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1 same JUNQ-like inclusion whereas the other, polyglutamine (72Q), formed spatially distinct IPOD-like
2 lins by genetic ablation or sequestration in polyglutamine aggregates leads to accumulation of non-in
3 ve disorders and intracerebral deposition of polyglutamine aggregates motivates attempts to better un
5 lerance and reduced levels of stress-induced polyglutamine aggregates, likely due to upregulated IPR
6 heart of huntingtin exon1 fibrils and other polyglutamine aggregates, via measurements of long-range
8 ward genetic screen in a C. elegans model of polyglutamine aggregation and identified the protein MOA
9 periments and in cell models and accelerated polyglutamine aggregation and toxicity in an oxidation-s
10 ify the driving forces for and mechanisms of polyglutamine aggregation as modulated by N17 and C38.
11 s on the one hand known to markedly increase polyglutamine aggregation rates and on the other hand ha
12 a possible pathway for the initial stages of polyglutamine aggregation, in which beta-hairpin-contain
14 mutant mice, placing a dominant HD knock-in polyglutamine allele onto the slow-aging Snell dwarf gen
17 polyglutamine toxicity and prevents purified polyglutamine and Abeta peptides from forming amyloid.
18 Htt17 monomer, as well as the impact of the polyglutamine and proline-rich segments, remains, howeve
19 ormational TR-FRET based immunoassay detects polyglutamine- and temperature-dependent changes on the
21 behavior, huntingtin exon1 fibrils and other polyglutamine-based aggregates contain identical beta-st
26 tability of dimers to assess whether a given polyglutamine conformer can be on the aggregation path.
27 We also find that these temperature- and polyglutamine-dependent conformational changes are sensi
29 on between aberrant accumulation of expanded polyglutamine-dependent insoluble protein species and pa
30 arly, largely independent, manifestations of polyglutamine disease and suggests that additional epige
31 Here, we show that, in a mouse model for the polyglutamine disease dentatorubral-pallidoluysian atrop
32 Consistently, the recovery of lifespan in polyglutamine disease fly models by TERA/VCP/p97 corresp
33 tment exists for the fatal neurodegenerative polyglutamine disease known both as Machado-Joseph disea
35 nally blocked versions of one substrate, the polyglutamine disease protein ataxin-3, and showed that
36 protein (VCP)/p97 directly binds to multiple polyglutamine disease proteins (huntingtin, ataxin-1, at
37 contrast to this view, we show that, in the polyglutamine disease spinal and bulbar muscular atrophy
39 ociation with age at onset when grouping all polyglutamine diseases (HD+SCAs; p = 1.43 x 10(-5) ).
40 etic mechanism modulates age at onset across polyglutamine diseases and could extend to other repeat
44 A key unanswered question in SCA3 and other polyglutamine diseases is the extent to which neurodegen
45 de a novel common pathomechanism in multiple polyglutamine diseases that is mediated by DNA repair fu
46 ng all conditions studied (DM1, DM2, C9-ALS, polyglutamine diseases), reduction of polyglutamine prot
49 l sclerosis/frontotemporal dementia and with polyglutamine diseases, respectively, localize to neurit
50 orders, such as Alzheimer's, Parkinson's and polyglutamine diseases, share a common pathogenic mechan
51 ults, together with recent findings in other polyglutamine diseases, suggest that CAG repeat expansio
63 sion of neurodegenerative disease, including polyglutamine disorders such as Huntington's disease and
64 cellular compartment for the pathogenesis of polyglutamine disorders, including Huntington's disease
67 a an intramolecular collapse of the expanded polyglutamine domain and discuss the implications of thi
