ライフサイエンスコーパス: microfibril

1 alyses pointing toward an 18-chain cellulose microfibril.

2 rdered lattice constituting the core of each microfibril.

3 of type-I collagen within the context of the microfibril.

4 cular weight component of the fibrillin-rich microfibril.

5 n the culture medium and no association with microfibrils.

6 of obstacles, like disintegration of chitin microfibrils.

7 extracellular matrix protein associated with microfibrils.

8 the hemicelluloses that tether to cellulose microfibrils.

9 AGP1) is a component of extracellular matrix microfibrils.

10 ng assays, rVN bound to isolated nondegraded microfibrils.

11 les and the orientation of nascent cellulose microfibrils.

12 g of (1-->4)-beta-glucan chains in cellulose microfibrils.

13 al interactions to enhance HA recruitment to microfibrils.

14 lin-1, the main constituent of extracellular microfibrils.

15 ically in mediating the recruitment of HA to microfibrils.

16 tories to orient newly synthesized cellulose microfibrils.

17 in limited regions of tight contact between microfibrils.

18 celluloses via binding to emerging cellulose microfibrils.

19 come into direct contact with the cellulose microfibrils.

20 egulate the fibrillin isoform composition of microfibrils.

21 tion of mutant fibrillin-1 incorporated into microfibrils.

22 lice variant was able to assemble into short microfibrils.

23 is a ubiquitous component of fibrillin-rich microfibrils.

24 thick fibrils and spots with densely packed microfibrils.

25 ll adhesion and as a structural component of microfibrils.

26 these proteins have been immunolocalized to microfibrils.

27 atial scale of molecular connections between microfibrils.

28 LTBP-1 and LTBP-4 are not incorporated into microfibrils.

29 -1, LTBP-1, and LTBP-4 are incorporated into microfibrils.

30 bserve alterations in the lateral packing of microfibrils.

31 ofibril that interdigitates with neighboring microfibrils.

32 olecule to align and to form well-structured microfibrils.

33 accumulates in the narrow spaces between the microfibrils.

34 be visualized in the context of the stiffer microfibrils.

35 ndle individual glucan chains into cellulose microfibrils.

36 ellulosic polysaccharide, binds to cellulose microfibrils.

37 iate the adsorption of mucilage to cellulose microfibrils.

38 r xylan to the hydrophilic face of cellulose microfibrils.

39 rs, which are then secreted and assembled to microfibrils.

40 motetramers that are incorporated into mixed microfibrils.

41 ond to the hydrophilic surfaces of cellulose microfibrils.

42 zed the assembly of these into tetramers and microfibrils.

43 le, by partially dissolving silk fibers into microfibrils.

44 bule (CMT)-mediated orientation of cellulose microfibrils.

45 of certain matrix polymers within cellulose microfibrils.

46 he pectin backbone, lodged between cellulose microfibrils.

47 es containing LTBP-3 with mutant fibrillin-1 microfibrils.

48 f the 10-12 nm diameter extracellular matrix microfibrils.

49 lan onto the hydrophilic face of a cellulose microfibril (1-3) .

50 on three different models of Ibeta cellulose microfibrils, 18, 24, and 36 chains, to investigate thei

51 thickening and the orientation of cellulose microfibrils [2], our understanding of the composition o

52 ose polymer cellulose is assembled into long microfibrils a few nanometers in diameter.

53 lulose chains bridging continuously from one microfibril aggregate (macrofibril) to the next provide

54 from midribs were consistent with cellulose microfibril aggregation, and polarization microscopy rev

55 lastin, and proteins associated with elastic microfibrils, albeit miR-29b showed a stronger effect, p

56 re, including a slight increase in cellulose microfibril alignment along the growing stem.

57 ulose SFG spectrum is sensitive to cellulose microfibril alignment and packing within the cell wall.

58 d eight molecules in cross-section through a microfibril, allowing us to understand microfibril organ

59 cifically surrounded by abundant collagen VI microfibrils, an outcome accentuated by Down syndrome.

60 tween a hydrophobic surface of the cellulose microfibril and an aromatic motif on the expansin surfac

61 xes, which is a key determinate of cellulose microfibril and cell wall properties.

