ライフサイエンスコーパス: fibril

1 ollagen molecules inside 2D voids within the fibril.

2 ude from the entire length of the progenitor fibril.

3 entation of HAp crystals within the collagen fibril.

4 he atomic structure of the core of alpha-syn fibrils.

5 deposits composed in part of alpha-synuclein fibrils.

6 stallize along the surface of and within the fibrils.

7 ein after stereotaxic injection of preformed fibrils.

8 ordered, insoluble, beta-sheet-rich amyloid fibrils.

9 harges and secondary conformation in amyloid fibrils.

10 heterologously seeded using patient ex-vivo fibrils.

11 nomers can be catalyzed by preexisting Abeta fibrils.

12 le hydrogel in vitro containing amyloid-like fibrils.

13 ell extensions and the alignment of collagen fibrils.

14 eir monomeric precursors without forming new fibrils.

15 innately responded to NA-containing amyloid fibrils.

16 g seeding by human patient-derived alpha-syn fibrils.

17 ), most commonly used for monitoring amyloid fibrils.

18 loose, disorganized, and fragmented collagen fibrils.

19 sembly and results in highly ordered amyloid fibrils.

20 egative effects amongst hemicellulose-coated fibrils.

21 or disaggregating mature apolipoprotein C-II fibrils.

22 trix structure surrounding glycated collagen fibrils.

23 the contact points between adjacent collagen fibrils.

24 ritical role in the formation of polymorphic fibrils.

25 lmost all Abeta monomers are integrated into fibrils.

26 oteins and proteins that form condensates or fibrils.

27 t beta-sheet conformation in patient protein fibrils.

28 ng between the paired beta-sheets within Tau fibrils.

29 inds oligomeric tau, but not tau monomers or fibrils.

30 be prone to self-assembly into amyloid-like fibrils.

31 elongation mechanism and kinetics of protein fibrils.

32 of ~40 nm diameter, occupying spaces between fibrils.

33 sity of huntingtin exon-1 to form cross-beta fibrils.

34 M structure of recombinant full-length hIAPP fibrils.

35 ecular packing of alpha-synuclein within the fibrils.

36 chemical shifts that are highly like patient fibrils.

37 ions have on the nucleation rates of amyloid fibrils.

38 ged, lower energy fold compared to wild-type fibrils.

39 ser extent, Abeta42 aggregation into amyloid fibrils.

40 yn fibrils leads to the disassembly of these fibrils.

41 oteins, nanoparticles, exosomes, and amyloid fibrils.

42 more negative surface charge than unglycated fibrils.

43 monomeric Abeta pool for incorporation into fibrils.

44 ptide aggregation from monomers into amyloid fibrils, a hallmark of Alzheimer's disease, is crucial f

45 ompany the accumulation of insoluble amyloid fibrils, a histological hallmark of Alzheimer disease (A

46 We observed that cross-seeding by sRPT fibrils accelerates the rate of lRPT aggregation, result

47 e modification of beta-lactoglobulin amyloid fibrils (AFs) was investigated by performing the Maillar

48 s requires long cell extensions that mediate fibril alignment.

49 by medin aggregates compared to amyloid-beta fibrils, along with the absence of amyloid fibers in the

50 ell function was investigated in a preformed fibril alpha-syn-induced mouse PD model.

51 ed fractures were associated with lower peak fibril and mineral strain irrespective of treatment.

52 ain and normalized strength, with lower peak fibril and mineral strain.

53 bril induced by EGCG and inhibition of Abeta fibril and oligomer formation, as manifested by the reco

54 oked fMRI on 20 mice injected with alpha-syn fibrils and 20 PBS-injected mice at three timepoints (10

55 preformed human alpha-synuclein (alpha-syn) fibrils and adeno-associated virus (AAV) expressing huma

56 mally soluble protein molecules into amyloid fibrils and alter the fibril morphologies, yet the molec

57 glycoprotein B (gB) peptides assembled into fibrils and catalyzed amylin and Abeta42 aggregation.