69 sease caused by an abnormal expansion in the polyglutamine encoding CAG repeat of the androgen recept
70 is a neurodegenerative disorder caused by a polyglutamine-encoding CAG repeat expansion in the ATXN3
74 e show that treatment of myotubes expressing polyglutamine-expanded AR with the beta-agonist clenbute
75 found that NLK can phosphorylate the mutant polyglutamine-expanded AR, enhance its aggregation, and
78 role in the pathogenic pathways mediated by polyglutamine-expanded ataxin-3 and that phosphorylation
79 with ATXN1, modulates disease phenotypes of polyglutamine-expanded ATXN1 in a Drosophila model of SC
83 t tracking of individual cells enriched with polyglutamine-expanded Htt exon 1 (Httex1) monomers, oli
86 neurons exposed to an N-terminal fragment of polyglutamine-expanded huntingtin (Htt171-82Q), blocking
87 sp70 system in spatial organization of toxic polyglutamine-expanded Huntingtin (Huntingtin with 103Q
88 disorder Huntington's disease (HD), in which polyglutamine-expanded huntingtin (polyQ-htt) is predomi
89 as the capacity to suppress aggregation of a polyglutamine-expanded Huntingtin construct that aggrega
90 s the viability of neuronal cells expressing polyglutamine-expanded huntingtin exon 1 protein fragmen
91 euronal aggregates and inclusions containing polyglutamine-expanded huntingtin protein and peptide fr
94 rmal Htt and gain of a toxic function by the polyglutamine-expanded mutant Htt protein have been prop
95 tics aimed at correcting the conformation of polyglutamine-expanded proteins as well as the pharmacod
98 misfolded huntingtin exon I containing a 103-polyglutamine expansion (Htt103QP) as a model substrate
102 Spinocerebellar ataxia type 1 is one of nine polyglutamine expansion diseases and is characterized by
103 n in HD, and may have implications for other polyglutamine expansion diseases in which mutant protein
105 disease (HD) is the most commonly inherited polyglutamine expansion disorder, but how mutant Hunting
106 sight, down to the molecular level, into how polyglutamine expansion drives aggregation and explains
110 neurodegenerative disease caused by abnormal polyglutamine expansion in huntingtin (Exp-HTT) leading
115 s, we and others have recently reported that polyglutamine expansion in purified or recombinantly exp
116 eurodegenerative disorder caused by abnormal polyglutamine expansion in the amino-terminal end of the
118 progressive neuromuscular disease caused by polyglutamine expansion in the androgen receptor (AR) pr
121 fatal neurodegenerative disease caused by a polyglutamine expansion in the coding region of ATXN1.
122 neurodegenerative disease caused by abnormal polyglutamine expansion in the huntingtin protein (Htt).
125 erited neurodegenerative disease caused by a polyglutamine expansion in the huntington protein (htt).
126 erited neurodegenerative condition caused by polyglutamine expansion in the N terminus of the hunting
127 th Huntington disease (HD) is triggered by a polyglutamine expansion in the N-terminal region of the
128 se is neurodegenerative disorder caused by a polyglutamine expansion in the N-terminal region of the
129 ataxia type 1 (SCA1), a disease caused by a polyglutamine expansion in the protein ATAXIN1 (ATXN1).
132 neurodegenerative disorder that results from polyglutamine expansion of the ataxin-7 (ATXN7) protein.
133 Tat-beclin 1 decreases the accumulation of polyglutamine expansion protein aggregates and the repli
135 Huntington's disease (HD) is caused by a polyglutamine expansion within the huntingtin (Htt) prot
136 's disease (HD) is caused in large part by a polyglutamine expansion within the huntingtin (Htt) prot
138 n expression of the highly aggregation-prone polyglutamine-expansion proteins and Abeta-peptide.
