased the aggregation of huntingtin in STHdh(Q111/Q111) cells, with isoflurane having the largest effect.	Sevoflurane	12-23	huntingtin	Mus musculus	73-83
21059370-6	2011	Isoflurane, sevoflurane, and desflurane all increased the aggregation of huntingtin in STHdh(Q111/Q111) cells, with isoflurane having the largest effect.	Desflurane	29-39	huntingtin	Mus musculus	73-83
21059370-6	2011	Isoflurane, sevoflurane, and desflurane all increased the aggregation of huntingtin in STHdh(Q111/Q111) cells, with isoflurane having the largest effect.	Isoflurane	116-126	huntingtin	Mus musculus	73-83
21059370-7	2011	Isoflurane induced greater calcium release from the ER and relatively more cell damage in the STHdh(Q111/Q111) huntingtin cells than in the wild type STHdh(Q7/Q7) striatal cells.	Isoflurane	0-10	huntingtin	Mus musculus	111-121
21059370-9	2011	Xestospongin C inhibited the isoflurane-induced calcium release from the ER, aggregation of huntingtin, and cell damage in the STHdh(Q111/Q111) cells.	xestospongin C	0-14	huntingtin	Mus musculus	92-102
21059370-9	2011	Xestospongin C inhibited the isoflurane-induced calcium release from the ER, aggregation of huntingtin, and cell damage in the STHdh(Q111/Q111) cells.	Isoflurane	29-39	huntingtin	Mus musculus	92-102
21059370-10	2011	In summary, the Q111 form of huntingtin increases the vulnerability of striatal neurons to isoflurane neurotoxicity through combined actions on the ER IP(3) receptors.	Isoflurane	91-101	huntingtin	Mus musculus	29-39
21059370-11	2011	Calcium release from the ER contributes to the anesthetic induced huntingtin aggregation in STHdh(Q111/Q111) striatal cells.	Calcium	0-7	huntingtin	Mus musculus	66-76
21248135-1	2011	In Huntington"s disease (HD), the expansion of polyglutamine (polyQ) repeats at the N terminus of the ubiquitous protein huntingtin (htt) leads to neurodegeneration in specific brain areas.	polyglutamine	47-60	huntingtin	Mus musculus	133-136
21248135-1	2011	In Huntington"s disease (HD), the expansion of polyglutamine (polyQ) repeats at the N terminus of the ubiquitous protein huntingtin (htt) leads to neurodegeneration in specific brain areas.	polyglutamine	62-67	huntingtin	Mus musculus	121-131
21248135-1	2011	In Huntington"s disease (HD), the expansion of polyglutamine (polyQ) repeats at the N terminus of the ubiquitous protein huntingtin (htt) leads to neurodegeneration in specific brain areas.	polyglutamine	62-67	huntingtin	Mus musculus	133-136
22180703-2	2011	It is caused by expansion of a polyglutamine tract within the N-terminal domain of the Huntingtin protein.	polyglutamine	31-44	huntingtin	Mus musculus	87-97
22180703-8	2011	We then discuss how potential loss-of-function phenotypes resulting in polyglutamine expansion within Huntingtin may have direct relevance to the underlying pathophysiology of Huntington"s Disease.	polyglutamine	71-84	huntingtin	Mus musculus	102-112
21907096-1	2011	Huntington"s disease (HD) is an autosomal dominant, progressive, and fatal neurodegenerative disorder caused by an expanded polyglutamine cytosine-adenine-guanine repeat in the gene coding for the protein huntingtin.	polyglutamine cytosine-adenine-guanine	124-162	huntingtin	Mus musculus	205-215
21336284-1	2011	Huntington"s disease is an inherited and incurable neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in huntingtin (encoded by HTT).	polyglutamine	100-113	huntingtin	Mus musculus	135-145
21336284-1	2011	Huntington"s disease is an inherited and incurable neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in huntingtin (encoded by HTT).	polyglutamine	100-113	huntingtin	Mus musculus	158-161
21336284-1	2011	Huntington"s disease is an inherited and incurable neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in huntingtin (encoded by HTT).	polyglutamine	115-120	huntingtin	Mus musculus	135-145
21336284-1	2011	Huntington"s disease is an inherited and incurable neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in huntingtin (encoded by HTT).	polyglutamine	115-120	huntingtin	Mus musculus	158-161
22216210-1	2011	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by a trinucleotide (CAG)(n) repeat expansion in the coding sequence of the huntingtin gene, and an expanded polyglutamine (&gt;37Q) tract in the protein.	trinucleotide	95-108	huntingtin	Mus musculus	165-175
20736066-1	2011	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) repeat in exon-1 in the Huntingtin gene (HTT).	polyglutamine	113-126	huntingtin	Mus musculus	159-169
20736066-1	2011	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) repeat in exon-1 in the Huntingtin gene (HTT).	polyglutamine	113-126	huntingtin	Mus musculus	176-179
20736066-1	2011	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) repeat in exon-1 in the Huntingtin gene (HTT).	polyglutamine	128-133	huntingtin	Mus musculus	159-169
20736066-1	2011	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by an expansion of the polyglutamine (polyQ) repeat in exon-1 in the Huntingtin gene (HTT).	polyglutamine	128-133	huntingtin	Mus musculus	176-179
22216210-1	2011	Huntington"s disease (HD) is a fatal autosomal dominant neurodegenerative disorder caused by a trinucleotide (CAG)(n) repeat expansion in the coding sequence of the huntingtin gene, and an expanded polyglutamine (&gt;37Q) tract in the protein.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	110-113	huntingtin	Mus musculus	165-175
21887328-1	2011	Huntington"s disease (HD) is caused by the expansion of N-terminal polymorphic poly Q stretch of the protein huntingtin (HTT).	polyglutamine	79-85	huntingtin	Mus musculus	109-119
21897851-1	2011	BACKGROUND: Age at onset of Huntington"s disease (HD) is largely determined by the CAG trinucleotide repeat length in the HTT gene.	trinucleotide	87-100	huntingtin	Mus musculus	122-125
21713039-1	2011	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disease caused by a CAG trinucleotide expansion in the Huntingtin (Htt) gene.	trinucleotide	85-98	huntingtin	Mus musculus	116-126
21713039-1	2011	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disease caused by a CAG trinucleotide expansion in the Huntingtin (Htt) gene.	trinucleotide	85-98	huntingtin	Mus musculus	128-131
21713039-2	2011	The expanded CAG repeats are translated into polyglutamine (polyQ), causing aberrant functions as well as aggregate formation of mutant Htt.	polyglutamine	45-58	huntingtin	Mus musculus	136-139