62 ment increased intracutaneous fibrillin-rich microfibril and collagen III deposition and decreased ma

63 d in vertebrates and have important roles in microfibril and elastic fiber structure, homeostasis, an

64 nterestingly, jia1 results in both cellulose microfibril and microtubule disorganization.

65 d by walls composed of crystalline cellulose microfibrils and a variety of matrix polymers.

66 Improved understanding of how fibrillin microfibrils and associated proteins regulated TGF-beta

67 fibrillin-2 epitopes are masked in postnatal microfibrils and can be revealed by enzymatic digestion

68 creating a dense matrix that binds cellulose microfibrils and crosslinks other wall components, there

69 Thus, alteration of MAGP-2, a component of microfibrils and elastic fibers, appears as an initiatin

70 e are deficient in extracellular collagen VI microfibrils and exhibit myopathic features, including d

71 establishing interactions between cellulose microfibrils and hemicelluloses.

72 beta-1,4-glucan chains that coalesce to form microfibrils and higher-ordered macrofibrils.

73 for KOR1 both in the synthesis of cellulose microfibrils and in the intracellular trafficking of CSC

74 , xyloglucan is thought to connect cellulose microfibrils and regulate their separation during wall e

75 polymers form an inner core within postnatal microfibrils and that microfibril structure evolves as g

76 length or quantity of a subset of cellulose microfibrils and that this, in turn, alters microfibril

77 s made between the interaction of individual microfibrils and the change in their suprafibrillar cohe

78 ) C2a chain do not assemble efficiently into microfibrils and there is a severe collagen VI deficienc

79 rVN enhanced HA recruitment both to isolated microfibrils and to microfibrils in tissue sections in a

80 , our data identify MFAP4 as a new ligand of microfibrils and tropoelastin involved in proper elastic

81 ggest that Chs8p synthesizes the long-chitin microfibrils, and Chs3p synthesizes the short-chitin rod

82 association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers.

83 e ECM collagen into triple-helical monomers, microfibrils, and macrofibrils, little or no inhibition

84 n that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions i

85 omain can be cleaved off after assembly into microfibrils, and the cleavage product has been implicat

86 es in individual polymer chains of cellulose microfibrils, and typically exhibit specificity for eith

87 l associations with wood density, stiffness, microfibril angle and ring width in a population of 1694

88 c gravity, percentage of latewood, earlywood microfibril angle, and wood chemistry (lignin and cellul

89 between the gene PgNAC8, wood stiffness and microfibril angle, as well as considerable within-season

90 possible role for Ca(2+) in stabilizing the microfibril architecture and moderating extension in viv

91 Fibrillin microfibrils are 10-12 nm diameter, extracellular matrix

92 ctron microscopy demonstrated that cellulose microfibrils are oriented in near longitudinal orientati

93 imary wall microfibril structure because its microfibrils are oriented with unusual uniformity, facil

94 Cellulose microfibrils are para-crystalline arrays of several doze

95 Fibrillin microfibrils are polymeric structures present in connect

96 Cellulose microfibrils are synthesized at the plasma membrane, whe

97 Plant cellulose microfibrils are synthesized by a process that propels t

98 Fibrillin-rich microfibrils are the major structural components of the

99 mplex that synthesizes an 18-chain cellulose microfibril as its fundamental product.

100 r, these findings identify the extracellular microfibrils as critical regulators of bone formation th

101 brillin strengthens the concept of fibrillin microfibrils as extracellular scaffolds integrating cell

102 Fibrillin-1 microfibril assembly and secreted lysyl oxidase activity

103 At present the mechanisms that regulate microfibril assembly are still to be elucidated.

104 there were differences in the secretion and microfibril assembly profiles of fibrillin-1 variants co

105 site at the C terminus to prevent premature microfibril assembly.

106 t the first hybrid domain is dispensable for microfibril assembly.

107 Microfibril-associated glycoprotein (MAGP) 1 and 2 are e

108 Microfibril-associated glycoprotein 1 (MAGP1) is a compo

109 Microfibril-associated glycoprotein-1 (MAGP-1) is a smal

110 sualized using antibodies to Fbn1, Fbn2, and microfibril-associated glycoprotein-1 (Magp1) in conjunc

111 The microfibril-associated glycoproteins (MAGPs) are cystein

112 illar proteins mainly include fibrillins and microfibril-associated glycoproteins (MAGPs).