58 the circadian clock causes abnormal collagen fibrils and collagen accumulation, which are reduced in

59 ods of structural comparison between ex vivo fibrils and fibrils generated in vitro Our finding that

60 s induced by the binding between the amyloid fibrils and membrane components and its direct effects o

61 des (Abeta) assemble into both rigid amyloid fibrils and metastable oligomers termed AbetaO or protof

62 Here, we study the formation of fibrils and oligomers by exon 1 of huntingtin protein.

63 s showed specific activity towards alpha-syn fibrils and oligomers in comparison to monomers and reco

64 However, the relationship between BM fibrils and stress fibers and their respective impact on

65 Biomarkers such as beta-amyloid (Abeta) fibrils and Tau tangles in Alzheimer's disease are acces

66 can provide structural details about amyloid fibrils and their polymorphs.

67 sine-rich fragment of ALIX-PRD forms amyloid fibrils and viscous gels validated using dye-binding ass

68 udinal ordering of the molecules in collagen fibrils and, using KFM and FLiM, that R5P-glycated colla

69 nt, calcium-rich deposits appear between the fibrils and, with time, mineral propagates along and wit

70 in (alpha-syn) to form oligomers and amyloid fibrils, and how such species promote brain death.

71 ed with a nitro group bind to mature amyloid fibrils, and the activity moreover depends on the positi

72 imary neurons with alpha-synuclein preformed fibrils, and we observed marked reductions in alpha-synu

73 Collagen fibrils are central to the molecular organization of the

74 Amyloid fibrils are highly ordered nanoscopic protein aggregates

75 We find that beta-endorphin fibrils are in a beta-solenoid conformation that is gene

76 mobilization of invertase using amyloid-like fibrils as a support.

77 saggregation machinery processed recombinant fibrils assembled from all six Tau isoforms as well as S

78 l procollagen synthesis and daytime collagen fibril assembly in mice.

79 ntial structural basis for surface-templated fibril assembly.

80 ZP-C, with ZP-N of ZP2 and ZP3 required for fibril assembly.

81 markable resemblance to amyloid beta (Abeta) fibrils associated with Alzheimer's disease, highlightin

82 In the case of amyloid fibrils associated with Alzheimer's disease, this proces

83 lin (beta(2)m), which assembles into amyloid fibrils associated with dialysis-related amyloidosis.

84 llagen (C7), the main component of anchoring fibrils at the dermal-epidermal junction.

85 The fibril axial pattern is determined solely by the distrib

86 rs may be transported through spaces between fibrils before they crystallize along the surface of and

87 the terminal regions are required for stable fibril binding by both sHSPs and for mediating lateral f

88 mers antagonize their replacement by amyloid fibrils both by competing for monomers and blocking seco

89 It forms fibrils both under cellular stress and in mutated form i

90 yte) lacunae surround extracellular collagen fibril bundles.

91 Tractional remodeling of collagen fibrils by fibroblasts requires long cell extensions tha

92 This promotes the formation of fibronectin fibrils by indolent cells that drive integrin-dependent

93 s the autocatalytic proliferation of amyloid fibrils by secondary nucleation on the fibril surface.

94 S20G fibrils, by contrast, contain two major polymorphs.

95 Crystals, nanoparticles, and fibrils catalyze the generation of new aggregates on the

96 hat can misfold and polymerize to form toxic fibrils coalescing into pathologic inclusions in neurode

97 rted the presence of functional amyloid-like fibrils composed of Aap within S. epidermidis biofilms a

98 L-activated Skd3 solubilizes alpha-synuclein fibrils connected to Parkinson's disease.

99 In Alzheimer's disease, Abeta fibrils constitute the core of senile plaques, but Abeta

100 scopy (cryo-EM) structure of alpha-synuclein fibrils containing the hereditary E46K mutation.

101 oscopy (cryoEM) structure of the hnRNPA2 LCD fibril core and demonstrate its capability to form a rev

102 amics simulations indicate that the FUS-LC-C fibril core is stabilized by a plethora of hydrogen bond

103 In the FUS-LC-C fibril core, residues 112-150 adopt U-shaped conformatio

104 metalloprotease-1 (MMP1) on type 1 collagen fibrils correlate with its activity.

105 fibrils generated in vitro Our finding that fibrils created via an in vitro amyloidogenic pathway ar

106 Fibrils cross-linked artificially by glutaraldehyde do n

107 fiber orientation relies on the preceding BM fibril deposition, indicating two distinct but interdepe

108 (Dg) and Dystrophin (Dys) are involved in BM fibril deposition.