21713039-2	2011	The expanded CAG repeats are translated into polyglutamine (polyQ), causing aberrant functions as well as aggregate formation of mutant Htt.	polyglutamine	60-65	huntingtin	Mus musculus	136-139
21713039-10	2011	Most importantly, addition of T1-11 (0.05 mg/ml) to the drinking water of a transgenic mouse model of HD (R6/2) ameliorated the progressive deterioration in motor coordination, reduced the formation of striatal Htt aggregates, elevated proteasome activity, and increased the level of an important neurotrophic factor (brain derived neurotrophic factor) in the brain.	t1-11	30-35	huntingtin	Mus musculus	211-214
21677773-3	2011	In parallel, several reports have demonstrated a role for histone deacetylase 6 (HDAC6) in the modulation of the toxicity caused by the accumulation of misfolded proteins, including that of expanded polyglutamine in an N-terminal huntingtin fragment.	polyglutamine	199-212	huntingtin	Mus musculus	230-240
21156064-1	2010	BACKGROUND: The mutation in Huntington"s disease is a polyglutamine expansion near the N-terminus of huntingtin.	polyglutamine	54-67	huntingtin	Mus musculus	101-111
21156064-2	2010	Huntingtin expressed in immortalized neurons is cleaved near the N-terminus to form N-terminal polypeptides known as cleavage products A and B (cpA and cpB).	cpb	152-155	huntingtin	Mus musculus	0-10
21156064-5	2010	RESULTS: Delivery of htt cDNA into the mouse striatum using adeno-associated virus or into primary cortical neurons using lentivirus generated cpA and cpB, indicating that neurons in brain and in vitro can form these fragments.	cpb	151-154	huntingtin	Mus musculus	21-24
21156064-10	2010	LY-411,575 or DAPT also increased survival of primary neurons expressing endogenous full-length mutant huntingtin.	Lysine	0-2	huntingtin	Mus musculus	103-113
21156064-10	2010	LY-411,575 or DAPT also increased survival of primary neurons expressing endogenous full-length mutant huntingtin.	dapt	14-18	huntingtin	Mus musculus	103-113
21156064-11	2010	CONCLUSION: We show that cpA and cpB are produced from a larger huntingtin fragment in vivo in mouse brain and in primary neuron cultures.	cpb	33-36	huntingtin	Mus musculus	64-74
21887328-1	2011	Huntington"s disease (HD) is caused by the expansion of N-terminal polymorphic poly Q stretch of the protein huntingtin (HTT).	polyglutamine	79-85	huntingtin	Mus musculus	121-124
21044321-1	2010	Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain.	Glutamine	49-58	huntingtin	Mus musculus	111-121
20935460-7	2010	Early and sustained expression of: autophagy-related proteins in this genetically precise mouse model of HD suggests that alteration of autophagic flux is an important and early component of neuronal response to polyglutamine expanded huntingtin.	polyglutamine	212-225	huntingtin	Mus musculus	235-245
21931779-1	2011	Abnormalities in mitochondrial function and epigenetic regulation are thought to be instrumental in Huntington"s disease (HD), a fatal genetic disorder caused by an expanded polyglutamine track in the protein huntingtin.	polyglutamine	174-187	huntingtin	Mus musculus	209-219
21044321-1	2010	Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain.	Glutamine	49-58	huntingtin	Mus musculus	123-126
21044321-1	2010	Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain.	Glutamine	71-81	huntingtin	Mus musculus	111-121
21044321-1	2010	Huntington"s disease results from expansion of a glutamine repeat (>36 glutamines) in the N-terminal region of huntingtin (htt) and is characterized by preferential neurodegeneration in the striatum of the brain.	Glutamine	71-81	huntingtin	Mus musculus	123-126
21044321-2	2010	N171-82Q mice that express N-terminal 171 amino acids of htt with an 82-glutamine repeat show severe neurological phenotypes and die early, suggesting that N-terminal mutant htt is pathogenic.	Glutamine	72-81	huntingtin	Mus musculus	57-60
21044321-2	2010	N171-82Q mice that express N-terminal 171 amino acids of htt with an 82-glutamine repeat show severe neurological phenotypes and die early, suggesting that N-terminal mutant htt is pathogenic.	Glutamine	72-81	huntingtin	Mus musculus	174-177
20467442-7	2010	Moreover, Omi-induced autophagy facilitates the degradation of neurodegenerative proteins such as pathogenic A53T alpha-synuclein and truncated polyglutamine-expanded huntingtin, as well as the endogenous autophagy substrate p62.	polyglutamine	144-157	huntingtin	Mus musculus	167-177
20668093-1	2010	Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (HTT) gene.	trinucleotide	90-103	huntingtin	Mus musculus	128-138
20668093-1	2010	Huntington"s disease (HD) is a neurodegenerative disease caused by the expansion of a CAG trinucleotide repeat in exon 1 of the huntingtin (HTT) gene.	trinucleotide	90-103	huntingtin	Mus musculus	140-143
20668093-4	2010	Chronic treatment of R6/2 mice with an agonist of PPARgamma (thiazolidinedione, TZD) rescued progressive weight loss, motor deterioration, formation of mutant Htt aggregates, jeopardized global ubiquitination profiles, reduced expression of two neuroprotective proteins (brain-derived neurotrophic factor and Bcl-2) and shortened life span exhibited by these mice.	2,4-thiazolidinedione	61-78	huntingtin	Mus musculus	159-162
20668093-4	2010	Chronic treatment of R6/2 mice with an agonist of PPARgamma (thiazolidinedione, TZD) rescued progressive weight loss, motor deterioration, formation of mutant Htt aggregates, jeopardized global ubiquitination profiles, reduced expression of two neuroprotective proteins (brain-derived neurotrophic factor and Bcl-2) and shortened life span exhibited by these mice.	tzd	80-83	huntingtin	Mus musculus	159-162
20668093-5	2010	By reducing HTT aggregates and, thus, ameliorating the recruitment of PPARgamma into HTT aggregates, chronic TZD treatment also elevated the availability of the PPARgamma protein and subsequently normalized the expression of two of its downstream genes (the glucose transporter type 4 and PPARgamma coactivator-1 alpha genes).	tzd	109-112	huntingtin	Mus musculus	12-15
20668093-5	2010	By reducing HTT aggregates and, thus, ameliorating the recruitment of PPARgamma into HTT aggregates, chronic TZD treatment also elevated the availability of the PPARgamma protein and subsequently normalized the expression of two of its downstream genes (the glucose transporter type 4 and PPARgamma coactivator-1 alpha genes).	tzd	109-112	huntingtin	Mus musculus	85-88
