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1 ulofilaments (previously shown, by us, to be paired helical filaments).
2 believed to play a role in the formation of paired helical filaments.
3 sitive inclusions, and structures resembling paired helical filaments.
4 cally by vacuolated muscle fibres containing paired helical filaments.
5 the dentate gyrus and midbrain demonstrated paired helical filaments.
6 poradic myositis was localized mainly to the paired helical filaments.
7 cally by vacuolated muscle fibers containing paired helical filaments.
8 l repeat region formed structures resembling paired helical filaments.
9 ired helical filaments, but never was on the paired helical filaments.
10 but may also play a role in the formation of paired helical filaments.
11 -sheet secondary folding of tau protein into paired helical filaments.
12 e-associated protein Tau forms intracellular paired helical filaments.
13 antibodies, and electron microscopy revealed paired helical filaments.
14 cytochemistry using antibodies against human paired helical filaments.
15 immuno-electron microscopy were confined to paired helical filaments.
16 are major components of Alzheimer's disease paired helical filaments.
17 amorphous tufts adjacent to the muscle fiber paired-helical filaments.
19 was a significant decrease in the density of paired helical filament-1-positive neurons in the immuni
20 idue amino-acid sequence, referred to as the paired helical filament 6 (PHF6), which may play an impo
21 phorylated tau is the principal component of paired helical filaments, a pathological hallmark of Alz
22 , amyloid-beta immunoreactive filaments, and paired helical filaments, all of which are pathological
23 t et al reports that antibodies generated to paired helical filaments (AMY antibodies) unexpectedly l
24 tion and vacuolated muscle fibers containing paired helical filaments and 6- to 10-nm fibrils, both r
26 at in Alzheimer's disease, the copresence of paired helical filaments and Abeta-amyloidosis indicates
27 he formation and/or stabilization of NFT and paired helical filaments and provide a model system to i
28 ation of isolated tau filaments demonstrated paired helical filaments and ribbon-like structures.
30 ylated tau (P-tau) in the form of tangles of paired helical filaments and/or straight filaments is on
32 nd beta-amyloid precursor protein, and their paired helical filaments are composed of phosphorylated
34 bodies which recognize phosphorylated tau in paired helical filaments (AT8 and PHF-1) show positive i
35 angstrom structure of AD patient-derived tau paired-helical filaments bound to the PET ligand GTP-1.
36 curred on material in close proximity to the paired helical filaments, but never was on the paired he
37 idely regarded as the principal component of paired helical filaments comprising Alzheimer neurofibri
38 ed to, but distinct from, the PTMs of mature paired helical filaments, consistent with the idea that
39 ly hyperphosphorylated tau polymers known as paired helical filaments constitute one of the major cha
40 endent epitope of tau in Alzheimer's disease paired helical filaments, demonstrates positivity in the
42 main component of "plaques") and tau protein paired helical filaments/fibrils (the main component of
43 ide (Abeta) concentration, Abeta deposition, paired helical filament formation, cerebrovascular amylo
45 recognition of the role of proteoglycans in paired helical filaments formation makes proteoglycans o
46 ments by a method used for the extraction of paired helical filaments from Alzheimer's disease brain.
48 n IBM muscle and AD brain phenotypes include paired helical filaments, hyperphosphorylated tau protei
49 vidence for hyperphosphorylated tau protein (paired helical filament-I tau), which has been associate
51 ongly binds to tau lesions primarily made of paired helical filaments in Alzheimer brains (eg, intran
52 mentia through its deposition in the form of paired helical filaments in Alzheimer's disease neurofib
53 We document the first case of tauopathy with paired helical filaments in an aged chimpanzee (Pan trog
54 phosphorylated tau is the major component of paired helical filaments in neurofibrillary lesions asso
55 tau (microtubule-binding protein that forms paired helical filaments in neurons of the Alzheimer's d
56 s disease (AD) and accumulates as tangles of paired helical filaments in neurons undergoing degenerat
58 eadily bound thioflavin-S, a dye that stains paired helical filaments in the histochemical diagnosis
59 ociated protein tau is found aggregated into paired helical filaments in the intraneuronal neurofibri
60 cytochemistry, including colocalization with paired helical filaments in the neuropil and perikarya.
61 ubule-associated protein tau aggregates into paired helical filaments in which each protofilament has
62 s dysfunction and aggregation into insoluble paired helical filaments is involved in the pathogenesis
64 lated tau adopt a fold comparable to that of paired helical filaments isolated from the brains of AD
65 aneously in physiological conditions to form paired helical filament-like fibres in vitro in the abse
68 nstrate that all Tau isoform fibrils exhibit paired-helical-filament-like structures consisting of tw
69 pal (hilar subregion) amyloid plaque and tau paired-helical filament load, and microgliosis compared
71 , including hippocampal amyloid plaques, tau paired-helical filaments, neuronal loss and microgliosis
72 otein tau that is the major component of the paired helical filaments observed in Alzheimer's disease
73 Tau PET has enabled the visualization of paired helical filaments of 3 or 4 C-terminal repeat tau
74 s of Alzheimer disease (AD), are composed of paired helical filaments of abnormally hyperphosphorylat
77 cated tau (amino acid residues 297-391) into paired helical filaments of Alzheimer's disease or into
80 of neuritic plaques (NPs) and from the 24 nm paired helical filaments of neurofibrillary tangles (NFT
81 rus neurons showed cytoplasmic inclusions of paired helical filaments, P-tau aggregates characteristi
85 isease (AD), immunohistochemistry of WT1 and paired helical filament (PHF) in serial sections was car
87 formation of amyloid fibrils displaying the paired helical filament (PHF) morphology characteristic
88 Ser 262 is phosphorylated extensively in paired helical filament (PHF) tau from Alzheimer's disea
89 elated positively with binding levels of the paired helical filament (PHF) tracer [(18)F]Flortaucipir
90 m the progressive pattern of neuropathology [paired helical filament (PHF)-tau and amyloid-beta] in A
91 r AV-1451 exhibits high binding affinity for paired helical filament (PHF)-tau pathology in Alzheimer
97 gical aggregation and deposition of tau into paired helical filaments (PHF) in neurofibrillary tangle
98 hosphorylated and accumulates in the form of paired helical filaments (PHF) in the brains of patients
100 of several solvents to solubilize insoluble paired helical filaments (PHF) of Alzheimer disease.