109 is is characterized by deposition of amyloid fibrils derived from a particular antibody light chain.

110 f synthetic, recombinant, and native amyloid fibrils derived from different amyloidogenic proteins.

111 andscapes of nucleation of the two different fibrils derived from patients with Pick's and Alzheimer'

112 in average collagen interfibrillar spacing, fibril diameter, D-periodicity or intermolecular spacing

113 his cross-seeding was unidirectional, as RPT fibrils did not influence alpha-syn aggregation.

114 Raman spectroscopy, limited-proteolysis, and fibril disaggregation experiments, suggesting the fibril

115 sociate alphaSyn aggregates, suggesting that fibril disassembly is linked to the increased rate of pe

116 of the protonation state of this residue in fibril disassembly, among other environmental changes.

117 ependent mechanisms of amyloid formation and fibril dissolution.

118 Remarkably, fibrils dissolve at low temperatures (2 to 6 degrees C)

119 tructurally similar to ex vivo human amyloid fibrils does not necessarily establish that the fibrillo

120 rphologically distinct from the well-ordered fibrils dominating at the end of the aggregation process

121 ctions between the monomeric species and the fibrils during this key process, and indeed the ultrastr

122 parameter-free, comprehensive description of fibril elongation of Abeta(16-22) and how it is modulate

123 and then proceeds via primary nucleation and fibril elongation processes.

124 e fingerprints of order found in the amyloid fibrils encoded in the conformations that the monomers a

125 This is especially reflected in a decreased fibril-end elongation rate.

126 Our results demonstrate that all Tau isoform fibrils exhibit paired-helical-filament-like structures

127 The cross-seeded fibrils exhibited alpha-syn-like ultrastructural feature

128 At all-time points, females injected with fibrils exhibited reduced odor detection sensitivity, wh

129 treated with human alpha-synuclein preformed fibrils, exosomes containing alpha-synuclein released by

130 cally and morphologically similar to natural fibrils extracted from human amyloidotic tissue.

131 inhibits seeding of Abeta catalyzed by Abeta fibrils extracted from the brain of an Alzheimer's patie

132 ding by both sHSPs and for mediating lateral fibril-fibril association, which sequesters preformed fi

133 nder conditions which would normally lead to fibril formation and found that the degree of tetramer s

134 as HW-155, were effective inhibitors of the fibril formation by hIAPP(.)

135 ermolecular disulfide bonds initiate amyloid fibril formation by recruitment of monomers.

136 Here we propose that fibril formation by these amyloidogenic molecules reflec

137 a(3) or genetic loss of GPVI reduced amyloid fibril formation in cultured platelets and decreased the

138 (RPT), an amyloidogenic domain essential for fibril formation in melanosomes.

139 Amyloid fibril formation is central to the etiology of a wide ra

140 n of compounds capable of inhibiting amyloid-fibril formation is critical to the development of poten

141 ary structure during pH- and heparin-induced fibril formation of apolipoprotein A-I (apoA-I) associat

142 iseases, detection and inhibition of amyloid fibril formation using FPs can provide insights on devel

143 The free energies for fibril formation were -12.36, -8.10, and -10.61 kcal mol

144 eptides are only transiently redirected from fibril formation, and eventually almost all Abeta monome

145 t a likely contributor to early oligomer and fibril formation, and thus a potential critical mechanis

146 recapitulating the entire process of amyloid fibril formation, beginning with thousands of free monom

147 stabilize specific oligomers during amyloid fibril formation, facilitating the structural characteri

148 process of LB formation, rather than simply fibril formation, is one of the major drivers of neurode

149 s susceptible to biophysical aggregation and fibril formation, promoted by manual agitation and eleva

150 protein primary sequence trigger cross-beta fibril formation, with insights that have direct implica

151 fic, as the reversed reaction inhibited sRPT fibril formation.

152 in an isolated V(L) domain is essential for fibril formation.

153 ucine to valine mutation, is responsible for fibril formation.

154 is widely used as a model system for amyloid fibril formation.