113 ers caused by mutations in fibrillins and in microfibril-associated molecules.

114 racterization of the Drosophila homologue of microfibril-associated protein 1 (dMFAP1), a previously

115 n microscopy, which revealed localization to microfibrils at the microscopic level.

116 ely our data demonstrated that extracellular microfibrils balance local catabolic and anabolic signal

117 alytic domain (CD) of Cel7B with a cellulose microfibril before and after complexing a glucan chain i

118 ndings suggest that ADAMTS10 participates in microfibril biogenesis rather than in fibrillin-1 turnov

119 ate, and the role of ADAMTS10 in influencing microfibril biogenesis was addressed.

120 otein which has been implicated in fibrillin microfibril biogenesis, cause ectopia lentis (EL) and EL

121 To investigate the role of ADAMTS10 in microfibril biogenesis, fetal bovine nuchal ligament cel

122 dded ADAMTS10 led to accelerated fibrillin-1 microfibril biogenesis.

123 syndrome (WMS), implicating it in fibrillin microfibril biology since some fibrillin-1 mutations als

124 so known as Magp2), which encodes an elastin-microfibril bridging factor, is upregulated in Fgfr3;4 m

125 an essential component for the formation of microfibril bundles in ciliary zonules.

126 brils merge into and out of short regions of microfibril bundles, thereby forming a reticulated netwo

127 e, and has similar rigidity to the cellulose microfibrils, but reverts to the threefold screw conform

128 g the 20- to 40-nm spacing between cellulose microfibrils, but they do implicate a minor xyloglucan c

129 he AFM thus preferentially detects cellulose microfibrils by probing through the soft matrix in these

130 that fibrillin-1, which forms extracellular microfibrils, can regulate the bioavailability of transf

131 major structural components of extracellular microfibrils, cause pleiotropic manifestations in Marfan

132 icellulose (HC) tethering with the cellulose microfibrils (CMFs) as one of the major load-bearing mec

133 coupling networks in Cel7B-glucan and Cel7B-microfibril complexes reveal a previously unresolved all

134 that mediates the synthesis of a fundamental microfibril composed of 18 glucan chains.

135 Our results show that wall loosening alters microfibril connectivity, enabling microfibril dynamics

136 The cellulose microfibril consists of bundles of linear beta-1,4-gluca

137 e-digested microfibrils, guanidine-extracted microfibrils contained all fibrillin-1 epitopes recogniz

138 n of how many chains an elementary cellulose microfibril contains is critical to understanding the mo

139 The rigidity and orientation of these microfibrils control cell expansion; therefore, cellulos

140 ll stability of the crystalline structure of microfibrils could facilitate the design of more effecti

141 Consistent with measurements of lower microfibril crystallinity, cellulose extracts from mutat

142 2 immunoreactivity can serve as a marker for microfibril degradation.

143 rid domain) in fibrillin-1 results in stable microfibrils, demonstrating that fibrillin-1 molecules a

144 ntact or defective surface structures on the microfibril, depending on the complexation state.

145 We previously showed that microfibril deposition requires fibronectin-induced foca

146 epithelial cell-cell junction formation, and microfibril deposition.

147 Elastic tissues rich in MAGP-1-containing microfibrils develop normally and show normal function.

148 , the structural components of extracellular microfibrils, differentially regulate TGF-beta and bone

149 Microfibril direction within a lamella did not change gr

150 -ray diffraction, we show that the cellulose microfibrils displayed reduced width and an additional c

151 are often considered as spacers of cellulose microfibrils during growth.

152 ng alters microfibril connectivity, enabling microfibril dynamics not seen during mechanical stretch.

153 The cell wall consists of cellulose microfibrils embedded within a matrix of hemicellulose a

154 Microfibrils, enriched in Fbn2 and Magp1, were prominent

155 In conclusion, when microfibrils extend, there is a large molecular rearrang

156 Fibrillin microfibrils form the ocular zonule and are present in t

157 , linkage analysis, and imaging of cellulose microfibril formation using transmission electron micros

158 ifference in glucan chain association during microfibril formation.