139 se (HD) is a neurological disorder caused by polyglutamine expansions in mutated Huntingtin (mHtt) pr
140 ominant neurodegenerative disorder caused by polyglutamine expansions in the amino-terminal region of
141 cts males, results from a CAG triplet repeat/polyglutamine expansions in the androgen receptor (AR) g
142 in yeast and flies, and intermediate-length polyglutamine expansions in the ataxin-2 gene increase r
143 an indirect and poorly understood manner by polyglutamine expansions in the huntingtin (HTT) protein
145 dence for beta-arch-containing structures in polyglutamine fibrils and open future possibilities for
148 neurodegenerative disease-related proteins (polyglutamine, huntingtin, ataxin-1, and superoxide dism
149 Abeta aggregation mechanism that uses Abeta-polyglutamine hybrid peptides designed to retard amyloid
151 mice, accumulation of RanGAP1 together with polyglutamine is shifted to perinuclear and cytoplasmic
152 that although the alpha-helical conformer of polyglutamine is very stable, dimers of alpha-helices la
153 t onset of disease decreases with increasing polyglutamine length in these proteins and the normal le
155 1 aggregation in cells with respect to time, polyglutamine length, expression levels, cell survival,
156 d that HDAC4 associates with huntingtin in a polyglutamine-length-dependent manner and co-localises w
159 ay impair FOXO protective activity in mutant polyglutamine neurons, suggesting that neurons are unabl
162 l fragment delays aggregation onset by Abeta-polyglutamine peptides and redirects assembly of Abeta42
163 nhibit the formation of amyloid fibrils from polyglutamine peptides associated with neurodegenerative
164 ogy calls for understanding the structure of polyglutamine peptides in the early stages of aggregatio
165 to simultaneously probe fibril formation in polyglutamine peptides, the aggregating subunit associat
166 ington disease (HD) is caused by an expanded polyglutamine (poly(Q)) repeat near the N terminus of th
168 egenerative disease caused by expansion of a polyglutamine [poly(Q)] tract in ATXN7, a subunit of the
170 AT yeast homologs, NMA1 and NMA2, suppresses polyglutamine (PolyQ) and alpha-synuclein-induced cytoto
173 further show that PML deficiency exacerbates polyglutamine (polyQ) disease in a mouse model of spinoc
174 odegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the
175 ington's disease is caused by expansion of a polyglutamine (polyQ) domain within exon 1 of the huntin
176 ith an increased aggregation propensity of a polyglutamine (polyQ) expansion in exon 1 of mutant hunt
178 rebellar ataxia type 7 (SCA7) is caused by a polyglutamine (polyQ) expansion in the ataxin-7 protein,
179 -onset neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the N-terminal region
181 n an encoded region of the gene resulting in polyglutamine (polyQ) expansion which has been assumed t
182 A7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal re
183 nerative disorder caused by the expansion of Polyglutamine (polyQ) in exon 1 of the Huntingtin protei
185 the toxic molecular species in the expanded polyglutamine (polyQ) repeat diseases range from various
186 neurodegenerative disorder caused by a CAG - polyglutamine (polyQ) repeat expansion in the ataxin-7 g
189 ington's disease is caused by expansion of a polyglutamine (polyQ) repeat in the huntingtin protein.
190 odegenerative disorder caused by an expanded polyglutamine (polyQ) repeat in the TATA-box-binding pro
191 odegenerative disorder caused by an expanded polyglutamine (polyQ) repeat within the protein huntingt
193 esulting mutant protein (mHtt) with extended polyglutamine (polyQ) sequence at the N terminus leads t
194 rongly dependent on the repeat length of the polyglutamine (polyQ) sequence in the disease protein.
197 of huntingtin protein arising from expanded polyglutamine (polyQ) sequences in the exon-1 region of
198 generative disorder caused by expansion of a polyglutamine (polyQ) stretch within the Huntingtin (Htt
199 sease caused by an abnormal expansion in the polyglutamine (polyQ) track of the Huntingtin (HTT) prot
200 are enhanced in the presence of the expanded polyglutamine (polyQ) tract and are stronger in the nucl
201 Fragments of proteins containing an expanded polyglutamine (polyQ) tract are thought to initiate aggr
202 gene, which is translated into an elongated polyglutamine (polyQ) tract in AR protein (ARpolyQ).