20668093-5	2010	By reducing HTT aggregates and, thus, ameliorating the recruitment of PPARgamma into HTT aggregates, chronic TZD treatment also elevated the availability of the PPARgamma protein and subsequently normalized the expression of two of its downstream genes (the glucose transporter type 4 and PPARgamma coactivator-1 alpha genes).	Glucose	258-265	huntingtin	Mus musculus	12-15
20668093-5	2010	By reducing HTT aggregates and, thus, ameliorating the recruitment of PPARgamma into HTT aggregates, chronic TZD treatment also elevated the availability of the PPARgamma protein and subsequently normalized the expression of two of its downstream genes (the glucose transporter type 4 and PPARgamma coactivator-1 alpha genes).	Glucose	258-265	huntingtin	Mus musculus	85-88
20838238-1	2010	Huntington disease (HD) is a progressive neurodegenerative disease caused by an expansion of a polyglutamine sequence in mutant huntingtin (mhtt) that produces abnormal folding and aggregation that results in the formation of nuclear and cytoplasmic neuronal inclusion bodies.	polyglutamine	95-108	huntingtin	Mus musculus	128-138
20980587-0	2010	Phosphorylation of huntingtin at Ser421 in YAC128 neurons is associated with protection of YAC128 neurons from NMDA-mediated excitotoxicity and is modulated by PP1 and PP2A.	N-Methylaspartate	111-115	huntingtin	Mus musculus	19-29
20547568-3	2010	Recently, we discovered that expression of mutant HTT is associated with impaired manganese (Mn) uptake following overexposure in a striatal neuronal cell line and mouse model of HD.	Manganese	82-91	huntingtin	Mus musculus	50-53
20558522-1	2010	Huntington"s disease (HD) is an incurable autosomal-dominant neurodegenerative disorder initiated by an abnormally expanded polyglutamine domain in the huntingtin protein.	polyglutamine	124-137	huntingtin	Mus musculus	152-162
20639122-7	2010	The Tet/HD94 conditional mouse model allowed us to demonstrate that increased carbonylation in striatum is dependent on mutant huntingtin expression.	tetramethylenedisulfotetramine	4-7	huntingtin	Mus musculus	127-137
20005957-2	2010	In vitro, expression of UBB(+1) and mutant huntingtin synergistically increase aggregate formation and polyglutamine induced cell death.	polyglutamine	103-116	huntingtin	Mus musculus	43-53
20494921-0	2010	In vivo expression of polyglutamine-expanded huntingtin by mouse striatal astrocytes impairs glutamate transport: a correlation with Huntington"s disease subjects.	polyglutamine	22-35	huntingtin	Mus musculus	45-55
20494921-0	2010	In vivo expression of polyglutamine-expanded huntingtin by mouse striatal astrocytes impairs glutamate transport: a correlation with Huntington"s disease subjects.	Glutamic Acid	93-102	huntingtin	Mus musculus	45-55
20494921-4	2010	Astrocytes expressing mHtt developed a progressive phenotype of reactive astrocytes that was characterized by a marked decreased expression of both glutamate transporters, GLAST and GLT-1, and of glutamate uptake.	Glutamic Acid	148-157	huntingtin	Mus musculus	22-26
20494921-10	2010	These findings suggest that the presence of mHtt in astrocytes alters glial glutamate transport capacity early in the disease process and may contribute to HD pathogenesis.	Glutamic Acid	76-85	huntingtin	Mus musculus	44-48
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	polyglutamine	44-57	huntingtin	Mus musculus	7-17
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	polyglutamine	44-57	huntingtin	Mus musculus	19-22
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	polyglutamine	44-57	huntingtin	Mus musculus	129-132
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	polyglutamine	59-64	huntingtin	Mus musculus	7-17
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	polyglutamine	59-64	huntingtin	Mus musculus	19-22
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	polyglutamine	59-64	huntingtin	Mus musculus	129-132
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	Glutamine	79-89	huntingtin	Mus musculus	7-17
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	Glutamine	79-89	huntingtin	Mus musculus	19-22
20519964-1	2010	Mutant huntingtin (htt) carries an expanded polyglutamine (polyQ) repeat (> 36 glutamines) in its N-terminal region, which leads htt to become misfolded and kill neuronal cells in Huntington disease (HD).	Glutamine	79-89	huntingtin	Mus musculus	129-132
20569486-8	2010	In muscle but not brain, everolimus significantly decreased soluble mutant huntingtin levels.	Everolimus	25-35	huntingtin	Mus musculus	75-85
20147317-1	2010	Huntingtin protein (Htt) is ubiquitously expressed, yet Huntington"s disease (HD), a fatal neurologic disorder produced by expansion of an Htt polyglutamine tract, is characterized by neurodegeneration that occurs primarily in the striatum and cerebral cortex.	polyglutamine	143-156	huntingtin	Mus musculus	0-10
20147317-1	2010	Huntingtin protein (Htt) is ubiquitously expressed, yet Huntington"s disease (HD), a fatal neurologic disorder produced by expansion of an Htt polyglutamine tract, is characterized by neurodegeneration that occurs primarily in the striatum and cerebral cortex.	polyglutamine	143-156	huntingtin	Mus musculus	20-23
20147317-1	2010	Huntingtin protein (Htt) is ubiquitously expressed, yet Huntington"s disease (HD), a fatal neurologic disorder produced by expansion of an Htt polyglutamine tract, is characterized by neurodegeneration that occurs primarily in the striatum and cerebral cortex.	polyglutamine	143-156	huntingtin	Mus musculus	139-142
20147317-6	2010	In a brain-slice explant model of HD, knock-down of CalDAG-GEFI expression rescues striatal neurons from pathology induced by transfection of polyglutamine-expanded Htt exon 1.	polyglutamine	142-155	huntingtin	Mus musculus	165-168
20084070-1	2010	OBJECTIVE: Mice deficient of the serotonin transporter (5-HTT ko) mice have a reduced brain serotonin content and develop late-onset obesity.	Serotonin	33-42	huntingtin	Mus musculus	58-61
20084070-10	2010	CONCLUSIONS: We propose that low brain serotonin level due to the 5-HTT ko genotype leads to reduced physical activity and low BDNF, which together with the lack of fasting-induced hypothalamic BDNF and LR production results in late-onset obesity.	Serotonin	39-48	huntingtin	Mus musculus	68-71