159 ESA) glycosyltransferases mediates cellulose microfibril formation.

160 ng estimates of the diameter of the smallest microfibril formed from the beta-1,4 glucan chains synth

161 rculating fragments of fibrillin-1, or other microfibril fragments, are associated with TAA and disse

162 diffraction study of hydrated fibrillin-rich microfibrils from zonular filaments has been conducted t

163 y walls of grasses are composed of cellulose microfibrils, glucuronoarabinoxylans, and mixed-linkage

164 In contrast to collagenase-digested microfibrils, guanidine-extracted microfibrils contained

165 pe II arabinogalactans retained by cellulose microfibrils had a higher content of (methyl)glucuronic

166 plex and the number of cellulose chains in a microfibril have been debated for many years.

167 Fibrillin microfibrils have essential roles in elastic fiber forma

168 15), nanometre-scale movements of individual microfibrils have not been directly observed.

169 hat control the interactions among cellulose microfibrils, hemicelluloses, and lignin are still not w

170 x-ray diffraction structure of the collagen microfibril in situ, indicating the existence of domains

171 It colocalizes to fibrillin-1 containing microfibrils in cultured fibroblasts and suppresses fibr

172 scopy visualized ultrastructurally different microfibrils in Fbn1 null compared with control cell cul

173 Disruption of microfibrils in fibrillin-1-deficient mice leads to frag

174 localized ADAMTS10 to fibrillin-1-containing microfibrils in human tissues.

175 e an insight into the molecular structure of microfibrils in intact tissue.

176 c lamellae and also display fragmentation of microfibrils in other tissues.

177 py is sensitive to the ordering of cellulose microfibrils in plant cell walls at the meso scale (nm t

178 in vitro evidence excludes a direct role of microfibrils in supporting mineral deposition.

179 wall polymers that are retained by cellulose microfibrils in tension wood and normal wood of hybrid a

180 ell wall; and a network of longer interlaced microfibrils in the bud scars and primary septa.

181 riented deposition of load-bearing cellulose microfibrils in the cell wall.

182 screw ribbon to bind intimately to cellulose microfibrils in the cell wall.

183 ADAMTSL4 colocalized with fibrillin-1 microfibrils in the ECM of these cells.

184 have significant interactions with cellulose microfibrils in the native primary wall.

185 iable, but still small, surface of cellulose microfibrils in the onion wall is tightly bound with ext

186 ed to function as a tether between cellulose microfibrils in the primary cell wall, limiting cell enl

187 at EMILIN-1 and -2 are targeted to fibrillin microfibrils in the skin.

188 A role for fibrillin microfibrils in tissue elasticity has been implied by th

189 uitment both to isolated microfibrils and to microfibrils in tissue sections in a dose-dependent mann

190 me, demonstrating a critical requirement for microfibrils in vessel structure and function.

191 ppresses fibrillin-2 (FBN2) incorporation in microfibrils, in part by transcriptional downregulation

192 he least characterized member of the elastin microfibril interface-located protein (EMILIN)/Multimeri

193 to interact with an intracellular domain of microfibril interface-located protein 1 (EMILIN 1), a me

194 Elastin microfibril interface-located proteins (EMILINs) 1 and 2

195 cellulose microfibril surfaces and to tether microfibrils into a load-bearing network, thereby playin

196 fibrillar networks with focal aggregation of microfibrils into PEX-like fibrils on stimulation with T

197 ential physical interactions that stabilizes microfibrils is a network of hydrogen (H) bonds: both in

198 reinforcement of the wall by stiff cellulose microfibrils is central to contemporary models of plant

199 Synthesis of 18-chain microfibrils is consistent with a model for cellulose-sy

200 osition of aggregated and helically oriented microfibrils is coupled to rapid and highly localized ce

201 The interaction between xylan and cellulose microfibrils is important for secondary cell wall proper

202 The crystalline nature of cellulose microfibrils is one of the key factors influencing bioma

203 Assembly of fibrillin monomers into microfibrils is thought to occur at the cell surface, wi

204 as predigested with xyloglucanase, whereupon microfibril labelling was extensive.