155 ed molecular chaperones that inhibit amyloid fibril formation; however, their mechanisms of action re

156 l protein from patient FOR005, together with fibrils formed by protein sequence variants that are der

157 gh-resolution molecular structural model for fibrils formed by the C-terminal half of the FUS LC doma

158 f Michler's hydrol blue (MHB) to investigate fibrils formed by the weak and strong prion fibrils of S

159 A+pH) We then measured the solubilization of fibrils formed from different FapC variants with varying

160 monstrate that FPs specifically bind amyloid fibrils formed from many natural peptides and proteins.

161 ivity, consistent with our recently reported fibril-fragmenting activity.

162 e and consequently lowered the height of the fibrils from 8.0 nm (after 1 h) to 6.0 nm (after 24 h),

163 Fibrils from the GL protein and from the patient protein

164 rmation, and we confirmed that extracellular fibrils from these biofilms contain Aap.

165 natural transthyretin fibrils with those of fibrils generated in vitro either using the common acidi

166 tural comparison between ex vivo fibrils and fibrils generated in vitro Our finding that fibrils crea

167 The fibrils generated via plasmin cleavage were more stable

168 r residues, both along and transverse to the fibril growth direction, including diverse sidechain-to-

169 of productive and nonproductive pathways of fibril growth.

170 t to construct Markov State Models (MSMs) of fibril growth.

171 ral differences, self- and cross-seeded lRPT fibrils had a similar beta-sheet structured core, reveal

172 ing KFM and FLiM, that R5P-glycated collagen fibrils have a more negative surface charge than unglyca

173 table assemblies, including so-called labile fibrils, hydrogels, and pathological amyloids.

174 e report here that alpha-synuclein preformed fibrils impaired autophagy flux by upregulating PELI1, w

175 n beta2-microglobulin (beta2m) forms amyloid fibrils in a condition known as dialysis-related amyloid

176 syn misfolding and propagation of pathologic fibrils in a prion-like process.

177 semble abnormal and dysfunctional FNDeltaRGD fibrils in a syndecan-dependent manner.

178 Lastly, inoculation of alpha-Syn fibrils in aged mice, but not younger mice, resulted in

179 cal morphology of unfixed, hydrated collagen fibrils in native tendon with a 0.1 nm depth resolution

180 ons of current tools to size and count Abeta fibrils in real time.

181 ide/lipid coaggregates that resemble amyloid fibrils in some important ways but are a distinct specie

182 position of amyloid beta (Abeta) plaques and fibrils in the brain parenchyma is a hallmark of Alzheim

183 Fibrils in the inner and outer regions of the ZP are ori

184 leic acid-containing (NA-containing) amyloid fibrils in the periphery.

185 hanical properties among individual collagen fibrils in their adhesive and in their repulsive, viscoe

186 dent human chaperone system disassembles Tau fibrils in vitro We found that this function is mediated

187 y dementia, and E46K creates more pathogenic fibrils in vitro.

188 ity to bind alpha-synuclein and amyloid beta fibrils in vitro.

189 (PD)-associated alpha-synuclein (alpha-syn) fibrils, in part, due to lack of information of the stru

190 are dominated by only a few residues in the fibrils, including hydrophobic pai-pai interactions with

191 onship between the structures of polymorphic fibrils, including their PTMs, and neurodegenerative dis

192 ata are consistent with degradation of Abeta fibril induced by EGCG and inhibition of Abeta fibril an

193 dence that peripheral injection of alpha-syn fibrils induces unique patterns of functional and struct

194 Here, we show for two fibril inhibiting ligands, an ionic molecular tweezer an

195 The protofibril-fibril interaction governs their temporal evolution and

196 12-17 segment of insulin that forms amyloid fibrils (intermolecularly hydrogen-bonded beta-sheets) w

197 erior of senile plaques, yet the protofibril-fibril interplay is not well understood.

198 d, HSA remodels alphaS oligomers and high-MW fibrils into chimeric intermediates with reduced toxicit

199 bril association, which sequesters preformed fibrils into large aggregates and is believed to have a

200 laterally injected alpha-synuclein preformed fibrils into the olfactory bulbs of wild type male and f

201 The mineralized collagen fibril is the basic building block of bone, and is commo

202 Formation of polymorphic amyloid fibrils is a common feature in neurodegenerative disease

203 al information on classical alphaSyn amyloid fibrils is available, little is known about the conforma

204 operties closely similar to those of natural fibrils is central to improving our understanding of the

205 robust morphology of self-assembled collagen fibrils is currently almost completely missing.