20448484-1	2010	Previous studies have reported that mutant huntingtin (htt) interferes with cyclic AMP response element binding protein binding protein (CBP)-mediated transcription, possibly by inhibiting the acetylation of histones.	Cyclic AMP	76-86	huntingtin	Mus musculus	43-53
20448484-1	2010	Previous studies have reported that mutant huntingtin (htt) interferes with cyclic AMP response element binding protein binding protein (CBP)-mediated transcription, possibly by inhibiting the acetylation of histones.	Cyclic AMP	76-86	huntingtin	Mus musculus	55-58
20424159-1	2010	We recently reported that the small G-protein Rhes has the properties of a SUMO-E3 ligase and mediates mutant huntingtin (mHtt) cytotoxicity.	mhtt	122-126	huntingtin	Mus musculus	110-120
20227407-1	2010	Huntington"s disease (HD) is an autosomal dominant disorder caused by expansion of polyglutamine repeats in the huntingtin gene leading to loss of striatal and cortical neurons followed by deficits in cognition and choreic movements.	polyglutamine	83-96	huntingtin	Mus musculus	112-122
20354076-1	2010	An expanded polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt) causes misfolding and accumulation of htt in neuronal cells and the subsequent neurodegeneration of Huntington"s disease (HD).	polyglutamine	12-25	huntingtin	Mus musculus	69-79
20354076-1	2010	An expanded polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt) causes misfolding and accumulation of htt in neuronal cells and the subsequent neurodegeneration of Huntington"s disease (HD).	polyglutamine	12-25	huntingtin	Mus musculus	81-84
20354076-1	2010	An expanded polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt) causes misfolding and accumulation of htt in neuronal cells and the subsequent neurodegeneration of Huntington"s disease (HD).	polyglutamine	12-25	huntingtin	Mus musculus	124-127
20354076-1	2010	An expanded polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt) causes misfolding and accumulation of htt in neuronal cells and the subsequent neurodegeneration of Huntington"s disease (HD).	polyglutamine	27-32	huntingtin	Mus musculus	69-79
20354076-1	2010	An expanded polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt) causes misfolding and accumulation of htt in neuronal cells and the subsequent neurodegeneration of Huntington"s disease (HD).	polyglutamine	27-32	huntingtin	Mus musculus	81-84
20354076-1	2010	An expanded polyglutamine (polyQ) domain in the N-terminal region of huntingtin (htt) causes misfolding and accumulation of htt in neuronal cells and the subsequent neurodegeneration of Huntington"s disease (HD).	polyglutamine	27-32	huntingtin	Mus musculus	124-127
20497470-1	2010	Huntington"s disease (HD) is a devastating neurodegenerative disorder caused by an expanded polyglutamine repeat within the N-terminus of the huntingtin protein.	polyglutamine	92-105	huntingtin	Mus musculus	142-152
20190273-1	2010	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease caused by a polyglutamine expansion in huntingtin.	polyglutamine	89-102	huntingtin	Mus musculus	116-126
20190273-9	2010	Rilmenidine administration attenuated the signs of disease in a HD mouse model and reduced levels of the mutant huntingtin fragment.	Rilmenidine	0-11	huntingtin	Mus musculus	112-122
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	Mus musculus	64-68
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	Mus musculus	64-68
20454921-6	2010	Dysfunctional astrocytic mitochondria in cortico-striatal tripartite synapses might be particularly relevant in the pathogenesis of juvenile/infantile HD, frequently associated with seizures and abnormally large mHtt polyglutamine expansions.	polyglutamine	217-230	huntingtin	Mus musculus	212-216
20461451-6	2010	In affected individuals, the mutant HD protein (Huntingtin, mHtt) thus contains an extended polyglutamine repeat.	polyglutamine	92-105	huntingtin	Mus musculus	60-64
21331299-4	2010	In this study we found that GSPE treatment significantly inhibits polyQ aggregation in phaeochromocytoma (PC)-12 cell line containing an ecdysone-inducible protein comprising the first 17 amino acid of huntingtin plus 103 glutamines fused with enhanced GFP.	Ecdysone	137-145	huntingtin	Mus musculus	202-212
20439996-4	2010	Mutant Htt interacts with Ku70, impairs DNA-dependent protein kinase function in nonhomologous end joining, and consequently increases DSB accumulation.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	135-138	huntingtin	Mus musculus	7-10
20420689-1	2010	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	82-95	huntingtin	Mus musculus	117-127
20420689-1	2010	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	82-95	huntingtin	Mus musculus	137-140
20420689-1	2010	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	97-102	huntingtin	Mus musculus	117-127
20420689-1	2010	BACKGROUND: Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) expansion in Huntingtin protein (Htt).	polyglutamine	97-102	huntingtin	Mus musculus	137-140
20145253-1	2010	Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) repeat (>37Q) in huntingtin (htt), and age of onset is inversely correlated with the length of the polyQ repeat.	polyglutamine	57-70	huntingtin	Mus musculus	96-106
20145253-1	2010	Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) repeat (>37Q) in huntingtin (htt), and age of onset is inversely correlated with the length of the polyQ repeat.	polyglutamine	57-70	huntingtin	Mus musculus	108-111
20145253-1	2010	Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) repeat (>37Q) in huntingtin (htt), and age of onset is inversely correlated with the length of the polyQ repeat.	polyglutamine	72-77	huntingtin	Mus musculus	96-106
20145253-1	2010	Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) repeat (>37Q) in huntingtin (htt), and age of onset is inversely correlated with the length of the polyQ repeat.	polyglutamine	72-77	huntingtin	Mus musculus	108-111
20145253-1	2010	Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) repeat (>37Q) in huntingtin (htt), and age of onset is inversely correlated with the length of the polyQ repeat.	polyglutamine	178-183	huntingtin	Mus musculus	96-106