205 llulose synthase complex rosette synthesizes microfibrils likely comprised of either 18 or 24 chains.

206 lecular assembly of VG1Fs in the HA-versican-microfibril macrocomplex has not yet been elucidated.

207 ing that it may be an important modulator of microfibril-mediated growth factor signaling.

208 ly deposited wall surface showed that single microfibrils merge into and out of short regions of micr

209 ells by siRNA disrupted the formation of the microfibril meshwork by the cells.

210 TBP-2 in culture medium not only rescued the microfibril meshwork formation in LTBP2-suppressed cilia

211 , and studies suggesting that alterations in microfibrils might contribute to human SSc.

212 illin molecules are highly folded within the microfibrils; more importantly, the connection is made b

213 its near-native state, with implications for microfibrils motions in different lamellae during uniaxi

214 These insights into microfibril movements and connectivities need to be inco

215 Microfibril movements during forced mechanical extension

216 ntation, we observed a diverse repertoire of microfibril movements that reveal the spatial scale of m

217 These data implicate the fibrillin microfibril network in the extracellular control of BMP

218 inding proteins fibrillins are components of microfibril networks, and both interact with members of

219 lanases capable of degrading the crystalline microfibrils of 1,3-xylan that reinforce the cell walls

220 is the efficient degradation of crystalline microfibrils of cellulose to glucose.

221 ly divergent proteins that are components of microfibrils of the extracellular matrix.

222 fibronectin and accumulation of fibronectin microfibrils on the cell surface.

223 nase-digested cell walls revealed an altered microfibril organization but did not yield clear evidenc

224 ndary cell walls, but their biosynthesis and microfibril organization have not been examined.

225 ucanase in cellulose synthesis and cellulose microfibril organization in plants.

226 ugh a microfibril, allowing us to understand microfibril organization in three dimensions.

227 layers characterized by transverse cellulose microfibril orientation in both normal and compression w

228 and polarization microscopy revealed helical microfibril orientation only in wild type leaves.

229 wood cell walls, including lignification and microfibril orientation, may be mediated by changes in t

230 lationships with lignification and cellulose microfibril orientation.

231 0 nm thick, containing 3.5-nm wide cellulose microfibrils oriented in a common direction within a lam

232 rounded by a rigid wall made up of cellulose microfibrils, pectins, hemicelluloses, and lignin.

233 In this study, we found that microfibril periodicity and structure are dependent on t

234 cused on how fibrillin-1 is organized within microfibril polymers.

235 tide blocks the assembly of fibrillin-1 into microfibrils produced by dermal fibroblasts; and (iii) t

236 Although passive microfibril reorientation during wall extension has been

237 N1 (encoding fibrillin-1, which forms tissue microfibrils), respectively, yet they are clinically ind

238 ghosts revealed two distinct forms of chitin microfibrils: short microcrystalline rodlets that compri

239 First, we develop a nematic silk microfibril solution, highly viscous and stable, by part

240 ations with hemicelluloses are important for microfibril spacing and for maintaining cell wall tensil

241 ith ADAMTS10 mutations deposited fibrillin-1 microfibrils sparsely compared with unaffected control c

242 II arabinogalactan are trapped by cellulose microfibrils specifically in tension wood and, thus, are

243 throughout development, and is essential for microfibril structural integrity.

244 e not required to be in perfect register for microfibril structure and function and that the first hy

245 A central question concerns the mechanism of microfibril structure and how this is linked to the cata

246 l model system for the study of primary wall microfibril structure because its microfibrils are orien

247 ns unclear whether modification of cellulose microfibril structure can be achieved genetically, which

248 core within postnatal microfibrils and that microfibril structure evolves as growth and development

249 CESA1(A903V) and CESA3(T942I) have modified microfibril structure in terms of crystallinity and sugg

250 microfibrils and that this, in turn, alters microfibril structure in the primary cell wall resulting

251 However, knowledge of microfibril structure is limited, largely due to their i

252 , these results suggest that perturbation of microfibril structure may underlie one of the major feat

253 er, while organization of the CSC determines microfibril structure, how individual CESA proteins are

254 1 cause disorders through primary effects on microfibril structure, two different mutations were gene

255 termine the role of fibrillin-2 in postnatal microfibril structure.