206 protein into highly ordered beta-sheet-rich fibrils is implicated in the pathogenesis of a range of

207 Glycation of collagen fibrils is known to impact on cell adhesion and migratio

208 hatase and has been reported to form amyloid fibrils, known as semen-derived enhancer of viral infect

209 but a few run obliquely within the collagen fibril layer for many micrometers before exiting.

210 mall fenestrae in the sub-epidermal collagen fibril layer; most nerves exit abruptly, but a few run o

211 , the addition of CypD to preformed alphaSyn fibrils leads to the disassembly of these fibrils.

212 ures of MG2a and PGLa formed surface-aligned fibril-like structures, which induced adhesion zones bet

213 terminant of a compartment composed of novel fibril-like substructures, which we identify here by thr

214 periments, were very low compared to amyloid fibrils made of other proteins.

215 erent backbone conformations within the same fibril may explain the increased aggregation propensity

216 These fibrils may induce further alphasyn misfolding and propa

217 om polylactic acid (PLA) and micro cellulose fibrils (MCF).

218 molecules into amyloid fibrils and alter the fibril morphologies, yet the molecular mechanisms throug

219 lting in propagation of an sRPT-like twisted fibril morphology, unlike the rodlike structure that lRP

220 Even though all mature amyloid fibrils must originate as oligomers, we found that most

221 rystallin are important for delaying amyloid fibril nucleation and for disaggregating mature apolipop

222 ee-dimensional (3D) structure of the amyloid fibril of the human hormone beta-endorphin was determine

223 Amyloid fibrils of beta-parvalbumin, a protein abundant in fish,

224 fer can decipher the architecture of amyloid fibrils of human alpha-synuclein.

225 fibrils formed by the weak and strong prion fibrils of Sup35NM and find that MHB differentiates betw

226 pe images shows that the formation of mature fibrils of VEALYL correlates with the appearance of sphe

227 irpin structure induced formation of amyloid fibrils on the surface of the droplets.

228 hat form either along the pathway to forming fibrils or in competition with their formation, making i

229 teraction mechanisms, the suppression of the fibril pathway can be deduced from the disappearance of

230 We have investigated if preformed alpha-syn fibrils (PFFs) impair GCase activity in mouse cortical n

231 /-) mice, inoculation of alpha-Syn preformed fibrils (PFFs) into the stellate and celiac ganglia indu

232 docytosis regulators for alpha-Syn preformed fibrils (PFFs).

233 t the secondary structure is similar in both fibril polymorphs.

234 P1 interacting with water-insoluble collagen fibrils poses challenges for biochemical studies that th

235 bose-5-phosphate (R5P) glycation of collagen fibrils - potentially important in the microenvironment

236 econdary nucleation as the main mechanism of fibril proliferation.

237 nt light chain fragment corresponding to the fibril protein from patient FOR005, together with fibril

238 llular prion protein (PrP(C)) into cytotoxic fibrils (PrP(Sc)).

239 structures were seeded with ex-vivo amyloid fibrils purified from the explanted heart of this patien

240 neurodegenerative diseases, including neural fibrils, reactive oxygen species, and cofilin-actin rods

241 etectable within grafts and lacked anchoring fibril reconstitution.

242 hat have the propensity to form amyloid-like fibrils reminiscent of those in neurodegenerative diseas

243 r to ensemble-type measurements but with per-fibril resolution.

244 tural elucidation of ex vivo Drosophila Orb2 fibrils revealed a novel amyloid formed by interdigitate

245 Both oligomers and fibrils seed the spread of Tau pathology, and by virtue

246 h binding affinities of 0.5 muM to alpha-syn fibril seeds.

247 al treatment, and decoupling hydrolysis from fibril self-assembly helped to identify the building blo

248 noindentation, we found that type I collagen fibrils show a pronounced nonlinear behavior in the form

249 The fibrils show a remarkable resemblance to amyloid beta (A

250 Seeded R49G fibrils show an increased heterogeneity in the C-termina

251 At the same time, agitated Abeta42 fibrils show stronger interactions between spin labels a

252 EPR studies of these two types of Abeta42 fibrils show that the secondary structure is similar in

253 energy transfer analyses revealed that these fibrils showed low cytotoxicity and affinity to plasma m

254 half B-repeats (Brpt5.5) forms amyloid-like fibrils similar to those observed in the biofilm.