20145253-1	2010	Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) repeat (>37Q) in huntingtin (htt), and age of onset is inversely correlated with the length of the polyQ repeat.	polyglutamine	178-183	huntingtin	Mus musculus	108-111
20145253-2	2010	Mutant htt with expanded polyQ is ubiquitously expressed in various types of cells, including glia, but causes selective neurodegeneration.	polyglutamine	25-30	huntingtin	Mus musculus	7-10
20145253-3	2010	Our recent study demonstrated that expression of the N-terminal mutant htt with a large polyQ repeat (160Q) in astrocytes is sufficient to induce neurological symptoms in mice (Bradford, J., Shin, J. Y., Roberts, M., Wang, C. E., Li, X.-J., and Li, S. H. (2009) Proc.	polyglutamine	88-93	huntingtin	Mus musculus	71-74
20145253-11	2010	However, htt-98Q mice show increased susceptibility to glutamate-induced seizure.	Glutamic Acid	55-64	huntingtin	Mus musculus	9-12
20190739-1	2010	Huntington"s Disease (HD) is a dominantly inherited pathology caused by the accumulation of mutant huntingtin protein (HTT) containing an expanded polyglutamine (polyQ) tract.	polyglutamine	147-160	huntingtin	Mus musculus	99-109
20053912-1	2010	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin protein (Htt).	polyglutamine	90-103	huntingtin	Mus musculus	121-131
20190739-1	2010	Huntington"s Disease (HD) is a dominantly inherited pathology caused by the accumulation of mutant huntingtin protein (HTT) containing an expanded polyglutamine (polyQ) tract.	polyglutamine	147-160	huntingtin	Mus musculus	119-122
20190739-1	2010	Huntington"s Disease (HD) is a dominantly inherited pathology caused by the accumulation of mutant huntingtin protein (HTT) containing an expanded polyglutamine (polyQ) tract.	polyglutamine	162-167	huntingtin	Mus musculus	99-109
20190739-1	2010	Huntington"s Disease (HD) is a dominantly inherited pathology caused by the accumulation of mutant huntingtin protein (HTT) containing an expanded polyglutamine (polyQ) tract.	polyglutamine	162-167	huntingtin	Mus musculus	119-122
19996106-3	2010	Mutant Huntingtin with expanded polyglutamine (polyQ) and the V66M polymorphism of BDNF reduce the dendritic distribution and axonal transport of BDNF.	polyglutamine	32-45	huntingtin	Mus musculus	7-17
19996106-3	2010	Mutant Huntingtin with expanded polyglutamine (polyQ) and the V66M polymorphism of BDNF reduce the dendritic distribution and axonal transport of BDNF.	polyglutamine	47-52	huntingtin	Mus musculus	7-17
19996106-5	2010	Here, we report that Huntingtin-associated protein-1 (HAP1) interacts with the prodomain of BDNF and that the interaction was reduced in the presence of polyQ-expanded Huntingtin and BDNF V66M.	polyglutamine	153-158	huntingtin	Mus musculus	21-31
20140187-0	2010	Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice.	polyglutamine	27-40	huntingtin	Mus musculus	16-26
20140187-1	2010	Expansion of a stretch of polyglutamine in huntingtin (htt), the protein product of the IT15 gene, causes Huntington"s disease (HD).	polyglutamine	26-39	huntingtin	Mus musculus	43-53
20140187-1	2010	Expansion of a stretch of polyglutamine in huntingtin (htt), the protein product of the IT15 gene, causes Huntington"s disease (HD).	polyglutamine	26-39	huntingtin	Mus musculus	55-58
20140187-1	2010	Expansion of a stretch of polyglutamine in huntingtin (htt), the protein product of the IT15 gene, causes Huntington"s disease (HD).	polyglutamine	26-39	huntingtin	Mus musculus	88-92
20140187-2	2010	Previous investigations into the role of the polyglutamine stretch (polyQ) in htt function have suggested that its length may modulate a normal htt function involved in regulating energy homeostasis.	polyglutamine	45-58	huntingtin	Mus musculus	78-81
20140187-2	2010	Previous investigations into the role of the polyglutamine stretch (polyQ) in htt function have suggested that its length may modulate a normal htt function involved in regulating energy homeostasis.	polyglutamine	45-58	huntingtin	Mus musculus	144-147
20140187-2	2010	Previous investigations into the role of the polyglutamine stretch (polyQ) in htt function have suggested that its length may modulate a normal htt function involved in regulating energy homeostasis.	polyglutamine	68-73	huntingtin	Mus musculus	78-81
20140187-2	2010	Previous investigations into the role of the polyglutamine stretch (polyQ) in htt function have suggested that its length may modulate a normal htt function involved in regulating energy homeostasis.	polyglutamine	68-73	huntingtin	Mus musculus	144-147
20140187-3	2010	Here we show that expression of full-length htt lacking its polyglutamine stretch (DeltaQ-htt) in a knockin mouse model for HD (Hdh(140Q/DeltaQ)), reduces significantly neuropil mutant htt aggregates, ameliorates motor/behavioral deficits, and extends lifespan in comparison to the HD model mice (Hdh(140Q/+)).	polyglutamine	60-73	huntingtin	Mus musculus	44-47
20140187-3	2010	Here we show that expression of full-length htt lacking its polyglutamine stretch (DeltaQ-htt) in a knockin mouse model for HD (Hdh(140Q/DeltaQ)), reduces significantly neuropil mutant htt aggregates, ameliorates motor/behavioral deficits, and extends lifespan in comparison to the HD model mice (Hdh(140Q/+)).	polyglutamine	60-73	huntingtin	Mus musculus	90-93
19745829-6	2010	The analysis of the conditional mouse model Tet/HD94 disclosed that after mutant huntingtin shutdown PHLPP1 levels returned to wild-type levels whereas phospho-Akt levels were partially reduced.	tetramethylenedisulfotetramine	44-47	huntingtin	Mus musculus	81-91
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	Mus musculus	293-303
20053912-1	2010	Huntington"s disease (HD) is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin protein (Htt).	polyglutamine	90-103	huntingtin	Mus musculus	141-144
20053912-5	2010	mGluR1/5-mediated inositol phosphate (InsP) formation is desensitized in striatal slices from Hdh(Q111/Q111) mice and this desensitization is PKC-mediated.	Inositol Phosphates	18-36	huntingtin	Mus musculus	94-97
20053912-5	2010	mGluR1/5-mediated inositol phosphate (InsP) formation is desensitized in striatal slices from Hdh(Q111/Q111) mice and this desensitization is PKC-mediated.	Inositol Phosphates	38-42	huntingtin	Mus musculus	94-97