203 h is caused by a pathological expansion of a polyglutamine (polyQ) tract in the coding region of the
204 gton's disease (HD) is caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) prot
205 ng catalytic activity or bearing an expanded polyglutamine (polyQ) tract led to partially overlapping
206 is unusual in that it includes a C-terminal polyglutamine (polyQ) tract that is absent in nonrodent
209 of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark
210 genes, TR copy number mutations that expand polyglutamine (polyQ) tracts beyond a certain threshold
212 degenerative diseases are caused by expanded polyglutamine (polyQ) tracts in different proteins, such
214 The aggregation of proteins with expanded polyglutamine (polyQ) tracts is directly relevant to the
215 caused by cell death after the expansion of polyglutamine (polyQ) tracts longer than approximately 4
218 a type 6 (SCA6) belongs to the family of CAG/polyglutamine (polyQ)-dependent neurodegenerative disord
219 xpansion of CAG repeats encoding consecutive polyglutamines (polyQ) in the corresponding disease prot
220 ists strong correlation between the extended polyglutamines (polyQ) within exon-1 of Huntingtin prote
222 ll-length protein, challenging the notion of polyglutamine protein fragment-associated toxicity by re
223 elated decline in chaperone activity affects polyglutamine protein function that is important for the
224 9-ALS, polyglutamine diseases), reduction of polyglutamine protein products, relocalization of repeat
225 y and involved in the clearance of misfolded polyglutamine protein, is strongly recruited to the muta
226 oratory and wild strains and disease-related polyglutamine proteins expressed in both yeast and mamma
234 diseases, namely at early stages of another polyglutamine-related disorder such as Huntington's dise
236 at residue T3) of a protein associated with polyglutamine repeat expansion, namely Huntingtin, and c
237 neurodegenerative disorder, caused by a CAG/polyglutamine repeat expansion, which is associated with
238 ative disorder caused by an expansion of the polyglutamine repeat in the first exon in the androgen r
239 odegenerative disorder caused by an extended polyglutamine repeat in the N terminus of the Huntingtin
241 nal properties in a manner dependent on both polyglutamine repeat length and temperature but independ
242 ng the aggregation free energy profile for a polyglutamine repeat with site-specific PG mutations tha
244 cular atrophy mice that carry 100 pathogenic polyglutamine repeats in the androgen receptor, and deve
245 degenerative disease, caused by expansion of polyglutamine repeats in the Huntingtin gene, with longe
246 is a rare genetic disease caused by expanded polyglutamine repeats in the huntingtin protein resultin
247 disorder caused by an abnormal expansion of polyglutamine repeats in the N-terminal of huntingtin.
249 ncoding huntingtin (Htt) leading to expanded polyglutamine repeats of mutant Htt (mHtt) that elicit o
250 pendent cohort of 1,462 subjects with HD and polyglutamine SCAs, and genotyped single-nucleotide poly
256 cleotide CAG repeat expansion that encodes a polyglutamine stretch in the huntingtin (HTT) protein.
257 of an RNA-binding protein, and deletion of a polyglutamine stretch in this protein results in random
258 on's disease (HD) results from expansions of polyglutamine stretches (polyQ) in the huntingtin protei
259 re we find DnaJB6-protected yeast cells from polyglutamine toxicity and cured yeast of both [URE3] pr
260 efects cause myopathies, protects cells from polyglutamine toxicity and prevents purified polyglutami
261 is due to an androgen receptor containing a polyglutamine tract (ARpolyQ) that misfolds and aggregat
263 ceptor sites; human MPI is translated into a polyglutamine tract associated with spinocerebellar atax
264 Our data support the hypothesis that the polyglutamine tract can act as a flexible domain, allowi
268 gregation diseases is an abnormally expanded polyglutamine tract found in the respective proteins.
271 the Huntington's disease gene HTT extends a polyglutamine tract in mutant huntingtin that enhances i
272 isorder associated with the expansion of the polyglutamine tract in the exon-1 domain of the huntingt
276 caused by a CAG repeat expansion encoding a polyglutamine tract in the huntingtin (Htt) protein.
277 exon 1 of the HTT gene that translates to a polyglutamine tract in the huntingtin protein (HTT).
278 vely worsened with age and was influenced by polyglutamine tract length in mutant huntingtin (mhtt).
279 nd explains the positive correlation between polyglutamine tract length, protein aggregation, and dis
280 aggregation is the anomalous expansion of a polyglutamine tract near the protein N-terminus, but the
282 ant huntingtin exon 1 containing an expanded polyglutamine tract with 51 residues (mhttQ51), and reso
284 ar ataxia associated with the expansion of a polyglutamine tract within the ataxin-1 (ATXN1) protein.
286 of huntingtin (HTT) protein with an expanded polyglutamine tract, could also benefit from this approa
287 s directly located upstream of the protein's polyglutamine tract, plays a decisive role in several im
288 ures caused by ATXN1[82Q] having an expanded polyglutamine tract, they fail to manifest the age-relat
293 scoideum has evolved to normally encode long polyglutamine tracts and express these proteins in a sol
294 s been suggested that proteins with expanded polyglutamine tracts impair ubiquitin-dependent proteoly
296 refore, we hypothesize that wild-type length polyglutamine tracts within huntingtin can form a flexib
297 This flexibility is impaired with expanded polyglutamine tracts, and we can detect changes in hunti
299 This regulation is lost in the presence of polyglutamine, which mislocalizes MOAG-2/LIR-3 from the
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