256 omplexity and tissue-specific differences in microfibril structure.

257 ypothesized to bind extensively to cellulose microfibril surfaces and to tether microfibrils into a l

258 The inferred site of chitin microfibril synthesis of these Chs enzymes was corrobora

259 and -5, are components of the elastic fiber/microfibril system and are implicated in the formation a

260 commonly depicted as a scaffold of cellulose microfibrils tethered by xyloglucans.

261 a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfi

262 extracellular glycoprotein fibrillin-1 forms microfibrils that act as the template for elastic fibers

263 omposite material containing stiff cellulose microfibrils that are embedded within a pectin matrix an

264 hains polymerized by CesA are assembled into microfibrils that are frequently bundled into macrofibri

265 ry elements and fibers are rich in cellulose microfibrils that are helically oriented and laterally a

266 glucan chains assembled into paracrystalline microfibrils that are synthesized by plasma membrane-loc

267 These chains form the microfibrils that confer the remarkable structural prope

268 reflection of helicoidally stacked cellulose microfibrils that form multilayers in the cell walls of

269 ted of a dense meshwork of radially oriented microfibrils that we termed the fibrillar girdle.

270 large matrix polymers retained by cellulose microfibrils that were specifically found in tension woo

271 By releasing LLC from microfibrils, the fibrillin-1 sequence encoded by exons

272 on the orientation of crystalline cellulose microfibrils, their bonding to the polysaccharide matrix

273 s synthesize elastin and other components of microfibrils; these may serve structural roles, providin

274 ween the rosette structure and the cellulose microfibrils they synthesize.

275 pose that cleaved VG1Fs can be recaptured by microfibrils through VG1F homotypical interactions to en

276 ily of genes responsible for the assembly of microfibrils throughout development, and is essential fo

277 ration; we then used these properties of the microfibril to trap conformation intermediates.

278 The importance of fibrillin microfibrils to connective tissue function has been demo

279 h was used to circumvent the insolubility of microfibrils to determine the role of fibrillin-2 in pos

280 of steps involved in the digestion of Abeta microfibrils to nanospheres or nanofilaments by protease

281 ll enlargement by restricting the ability of microfibrils to separate laterally.

282 ficiently "glued" the structural elements of microfibrils together, producing a unique inorganic-orga

283 the closed state, indicating that cellulose microfibrils undergo dynamic reorganization during stoma

284 age thickness and RMS roughness of cellulose microfibrils upon exposure to cellulolytic enzymes, prov

285 ich cell wall matrix embedded with cellulose microfibrils, we show that strong, circumferentially ori

286 pectroscopy, we show that celery collenchyma microfibrils were 2.9 to 3.0 nm in mean diameter, with a

287 ctron microscopy showed that the long-chitin microfibrils were absent in chs8 mutants and the short-c

288 Interestingly, cellulose microfibrils were disordered only in the epidermal cells

289 There was evidence that adjacent microfibrils were noncovalently aggregated together over

290 Several microfibrils were observed either inside or on the outer

291 guanidine-extracted and collagenase-digested microfibrils were subjected to extensive digestion by cr

292 ll surface obscured the underlying cellulose microfibrils when imaged by FESEM, but not by AFM.

293 llin-1 from being secreted or assembled into microfibrils, whereas MFS-associated substitutions in th

294 re viable models for an elementary cellulose microfibril, which also correlates with recent scatterin

295 lulose chains attached to adjacent cellulose microfibrils, which are disrupted above a threshold leve

296 ve pectin entrapment in or between cellulose microfibrils, which cannot be mimicked by in vitro bindi

297 SL4 influences the biogenesis of fibrillin-1 microfibrils, which compose the zonule.

298 this protease or its connection to fibrillin microfibrils, whose major component, fibrillin-1, is gen

299 Transmission electron microscopy imaging of microfibrils with a range of periodicities between 56 an

300 mulated peak shapes, calculated for 36-chain microfibrils with perfect order or uncorrelated disorder

301 of cellulose chains and their assembly into microfibrils within the cell walls of land plants and th