20053912-6	2010	Despite of decreased InsP formation, (S)-3,5-dihydroxylphenylglycine (DHPG)-mediated Ca(2+) release is higher in Hdh(Q111/Q111) than in Hdh(Q20/Q20) neurons.	3,5-dihydroxyphenylglycine	37-68	huntingtin	Mus musculus	113-116
20053912-6	2010	Despite of decreased InsP formation, (S)-3,5-dihydroxylphenylglycine (DHPG)-mediated Ca(2+) release is higher in Hdh(Q111/Q111) than in Hdh(Q20/Q20) neurons.	3,5-dihydroxyphenylglycine	37-68	huntingtin	Mus musculus	136-139
20053912-6	2010	Despite of decreased InsP formation, (S)-3,5-dihydroxylphenylglycine (DHPG)-mediated Ca(2+) release is higher in Hdh(Q111/Q111) than in Hdh(Q20/Q20) neurons.	dhpg	70-74	huntingtin	Mus musculus	113-116
20053912-6	2010	Despite of decreased InsP formation, (S)-3,5-dihydroxylphenylglycine (DHPG)-mediated Ca(2+) release is higher in Hdh(Q111/Q111) than in Hdh(Q20/Q20) neurons.	dhpg	70-74	huntingtin	Mus musculus	136-139
20053912-10	2010	PKC inhibition not only brings Hdh(Q111/Q111) DHPG-stimulated InsP formation to Hdh(Q20/Q20) levels, but also causes an increase in neuronal cell death in Hdh(Q111/Q111) neurons.	dhpg	46-50	huntingtin	Mus musculus	31-34
20053912-10	2010	PKC inhibition not only brings Hdh(Q111/Q111) DHPG-stimulated InsP formation to Hdh(Q20/Q20) levels, but also causes an increase in neuronal cell death in Hdh(Q111/Q111) neurons.	dhpg	46-50	huntingtin	Mus musculus	80-83
20053912-10	2010	PKC inhibition not only brings Hdh(Q111/Q111) DHPG-stimulated InsP formation to Hdh(Q20/Q20) levels, but also causes an increase in neuronal cell death in Hdh(Q111/Q111) neurons.	dhpg	46-50	huntingtin	Mus musculus	80-83
19591939-8	2009	However, Y-27632 treatment improved rotarod performance significantly, and also reduced soluble brain Htt levels.	Y 27632	9-16	huntingtin	Mus musculus	102-105
19845833-3	2010	We report that striatal cells expressing mutant Huntingtin exhibit elevated sensitivity to cadmium toxicity and resistance to manganese toxicity.	Cadmium	91-98	huntingtin	Mus musculus	48-58
19845833-3	2010	We report that striatal cells expressing mutant Huntingtin exhibit elevated sensitivity to cadmium toxicity and resistance to manganese toxicity.	Manganese	126-135	huntingtin	Mus musculus	48-58
20064390-1	2009	The N-terminal 17 amino acids of huntingtin (NT17) can be phosphorylated on serines 13 and 16; however, the significance of these modifications in Huntington"s disease pathogenesis remains unknown.	Serine	76-83	huntingtin	Mus musculus	33-43
20064390-2	2009	In this study, we developed BAC transgenic mice expressing full-length mutant huntingtin (fl-mhtt) with serines 13 and 16 mutated to either aspartate (phosphomimetic or SD) or alanine (phosphoresistant or SA).	Serine	104-111	huntingtin	Mus musculus	78-88
20064390-5	2009	Moreover, modification of these serines in expanded repeat huntingtin peptides modulates aggregation and amyloid fibril formation in vitro.	Serine	32-39	huntingtin	Mus musculus	59-69
20064390-6	2009	Together, our findings demonstrate that serines 13 and 16 are critical determinants of fl-mhtt-induced disease pathogenesis in vivo, supporting the targeting of huntingtin NT17 domain and its modifications in HD therapy.	fl-mhtt	87-94	huntingtin	Mus musculus	161-171
19733666-5	2009	Analysis of the conditional mouse model Tet/HD94 showed that mutant huntingtin specifically controls calcineurin A protein levels.	tetramethylenedisulfotetramine	40-43	huntingtin	Mus musculus	68-78
19845833-8	2010	Thus, this disease-toxicant interaction screen has revealed that expression of mutant Huntingtin results in heightened sensitivity to cadmium neurotoxicity and a selective impairment of manganese accumulation.	Cadmium	134-141	huntingtin	Mus musculus	86-96
19845833-8	2010	Thus, this disease-toxicant interaction screen has revealed that expression of mutant Huntingtin results in heightened sensitivity to cadmium neurotoxicity and a selective impairment of manganese accumulation.	Manganese	186-195	huntingtin	Mus musculus	86-96
20018729-1	2009	Huntington disease (HD) is an inherited neurological disorder caused by a polyglutamine expansion in the protein huntingtin and is characterized by selective neurodegeneration that preferentially occurs in striatal medium spiny neurons.	polyglutamine	74-87	huntingtin	Mus musculus	113-123
20018729-6	2009	We generated transgenic mice that express N-terminal mutant huntingtin in astrocytes, a major type of glial cell that remove extracellular glutamate in the brain.	Glutamic Acid	139-148	huntingtin	Mus musculus	60-70
19591939-0	2009	Y-27632 improves rotarod performance and reduces huntingtin levels in R6/2 mice.	Y 27632	0-7	huntingtin	Mus musculus	49-59
19591939-6	2009	We then initiated a trial in R6/2 mice, which express Htt exon 1, administering 100 mg/kg/day of Y-27632 in drinking water.	Y 27632	97-104	huntingtin	Mus musculus	54-57
19956633-1	2009	BACKGROUND: Huntington"s disease (HD) is an inherited progressive neurodegenerative disorder caused by a CAG repeat expansion in the ubiquitously expressed HD gene resulting in an abnormally long polyglutamine repeat in the huntingtin protein.	polyglutamine	196-209	huntingtin	Mus musculus	224-234
19622387-2	2009	This polyglutamine expansion within huntingtin is the causative factor in the pathogenesis of HD, however the underlying mechanisms have not been fully elucidated.	polyglutamine	5-18	huntingtin	Mus musculus	36-46
19622387-6	2009	Further, respiration in mitochondria from these mutant huntingtin-expressing cells is inhibited at significantly lower calcium concentrations compared to mitochondria from wild-type cells.	Calcium	119-126	huntingtin	Mus musculus	55-65
19622387-7	2009	Considering these and other findings this review explores the evidence suggesting that mutant huntingtin, directly or indirectly impairs mitochondrial function, which compromises cytosolic and mitochondrial calcium homeostasis, and contributes to neuronal dysfunction and death in HD.	Calcium	207-214	huntingtin	Mus musculus	94-104
19864571-1	2009	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease resulting from the expansion of a glutamine repeat in the huntingtin (Htt) protein.	Glutamine	111-120	huntingtin	Mus musculus	135-145
19699304-1	2009	The Huntington"s disease (HD) mutation causes polyglutamine expansion in huntingtin (Htt) and neurodegeneration.	polyglutamine	46-59	huntingtin	Mus musculus	73-83