255 al disengagement and the subsequent onset of fibril sliding is one of the key mechanisms leading to f

256 onged incubation periods and greater PrP(Sc) fibril stability compared to mice challenged with MM132

257 n used to detect morphological variations in fibril states of aggregated peptides and proteins.

258 -seeding experiments, we show that alpha-syn fibrils stimulate the aggregation of a Pmel17 fragment c

259 strength (i.e. ultimate stress), whilst peak fibril strain occurred afterwards (i.e. higher tissue st

260 ear evidence that the propagation of amyloid fibril strains is possible even in systems dominated by

261 logic milieu is a key determinant of amyloid fibril strains.

262 Using MAS solid-state NMR, we studied the fibril structure of a recombinant light chain fragment c

263 hat the replacement fundamentally alters the fibril structure to a more stable energetic state.

264 The wild-type fibril structure, solved to 3.6- angstrom resolution, co

265 arently unlocks a more stable and pathogenic fibril structure.

266 ridge to aspartate-25 in the patient protein fibril structure.

267 ) states, which resemble the monomers in the fibril structure.

268 atient mutations in FOR005 can stabilize the fibril structure.

269 In Alzheimer's disease, different fibril structures may be associated with different clini

270 topological classes encompassing all amyloid fibril structures so far discovered in the PDB.

271 Both analyzed fibril structures were seeded with ex-vivo amyloid fibri

272 essible and thermodynamically stable amyloid fibril structures.

273 strategy can be used on full-length cryo-EM fibril structures.

274 nd solid-state NMR studies reveal changes in fibril surface characteristics and flanking domain mobil

275 ssibility of cell adhesion sites and altered fibril surface charge on the integrity of the extracellu

276 ty has to be mediated by interactions of the fibril surface with its cellular environment, we wanted

277 nucleation with structural conversion at the fibril surface.

278 yloid fibrils by secondary nucleation on the fibril surface.

279 Fibril-surface-mediated branching, previously attributed

280 The in vitro preparation of amyloid fibrils that exhibit structural and biochemical properti

281 an antiparallel beta-sheet to propagate into fibrils that have a parallel-beta-sheet secondary struct

282 ggregation of cellular peptides into amyloid fibrils that may be due, in part, to VZV gB peptides.

283 Complete removal of all repeats led to fibrils that were solubilized at FA concentrations 2-3 o

284 a recent study, Hervas et al. extracted Orb2 fibrils, that are involved in long-term memory formation

285 flexibility for the adhesive tip of the CshA fibril to maintain bacterial attachment that withstands

286 r content, allowing the assembly of collagen fibrils to be imaged in high resolution beneath an appro

287 Because potential fibril toxicity has to be mediated by interactions of th

288 omes isolated from alpha-synuclein preformed fibrils treated microglia into the mouse striatum.

289 l disaggregation experiments, suggesting the fibril twist is modulated by N-terminal residues outside

290 The landscapes for nucleating both fibril types contain amorphous oligomers leading to bran

291 condary nucleation occurs along the sides of fibrils, which become heavily decorated under the curren

292 orms physiological granules and pathological fibrils, which facilitate RNA functions and cause neurod

293 turation and directly leads to canonical tau fibrils, while LLPS-ED is reversible, remains hydrated a

294 The biological fibrils with invertase activity turn into microstructure

295 o pathologically misfold into uniquely toxic fibrils with modulated prion-like seeding activity.

296 albumin dimers readily assemble into amyloid fibrils with similar morphology as those formed when sta

297 modynamic stability of natural transthyretin fibrils with those of fibrils generated in vitro either

298 d, peptide hormones can be stored as amyloid fibrils within acidic secretory granules before release

299 We show that FVIII forms amyloid-like fibrils within the ER lumen upon increased FVIII synthes

300 ic pH but, on exocytosis, the beta-endorphin fibril would encounter neutral pH conditions (pH 7.4) in