101 orylation is implicated in the biogenesis of paired helical filaments (PHF) seen in Alzheimer's disea
104 adopt the same molecular structure as the AD paired-helical filament (PHF) tau but are unable to temp
105 te-specific PTMs located within the PHF6(*) (paired helical filament [PHF] residues 275-280) and PHF6
109 drated tau 2-19 and collagen I and insoluble paired helical filaments (PHFs) and collagen I of weak h
110 an important contributor to the formation of paired helical filaments (PHFs) and neurofibrillary tang
111 ng of tau protein leads to the generation of paired helical filaments (PHFs) and neurofibrillary tang
112 generation of muscle fibers characterized by paired helical filaments (PHFs) composed of phosphorylat
113 s the neurofibrillary tangle, which contains paired helical filaments (PHFs) composed of the microtub
115 o determine if the high phosphate content of paired helical filaments (PHFs) in Alzheimer's disease (
117 ion of human Alzheimer high-molecular-weight paired helical filaments (PHFs) in the dentate gyrus of
119 rils are structurally closely related to the paired helical filaments (PHFs) isolated from Alzheimer'
120 lzheimer disease (AD) is the accumulation of paired helical filaments (PHFs) of hyperphosphorylated m
123 table aggregates leading to the formation of paired helical filaments (PHFs) which deposit into neuro
124 specific serine/threonine residues found in paired helical filaments (PHFs), and its expression is u
126 that phosphorylated tau, like that found in paired helical filaments (PHFs), does not promote microt
134 osphorylated form, aggregates into insoluble paired-helical filaments (PHFs) in Alzheimer's disease (
137 ur phosphospecific probes also revealed that paired helical filament preparations exhibited phospho-t
138 tau is the major structural component of the paired helical filaments present in the brains of Alzhei
139 ognizing independent phospho-epitopes in the paired helical filament proteins (PHF) found in AD brain
140 The introduction of PET ligands that bind to paired helical filaments provides the ability to measure
141 mbling straight filaments or Pronase-treated paired helical filaments raises fundamental questions co
143 specific Serine/Threonine residues found in paired helical filaments, suggesting its role in tauopat
144 onoclonal antibody Alz50 much like authentic paired helical filaments, suggesting that the conformati
145 Neuropathologic measures of amyloid-beta, paired helical filament tangles, neocortical Lewy bodies
146 with or without LOC was not associated with paired helical filament tangles, transactive response DN
147 ylated at the same amino acid residues as AD paired helical filament tau (PHFtau), but they exhibited
148 vasive analyses in cortical regions in which paired helical filament tau accumulation is expected in
149 vasive analyses in cortical regions in which paired helical filament tau accumulation is expected in
150 d in clinical studies) provides estimates of paired helical filament tau burden in good correlation w
151 d in clinical studies) provides estimates of paired helical filament tau burden in good correlation w
152 t analysis, Tau-nY29 detects soluble tau and paired helical filament tau from severely affected Alzhe
156 ripts of SORL1 and ABCA7 was associated with paired helical filament tau tangle density, and the expr
159 inding to primary tauopathy in cases without paired helical filament tau was found to be within the r
160 e phosphorylation site consistently found in paired helical filament tau, serine 413, is modified by
161 global pathology score, and as amyloid load, paired helical filament tau-positive (PHFtau) tangle den
163 nds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosph
164 were highly correlated with neuritic plaque, paired helical filaments tau neurofibrillary tangle and
166 h wt mice, prominent inner retinal Abeta and paired helical filament-tau, and decreased retinal gangl
167 ain tau pathology in the form of tangles and paired helical filament-tau-containing neurites in Alzhe
168 SP), tau proteins assemble into straight and paired helical filaments that form intraneuronal deposit
169 nds microtubules, and self-assembles to form paired helical filaments that likely contribute to neuro
171 n have the deposition of Alzheimer's disease paired helical filament type hyperphosphorylated tau.
172 ormation of either sarkosyl-insoluble tau or paired helical filaments was not induced by Abeta42.
174 demonstrates two novel components of the IBM paired helical filaments, which may lead to better under
175 lary tangles consisted of tau-immunoreactive paired helical filaments with a diameter and helical per
176 otracers depicted tau inclusions composed of paired helical filaments with high specificity, both in