19699304-1	2009	The Huntington"s disease (HD) mutation causes polyglutamine expansion in huntingtin (Htt) and neurodegeneration.	polyglutamine	46-59	huntingtin	Mus musculus	85-88
19551467-1	2009	Huntington"s disease (HD) is an autosomal dominantly inherited disorder, caused by an expanded polyglutamine region of a protein called huntingtin.	polyglutamine	95-108	huntingtin	Mus musculus	136-146
19566678-0	2009	Polyglutamine expansion in huntingtin alters its interaction with phospholipids.	polyglutamine	0-13	huntingtin	Mus musculus	27-37
19566678-0	2009	Polyglutamine expansion in huntingtin alters its interaction with phospholipids.	Phospholipids	66-79	huntingtin	Mus musculus	27-37
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	phosphoinositol	201-216	huntingtin	Mus musculus	29-39
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	phosphoinositol	201-216	huntingtin	Mus musculus	88-98
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	pi 3,4-bisphosphate	222-241	huntingtin	Mus musculus	29-39
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	pi 3,4-bisphosphate	222-241	huntingtin	Mus musculus	88-98
19860865-1	2009	BACKGROUND: Huntington"s disease (HD) is an inherited neurogenerative disease caused by an abnormal expansion of glutamine repeats in the huntingtin protein.	Glutamine	113-122	huntingtin	Mus musculus	138-148
19860865-9	2009	FK506 restored BDNF transport in two complementary models: rat primary neuronal cultures expressing mutant huntingtin and mouse cortical neurons from Hdh(Q111/Q111) HD knock-in mice.	Tacrolimus	0-5	huntingtin	Mus musculus	150-153
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	phosphatidylinositol 3,5-diphosphate	243-262	huntingtin	Mus musculus	29-39
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	phosphatidylinositol 3,5-diphosphate	243-262	huntingtin	Mus musculus	88-98
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	pi 3,4,5-triphosphate	268-289	huntingtin	Mus musculus	29-39
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	pi 3,4,5-triphosphate	268-289	huntingtin	Mus musculus	88-98
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	CHEMBL1685065	291-302	huntingtin	Mus musculus	29-39
19566678-4	2009	Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin from Huntington"s disease (Hdh(140Q/140Q)) mouse brain bound to large unilamellar vesicles containing phosphoinositol (PI) PI 3,4-bisphosphate, PI 3,5-bisphosphate, and PI 3,4,5-triphosphate [PI(3,4,5)P3].	CHEMBL1685065	291-302	huntingtin	Mus musculus	88-98
19566678-5	2009	Huntingtin interactions with multivalent phospholipids were similar to those of dynamin.	Phospholipids	41-54	huntingtin	Mus musculus	0-10
19566678-6	2009	Mutant huntingtin associated more with phosphatidylethanolamine and PI(3,4,5)P3 than did wild-type huntingtin, and associated with other phospholipids not recognized by wild-type huntingtin.	phosphatidylethanolamine	39-63	huntingtin	Mus musculus	7-17
19566678-6	2009	Mutant huntingtin associated more with phosphatidylethanolamine and PI(3,4,5)P3 than did wild-type huntingtin, and associated with other phospholipids not recognized by wild-type huntingtin.	CHEMBL1685065	68-79	huntingtin	Mus musculus	7-17
19566678-6	2009	Mutant huntingtin associated more with phosphatidylethanolamine and PI(3,4,5)P3 than did wild-type huntingtin, and associated with other phospholipids not recognized by wild-type huntingtin.	Phospholipids	137-150	huntingtin	Mus musculus	7-17
19566678-9	2009	Endogenous huntingtin recruited to the plasma membrane in cells that incorporated exogenous PI 3,4-bisphosphate and PI(3,4,5)P3 or were stimulated by platelet-derived growth factor or insulin growth factor 1, which both activate PI 3-kinase.	pi 3,4-bisphosphate	92-111	huntingtin	Mus musculus	11-21
19566678-9	2009	Endogenous huntingtin recruited to the plasma membrane in cells that incorporated exogenous PI 3,4-bisphosphate and PI(3,4,5)P3 or were stimulated by platelet-derived growth factor or insulin growth factor 1, which both activate PI 3-kinase.	CHEMBL1685065	116-127	huntingtin	Mus musculus	11-21
19864571-1	2009	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease resulting from the expansion of a glutamine repeat in the huntingtin (Htt) protein.	Glutamine	111-120	huntingtin	Mus musculus	147-150
19864571-4	2009	We previously showed that V(L)12.3, an intrabody recognizing the N terminus of Htt, and Happ1, an intrabody recognizing the proline-rich domain of Htt, both reduce mHtt-induced toxicity and aggregation in cell culture and brain slice models of HD.	Proline	124-131	huntingtin	Mus musculus	147-150
19864571-4	2009	We previously showed that V(L)12.3, an intrabody recognizing the N terminus of Htt, and Happ1, an intrabody recognizing the proline-rich domain of Htt, both reduce mHtt-induced toxicity and aggregation in cell culture and brain slice models of HD.	mhtt	164-168	huntingtin	Mus musculus	147-150
19443488-1	2009	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	Mus musculus	124-134
19602103-3	2009	In transgenic mice, the severity of the diabetic phenotype appears to correlate with the length of a polyglutamine expansion in the protein huntingtin.	polyglutamine	101-114	huntingtin	Mus musculus	140-150
19443488-1	2009	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	Mus musculus	136-139
19602042-1	2009	Huntington"s disease (HD) is an inherited neurodegenerative disease caused by the expansion of a polyglutamine tract in the protein huntingtin (htt).	polyglutamine	97-110	huntingtin	Mus musculus	132-142
19602042-1	2009	Huntington"s disease (HD) is an inherited neurodegenerative disease caused by the expansion of a polyglutamine tract in the protein huntingtin (htt).	polyglutamine	97-110	huntingtin	Mus musculus	144-147
19464273-1	2009	Huntington"s disease (HD) is a neurodegenerative disorder caused by an expansion of polyglutamines which makes huntingtin more resistant to degradation.	polyglutamine	84-98	huntingtin	Mus musculus	111-121
19498170-3	2009	We report that the small guanine nucleotide-binding protein Rhes, which is localized very selectively to the striatum, binds physiologically to mHtt.	Guanine Nucleotides	25-43	huntingtin	Mus musculus	144-148
19605647-2	2009	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) tract in the protein huntingtin (htt), which leads to its aggregation and accumulation in inclusion bodies.	polyglutamine	92-105	huntingtin	Mus musculus	135-145
19605647-2	2009	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) tract in the protein huntingtin (htt), which leads to its aggregation and accumulation in inclusion bodies.	polyglutamine	92-105	huntingtin	Mus musculus	147-150
19605647-2	2009	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) tract in the protein huntingtin (htt), which leads to its aggregation and accumulation in inclusion bodies.	polyglutamine	107-112	huntingtin	Mus musculus	135-145
19605647-2	2009	Huntington"s disease (HD) is a fatal neurodegenerative disorder caused by an expansion of a polyglutamine (polyQ) tract in the protein huntingtin (htt), which leads to its aggregation and accumulation in inclusion bodies.	polyglutamine	107-112	huntingtin	Mus musculus	147-150
19362590-1	2009	Huntington"s disease (HD) is an autosomal dominant, progressive, and fatal neurodegenerative disorder caused by an expanded polyglutamine cytosine-adenine-guanine repeat in the gene coding for the protein huntingtin.	polyglutamine cytosine-adenine-guanine	124-162	huntingtin	Mus musculus	205-215
19145225-0	2009	Imaging elevated brain arachidonic acid signaling in unanesthetized serotonin transporter (5-HTT)-deficient mice.	Arachidonic Acid	23-39	huntingtin	Mus musculus	93-96
19145225-1	2009	Certain polymorphisms reduce serotonin (5-HT) reuptake transporter (5-HTT) function and increase susceptibility to psychiatric disorders.	Serotonin	29-38	huntingtin	Mus musculus	70-73
19145225-3	2009	As postsynaptic 5-HT(2A/2C) receptors are coupled to cytosolic phospholipase A(2) (cPLA(2)), which releases arachidonic acid (AA) from membrane phospholipid, 5-HTT-deficient mice may have altered brain AA signaling and metabolism.	Arachidonic Acid	108-124	huntingtin	Mus musculus	160-163
19145225-10	2009	Pretreatment with para-chlorophenylalanine, a 5-HT synthesis inhibitor, restored head twitches in 5-HTT(-/-) mice to levels in 5-HTT(+/+) mice.	Fenclonine	18-42	huntingtin	Mus musculus	100-103
19145225-10	2009	Pretreatment with para-chlorophenylalanine, a 5-HT synthesis inhibitor, restored head twitches in 5-HTT(-/-) mice to levels in 5-HTT(+/+) mice.	Fenclonine	18-42	huntingtin	Mus musculus	129-132
19240033-3	2009	Ectopic expression of SCAMP5 augments the formation of ubiquitin-positive and detergent-resistant aggregates of mutant huntingtin (mtHTT).	mthtt	131-136	huntingtin	Mus musculus	119-129
19345187-3	2009	We report here that such clearance can be achieved by posttranslational modification of the mutant Huntingtin (Htt) by acetylation at lysine residue 444 (K444).	Lysine	134-140	huntingtin	Mus musculus	99-109
19345187-3	2009	We report here that such clearance can be achieved by posttranslational modification of the mutant Huntingtin (Htt) by acetylation at lysine residue 444 (K444).	Lysine	134-140	huntingtin	Mus musculus	111-114
19345187-3	2009	We report here that such clearance can be achieved by posttranslational modification of the mutant Huntingtin (Htt) by acetylation at lysine residue 444 (K444).	k444	154-158	huntingtin	Mus musculus	99-109
19345187-3	2009	We report here that such clearance can be achieved by posttranslational modification of the mutant Huntingtin (Htt) by acetylation at lysine residue 444 (K444).	k444	154-158	huntingtin	Mus musculus	111-114
19429000-1	2009	Huntington disease is an uncommon autosomal dominant neurodegenerative disorder caused by expanded polyglutamine repeats in the huntingtin protein.	polyglutamine	99-112	huntingtin	Mus musculus	128-138
19228972-2	2009	Polyglutamine expansion of huntingtin (htt) results in early, progressive loss of medium spiny striatal neurons, as well as cortical neurons that project to the striatum.	polyglutamine	0-13	huntingtin	Mus musculus	27-37
19228972-2	2009	Polyglutamine expansion of huntingtin (htt) results in early, progressive loss of medium spiny striatal neurons, as well as cortical neurons that project to the striatum.	polyglutamine	0-13	huntingtin	Mus musculus	39-42
18831068-3	2009	An expanded polyglutamine tract within the protein huntingtin (Htt) enables a gain-of-function phenotype that is often exhibited by a dysfunctional oligomerization process and the formation of protein aggregates.	polyglutamine	12-25	huntingtin	Mus musculus	51-61
18831068-3	2009	An expanded polyglutamine tract within the protein huntingtin (Htt) enables a gain-of-function phenotype that is often exhibited by a dysfunctional oligomerization process and the formation of protein aggregates.	polyglutamine	12-25	huntingtin	Mus musculus	63-66
19193873-1	2009	Huntington"s disease (HD) is a dominantly inherited, progressive neurodegenerative disease caused by an expanded polyglutamine tract in huntingtin protein (Htt).	polyglutamine	113-126	huntingtin	Mus musculus	136-146
19193873-1	2009	Huntington"s disease (HD) is a dominantly inherited, progressive neurodegenerative disease caused by an expanded polyglutamine tract in huntingtin protein (Htt).	polyglutamine	113-126	huntingtin	Mus musculus	156-159
18984744-2	2009	Huntington"s disease is a neurodegenerative disorder caused by a polyglutamine expansion within the huntingtin protein.	polyglutamine	65-78	huntingtin	Mus musculus	100-110
19187096-1	2009	Huntington"s disease is a hereditary neurodegenerative disorder caused by an aberrant polyglutamine expansion in the amino terminus of the huntingtin protein.	polyglutamine	86-99	huntingtin	Mus musculus	139-149
18838463-2	2009	Expansion of a polyglutamine stretch at the N-terminus of htt causes Huntington"s disease (HD), a dominant neurodegenerative disorder.	polyglutamine	15-28	huntingtin	Mus musculus	58-61
18805465-2	2008	Mice with an insertion of an expanded polyglutamine repeat in the mouse huntingtin gene (knock-in mice) most closely model the disease because the mutation is expressed in the proper genomic and protein context.	polyglutamine	38-51	huntingtin	Mus musculus	72-82
19074039-1	2008	Huntington"s disease (HD) is an autosomal dominant neurodegenerative disease linked to a polyQ (polyglutamine) expansion in the huntingtin protein.	polyq (polyglutamine)	89-110	huntingtin	Mus musculus	128-138
18854207-1	2008	Huntington"s disease (HD) is a neurodegenerative disorder caused by a polyglutamine repeat expansion in huntingtin.	polyglutamine	70-83	huntingtin	Mus musculus	104-114